Many common diseases, and others not as frequent, can have as a primary cause, or at least as a determinant cofactor, a defective chaperone: the abnormal chaperone is part of the pathogenic mechanism. Thus, elucidation of this mechanism will make treatment more adequate, more specific. The point is to ascertain whether in any given patient one or more molecular chaperones are involved in causing the disease. The signs and symptoms may be the same in various patients, thus leading to a standard diagnosis of a known pathological condition, distal motor neuropathy, for instance. However, some of these patients may have a chaperonopathy as part of the pathogenic mechanism whereas the others may not. This should be investigated by the clinician. A differential diagnosis exercise should be conducted to classify the patients into groups, depending on whether or not they have a chaperonopathy. It follows, that those patients that do have a chaperonopathy will be different from those that do not and will show distinctive signs and symptoms. These distinctive features must be unveiled by the physician by resorting to specific clinical and laboratory examinations.
The physician and the laboratory pathologist must be aware that there are various classes of chaperones, and that members of all these classes can be pathogenic if abnormal in structure and/or function. The specific manifestations of any given class of chaperone that is abnormal may be the same in patients which otherwise differ in signs and symptoms and, vice versa, patients with very similar signs and symptoms may differ in the class of chaperone which is abnormal. However, there are useful indicators that allow identification of chaperonopathies and of the class of chaperone that is abnormal. All this is explained in the book “The Chaperonopathies” (http://www.springer.com/biomed/book/978-94-007-4666-4) of which this Webpage is a complement. In addition, more information is available in works in the public domain; some of these resources are listed below.
A. Core references
BOOK:
Alberto J. L. Macario, Everly Conway de Macario, and Francesco Cappello. The Chaperonopathies. Diseases with defective molecular chaperones. 2013. http://dx.doi.org/10.1007/978-94-007-4667-1; ISSN 2211-9353; ISBN 978-94-007-4666-4; ISSN 2211-9361 (electronic); ISBN 978-94-007-4667-1 (eBook); DOI 10.1007/978-94-007-4667-1. Springer Dordrecht Heidelberg New York London. Library of Congress Control Number: 2013931840. http://www.springer.com/biomed/book/978-94-007-4666-4
BOOK UPDATE AUGUST 2016:
Life Safety and Security (LiSS). 4(6):101-123, 2016. DOI: 10.12882/2283-7604.2016.4.6.
https://www.iemest.eu/life-safety-and-security/images/Doc/ARTICOLI/2016/macario_24/Macario04.pdf
BOOK UPDATE APRIL 2018:
Alberto J. L. Macario, and Everly Conway de Macario, eds. (2018). Pathologic Conditions of the Human Nervous and Muscular Systems Associated with Mutant Chaperones: Molecular and Mechanistic Aspects. Lausanne: Frontiers Media. doi: 10.3389/978-2-88945-457-0. eBook 2018.
https://www.frontiersin.org/research-topics/4348/pathologic-conditions-of-the-human-nervous-and-muscular-systems-associated-with-mutant-chaperones-mo
BOOK UPDATE JANUARY 2019:
Macario AJL, Conway de Macario E. Chaperone proteins and chaperonopathies. In: Stress Physiology, Biochemistry, and Pathology. Handbook of Stress, Volume 3, Chapter 12. Pages 135-152. Edited by: George Fink. Elsevier/Academic Press, 2019.
https://doi.org/10.1016/B978-0-12-813146-6.00012-6
BOOK UPDATE OCTOBER 2019:
Macario AJL, Conway de Macario E. Molecular mechanisms in chaperonopathies: clues to understanding the histopathological abnormalities and developing novel therapies. J Pathol. 2019 Oct 3. doi: 10.1002/path.5349. J Pathol. January 2020; 250(1):9-18. PMID:31579936 https://onlinelibrary.wiley.com/doi/abs/10.1002/path.5349 https://doi.org/10.1002/path.5349
BOOK UPDATE JANUARY 2020:
Macario AJL, Conway de Macario E. Hidden chaperonopathies: alerting physicians and pathologists on the possibility that uncharacteristic, baffling clinical features in otherwise known diseases may be due to failure of the chaperoning system. Life Safety and Security (LiSS) 8.1 53 8(1):189-193, 2020
BOOK UPDATE JUNE 2021:
Macario AJL, Conway de Macario E. Chaperonins in cancer: Expression, function, and migration in extracellular vesicles. Semin Cancer Biol. 2021 Jun 1:S1044-579X(21)00159-0. doi: 10.1016/j.semcancer.2021.05.029. Online ahead of print. PMID:34087417
https://doi.org/10.1016/j.semcancer.2021.05.029 https://pubmed.ncbi.nlm.nih.gov/34087417/https://www.sciencedirect.com/science/article/abs/pii/S1044579X21001590?via%3Dihub
BOOK UPDATE JULY 2023:
Macario AJL, Conway de Macario E. The chaperone system in autoimmunity, inflammation, and virus-induced diseases: Role of chaperonins. In: Fink, G. (ed) Stress: Immunology and Inflammation. Handbook of Stress Series, Volume 5. Chapter 13. Elsevier/Academic Press, San Diego, CA USA, pp. 119-128, 2023. https://shop.elsevier.com/books/stress-immunology-and-inflammation/fink/978-0-12-817558-3
Macario, A.J.L. The chaperonopathies: a new field of medicine for study by physicians and all others involved in medical sciences and public health. Medicine & Health 2012, pp.202-204, 2012; published by Going International, Vienna, Austria. http://www.goinginternational.eu/pdfs/fachartikel/macario_the%20chapenonopathies_neu.pdf AUSTRIA.
Hansen, J.J., Durr, A., Cournu-Rebeix, I., Georgopoulos, C., Ang, D., Davoine, C.S., Brice, A., Fontaine, B., Gregersen, N. and Bross, P. Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am J Hum Genet 70: 1328-1332, 2002. http://www.sciencedirect.com/science/article/pii/S0002929707625257 DENMARK, FRANCE, SWITZWELAND.
Bouhouche, A., Benomar, A., Bouslam, N., Chkili, T. and Yahyaoui, M. Mutation in the epsilon subunit of the cytosolic chaperonin-containing t-complex peptide-1 (Cct5) gene causes autosomal recessive mutilating sensory neuropathy with spastic paraplegia. J. Med. Genet. 43: 441–443, 2006. doi: 10.1136/jmg.2005.039230. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2564519/ MOROCCO, AFRICA.
Magen D, Georgopoulos C, Bross P, Ang D, Segev Y, Goldsher D, Nemirovski A, Shahar E, Ravid S, Luder A, Heno B, Gershoni-Baruch R, Skorecki K, Mandel H. Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy. Am J Hum Genet. 2008 Jul;83(1):30-42. Epub 2008 Jun 19. PMID: 18571143. [PubMed – indexed for MEDLINE]. Available on-line at this link. ISRAEL, DENMARK.
Almeida-Souza L, Goethals S, de Winter V, Dierick I, Gallardo R, Van Durme J, Irobi J, Gettemans J, Rousseau F, Schymkowitz J, Timmerman V, Janssens S. Increased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathy. J Biol Chem. 2010 Apr 23;285(17):12778-86. Epub 2010 Feb 23. PMID: 20178975 [PubMed – indexed for MEDLINE]. Available on-line at this link. BELGIUM.
Maier, C.P. Chaperono- und Proteinopathien: molekulare Grundlagen – künftige Therapien. Dtsch. Med. Wochenschr. 2008;133:777-781. DOI 10.1055/s-2008-1075646. PDF Download – Thieme Connect. GERMANY.
Haak, J., Kregel, K.C. 1962-2007: a cell stress odyssey. 2008. The Biology of Extracellular Chaperones. Wiley, Chichester (Novartis Foundation Symposium 291) pp. 3-22. Available on-line at this link. CANADA, UNITED KINGDOM, INTERNATIONAL.
Martinez Picabea de Giorgiutti, E. Sobre chaperonas, epigénesis y enfermedad. Medicine (Buenos Aires) 71, 2011.
Available on-line at http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S0025-76802011000500023 and
http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S0025-76802011000800021. ARGENTINA.
Pharma Business Week, IX-3-2007. Published in Pharma Business Week, September 3rd, 2007
http://www.newsrx.com/newsletters/Pharma-Business-Week/2007-09-03/35090320071285PB.html
INTERNATIONAL.
http://web.sapmed.ac.jp/bssr/BSSR2009.html
大会のご案内2009 – 札幌医科大学
Symposium on Chaperonopathies, Sapporo, Japan October 6-9, 2009. JAPAN, ASIA.
Deocaris, C.C., Kaul, S.C. and Wadhwa, R. The versatile stress protein mortalin as a chaperone therapeutic agent. Protein Pept. Lett. 16: 517-229, 2009.
http://www.ncbi.nlm.nih.gov/pubmed/19442231 JAPAN, ASIA.
Turbpaiboon C, Wilairat P. Alpha-hemoglobin stabilizing protein: molecular function and clinical correlation. Front Biosci (Landmark Ed). 2010 Jan 1;15:1-11. PMID: 20036801.[PubMed – indexed for MEDLINE] http://www.ncbi.nlm.nih.gov/pubmed/20036801;
https://www.bioscience.org/2010/v15/af/3601/fulltext.htm THAILAND, ASIA.
Seigneuric R, Mjahed H, Gobbo J, Joly AL, Berthenet K, Shirley S, Garrido C. Heat shock proteins as danger signals for cancer detection. Front Oncol. 2011 Nov 10;1:37. doi: 10.3389/fonc.2011.00037. eCollection 2011. PMID: 22649762.
http://journal.frontiersin.org/article/10.3389/fonc.2011.00037/full FRANCE.
Hamelin C, Cornut E, Poirier F, Pons S, Beaulieu C, Charrier JP, Haïdous H, Cotte E, Lambert C, Piard F, Ataman-Önal Y, Choquet-Kastylevsky G.
Identification and verification of heat shock protein 60 as a potential serum marker for colorectal cancer.
FEBS J. 2011 Dec;278(24):4845-59. doi: 10.1111/j.1742-4658.2011.08385.x. Epub 2011 Nov 3. PMID: 21973086
http://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2011.08385.x/full FRANCE.
Symposium: Protein Misfolding and Chaperonopathies. 2:00 PM – 5:00 PM. Chairs: Monte S. Willis and Jonathan Lin. American Society for Investigative Pathology (ASIP) 2012 Annual Meeting at Experimental Biology. April 21-25, 2012 – San Diego, CA (USA), Program, Page 13. PDF program http://www.aspet.org/eb2012program/ Page 112. USA, INTERNATIONAL.
International Symposium: Molecular Chaperones, Chaperonopathies and Chaperonotherapy. Villa Malfitano, Via Dante, 167, Palermo, Italy. 29th October, 2013. https://plus.google.com/+IemestEu/posts/e6rhdbwRHjv. ITALY.
Melania Minoia. Chaperones, protein homeostasis and protein aggregation diseases. PhD thesis. Laboratory of Radiation and Stress Cell Biology, Department of Cell Biology of the University Medical Center Groningen and University of Groningen. The Netherlands. Pp. 1-164. June 30, 2014.
http://www.rug.nl/research/portal/files/13354615/Complete_disseration.pdf.
THE NETHERLANDS, ITALY.
Kevin Stein. Yeast prion variants as models of the phenotypic and pathological consequences of amyloid polymorphism. Ph.D. Thesis. Division of Biology and Biomedical Sciences, Molecular Cell Biology. Washington University in St. Louis. USA. Pp. 1-236, plus Appendix pp. 1-14. September 1, 2014.
http://openscholarship.wustl.edu/etd/1350/ and
http://openscholarship.wustl.edu/cgi/viewcontent.cgi?article=2350&context=etd. USA.
Radons J. Inflammatory stress and sarcomagenesis: a vicious interplay. Cell Stress Chaperones. 2014 Jan;19(1):1-13. doi: 10.1007/s12192-013-0449-4. Epub 2013 Aug 27. Review. PMID: 24046208.http://www.ncbi.nlm.nih.gov/pubmed/24046208. GERMANY.
Kakkar, V., Meister-Broekema, M., Minoia, M., Carra, S., Kampinga, H.H., Barcoding heat shock proteins to human diseases: looking beyond the heat shock response Dis. Model. Mech. April 2014, doi: 10.1242/dmm.014563vol. 7 no. 4 421-434 http://dmm.biologists.org/content/7/4/421. THE NETHERLANDS, ITALY.
Roos A, Buchkremer S, Kollipara L, Labisch T, Gatz C, Zitzelsberger M, Brauers E, Nolte K, Schröder JM, Kirschner J, Jesse CM, Goebel HH, Goswami A, Zimmermann R, Zahedi RP, Senderek J, Weis J. Myopathy in Marinesco-Sjögren syndrome links endoplasmic reticulum chaperone dysfunction to nuclear envelope pathology. Acta Neuropathol. 2014 May;127(5):761-77. doi: 10.1007/s00401-013-1224-4. Epub 2013 Dec 21. PMID: 24362440 http://www.ncbi.nlm.nih.gov/pubmed/24362440. GERMANY.
Bakthisaran R, Tangirala R, Rao ChM. Small heat shock proteins: Role in cellular functions and pathology. Biochim Biophys Acta. 2015 Apr;1854(4):291-319. doi: 10.1016/j.bbapap.2014.12.019. Epub 2014 Dec 30. Review. PMID: 25556000.
http://www.sciencedirect.com/science/article/pii/S1570963914003355. INDIA.
Roos A, Kollipara L, Buchkremer S, Labisch T, Brauers E, Gatz C, Lentz C, Gerardo-Nava J, Weis J, Zahedi RP. Cellular signature of sil1 depletion: disease pathogenesis due to alterations in protein composition beyond the ER machinery. Mol Neurobiol. 2015 Oct 14. [Epub ahead of print] PMID: 26468156 http://www.ncbi.nlm.nih.gov/pubmed/26468156. GERMANY.
Rubin’s Pathology. Clinicopathologic Foundations of Medicine. 2015. David S. Strayer MD, PhD; Emanuel Rubin MD. Ebook (VST PDF) ISBN/ISSN: 9781469883885
http://www.lww.com/product/9781469883885 Hard bound ISBN/ISSN: 9781451183900
http://www.lww.com/product/9781451183900. USA, INTERNATIONAL.
Royer-Bertrand B, Castillo-Taucher S, Moreno-Salinas R, Cho TJ, Chae JH, Choi M, Kim OH, Dikoglu E, Campos-Xavier B, Girardi E, Superti-Furga G, Bonafé L, Rivolta C, Unger S, Superti-Furga A. Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia. Sci Rep. 2015 Nov 24;5:17154. doi: 10.1038/srep17154.PMID: 26598328.
http://www.nature.com/articles/srep17154. SWITZERLAND, CHILE, REPUBLIC OF KOREA, AUSTRIA.
Buchkremer S, González Coraspe JA, Weis J, Roos A. Sil1-mutant mice elucidate chaperone function in neurological disorders. J Neuromuscul Dis. 2016 May 27;3(2):169-181. PMID: 27854219
http://content.iospress.com/articles/journal-of-neuromuscular-diseases/jnd160152. GERMANY.
Lupo V, Aguado C, Knecht E, Espinós C. Chaperonopathies: Spotlight on Hereditary Motor Neuropathies. Front Mol Biosci. 2016 Dec 14;3:81. doi: 10.3389/fmolb.2016.00081. Review. PMID: 28018906
http://journal.frontiersin.org/article/10.3389/fmolb.2016.00081/full. SPAIN.
Jha SK, Jha NK, Kumar P, Ambasta RK. Molecular chaperones and ubiquitin proteasome system in tumor biogenesis: An overview. J Cell Biol Cell Metab 3: 010. (2016).
http://heraldopenaccess.us/fulltext/Cell-Biology-&-Cell-Metabolism/Molecular-Chaperones-and-Ubiquitin-Proteasome-System-in-Tumor-Biogenesis-An-Overview.pdf. INDIA.
Lanfranco M, Vassallo N, Cauchi RJ. Spinal muscular atrophy: from defective chaperoning of snRNP assembly to neuromuscular dysfunction. Front Mol Biosci. 2017 Jun 8;4:41. doi: 10.3389/fmolb.2017.00041. eCollection 2017. Review. PMID: 28642865.
http://journal.frontiersin.org/article/10.3389/fmolb.2017.00041/full. MALTA.
Álvarez-Satta M, Castro-Sánchez S, Valverde D. Bardet-Biedl Syndrome as a chaperonopathy: Dissecting the major role of chaperonin-like BBS froteins (BBS6-BBS10-BBS12). Front Mol Biosci. 2017 Jul 31;4:55. doi: 10.3389/fmolb.2017.00055. eCollection 2017. Review. PMID: 28824921.
http://journal.frontiersin.org/article/10.3389/fmolb.2017.00055/full. SPAIN.
Blau N, Martinez A, Hoffmann GF, Thöny B. DNAJC12 deficiency: A new strategy in the diagnosis of hyperphenylalaninemias. Mol Genet Metab. 2018 Jan;123(1):1-5. doi: 10.1016/j.ymgme.2017.11.005. Epub 2017 Nov 20. PMID:29174366.
https://www.sciencedirect.com/science/article/pii/S1096719217306406. GERMANY, NORWAY, SWITZERLAND.
Meng Q, Li BX, Xiao X. Toward developing chemical modulators of Hsp60 as potential therapeutics. Front Mol Biosci. 2018 Apr 20;5:35. doi: 10.3389/fmolb.2018.00035. eCollection 2018. PMID:29732373.
https://www.frontiersin.org/articles/10.3389/fmolb.2018.00035/full. USA.
Cömert C, Fernandez-Guerra P, Bross P. A cell model for HSP60 deficiencies: modeling different levels of chaperonopathies leading to oxidative stress and mitochondrial dysfunction. Methods Mol Biol. 2019;1873:225-239. doi: 10.1007/978-1-4939-8820-4_14.
PMID:30341613. https://link.springer.com/protocol/10.1007%2F978-1-4939-8820-4_14. DENMARK.
Rodriguez A, Von Salzen D,. Holguin BA, Bernal RA. Complex destabilization in the mitochondrial chaperonin Hsp60 leads to disease. Front Mol Biosci. 2020; 7: 159. Published online 2020 Jul 14. doi:10.3389/fmolb.2020.00159. PMCID:PMC7381220 https://www.frontiersin.org/articles/10.3389/fmolb.2020.00159/full. USA.
Ray AM, Salim N, Stevens M, Chitre S, Abdeen S, Washburn A, Sivinski J, O’Hagan HM, Chapman E, Johnson SM. Exploiting the HSP60/10 chaperonin system as a chemotherapeutic target for colorectal cancer. Bioorg Med Chem. 2021 Jun 15;40:116129. DOI:10.1016/j.bmc.2021.116129. Epub 2021 Apr 19. PMID:33971488. PMCID:PMC8194340
Johnson JL.Mutations in Hsp90 cochaperones result in a wide variety of human disorders. Front Mol Biosci. 2021 Dec 8;8:787260. DOI:10.3389/fmolb.2021.787260. eCollection 2021.PMID:34957217. PMCID:PMC8694271. https://pubmed.ncbi.nlm.nih.gov/34957217/
Regimbeau M, Abrey J, Vautrot V, Causse S, Gobbo J, Garrido C. Heat shock proteins and exosomes in cancer theranostics. Semin Cancer Biol. 2022 Nov;86(Pt 1):46-57. DOI:10.1016/j.semcancer.2021.07.014. Epub 2021 Jul 31. PMID:34343652.
Eguchi T, Sheta M, Fujii M, Calderwood SK. Cancer extracellular vesicles, tumoroid models, and tumor microenvironment. Semin Cancer Biol. 2022 Nov;86(Pt 1):112-126. DOI:10.1016/j.semcancer.2022.01.003. Epub 2022 Jan 12. PMID:35032650.
Inoue M, Noguchi S, Inoue YU, Iida A, Ogawa M, Bengoechea R, Pittman SK, Hayashi S, Watanabe K, Hosoi Y, Sano T, Takao M, Oya Y, Takahashi Y, Miyajima H, Weihl CC, Inoue T, Nishino I. Distinctive chaperonopathy in skeletal muscle associated with the dominant variant in DNAJB4. Acta Neuropathol. 2023 Feb;145(2):235-255. DOI:10.1007/s00401-022-02530-4 Epub 2022 Dec 13.PMID:36512060. https://pubmed.ncbi.nlm.nih.gov/36512060/
Erger F, Aryal RP, Reusch B, Matsumoto Y, Meyer R, Zeng J, Knopp C, Noel M, Muerner L, Wenzel A, Kohl S, Tschernoster N, Rappl G, Rouvet I, Schröder-Braunstein J, Seibert FS, Thiele H, Häusler MG, Weber LT, Büttner-Herold M, Elbracht M, Cummings SF, Altmüller J, Habbig S, Cummings RD, Beck BB. Germline C1GALT1C1 mutation causes a multisystem chaperonopathy. Proc Natl Acad Sci U S A. 2023 May 30;120(22):e2211087120. DOI:10.1073/pnas.2211087120. Epub 2023 May 22. PMID:37216524. PMCID:PMC10235935 (available on 2023-11-22). https://pubmed.ncbi.nlm.nih.gov/37216524/
B. Publications pertaining to the chaperonopathies and the chaperoning (chaperone) system by IEMEST members
The chaperone system presentation: Macario, A.J.L., Conway de Macario, E. The chaperoning system: physiology and pathology, Exp. Med. Rev. 2-3 (2008) 9–21.
Macario, A.J.L. Heat-shock proteins and molecular chaperones: Implications for pathogenesis, diagnostics, and therapeutics. Intl. J. Clin. Lab. Res. 25: 59-70, 1995. http://www.ncbi.nlm.nih.gov/pubmed/7663007
Macario, A.J.L. and Conway de Macario, E. Stress and molecular chaperones in disease. Intl. J. Clin. Lab. Res. 30: 49-66, 2000.
http://www.ncbi.nlm.nih.gov/pubmed/11043498 and
http://link.springer.com/article/10.1007%2Fs005990070016
Macario AJL, Conway de Macario E. The molecular chaperone system and other anti-stress mechanisms in archaea. Front Biosci. 2001 Feb 1;6:D262-283. DOI:10.2741/macario. PMID:11171552. https://pubmed.ncbi.nlm.nih.gov/11171552/
Cappello, F., Bellafiore, M., Palma, A., Marcianò, V., Martorana, G., Belfiore, P., Martorana, A., Farina, F., Zummo, G. and Bucchieri, F. Expression of 60kDa heat shock protein increases during carcinogenesis in the uterine exocervix. Pathobiology 70: 83-88, 2002. Available on-line at this link.
Cappello, F., Bellafiore, M., Palma, A., Marcianò, V., Martorana, G., Belfiore, P., Martorana, A., Farina, F., Zummo, G. and Bucchieri, F. Expression of 60kDa heat shock protein increases during carcinogenesis in the uterine exocervix. Pathobiology 70: 83-88, 2002. Available on-line at this link.
Macario, A.J.L. and Conway de Macario, E. Sick chaperones and ageing: A perspective. Ageing Res. Rev. 1: 295-311, 2002. http://www.ncbi.nlm.nih.gov/pubmed/12039444 and http://www.sciencedirect.com/science/journal/15681637/1/2
Cappello, F. HSP60 and HSP10 as diagnostic and prognostic tools in the management of exocervical carcinoma. Gynecol. Oncol. 91: 661, 2003. Available on-line at this link.
Cappello, F., Bellafiore, M., David, S., Anzalone, R. and Zummo, G. Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix. Cancer Lett. 196: 35-41, 2003. Available on-line at this link.
Cappello, F., Bellafiore, M., Palma, A., David, S., Marcianò, V., Bartolotta, T., Sciumè, C., Modica, G., Farina, F., Zummo, G. and Bucchieri, F. 60kda chaperonin (hsp60) is over-expressed during colorectal carcinogenesis. Eur. J. Histochem. 47: 105-110, 2003. Available on-line at this link.
Cappello, F., Rappa, F., David, S., Anzalone, R. and Zummo, G. Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis. Anticancer Res. 23: 1325-1331, 2003. http://www.ncbi.nlm.nih.gov/pubmed/?term=Anticancer+Res.+23%3A+1325-1331%2C+2003
Pomara, G. and Cappello, F. Heat shock proteins: their role in urological tumors. J Urol. 170: 927-8, 2003. Available on-line at this link.
Cappello, F., Tripodo, C., Farina, F., Franco, V. and Zummo, G. HSP10 selective preference for myeloid and megakaryocytic precursors in normal human bone marrow. Eur. J. Histochem. 48: 261-265, 2004. http://www.ncbi.nlm.nih.gov/pubmed/?term=Eur.+J.+Histochem.+48%3A+261-265%2C+2004
Macario, A.J.L. and Conway de Macario, E. The pathology of anti-stress mechanisms: A new frontier. Stress 7: 243-249, 2004. http://informahealthcare.com/doi/abs/10.1080/10253890400019706
Macario, A.J.L., Malz, M. and Conway de Macario, E. Evolution of assisted protein folding: The distribution of the main chaperoning systems within the phylogenetic domain Archaea. Front. Biosci. (Landmark Ed.) 9: 1318-1332, 2004. To see Table of Contents, Abstract, and Tables go to: http://www.bioscience.org/2004/v9/af/1328/fulltext.htm
Cappello, F., David, S., Rappa, F., Bucchieri, F., Marasà, L., Bartolotta, T.E., Farina, F. and Zummo, G. The expression of HSP60 and HSP10 in large bowel carcinomas with lymph node metastases. BMC Cancer 5: 139, 2005. Available on-line at this link.
Cappello, F., Di Stefano, A., D’Anna, S.E., Donner, C.F. and Zummo, G. Immunopositivity of heat shock protein 60 as a biomarker of bronchial carcinogenesis. Lancet Oncol. 6: 816, 2005. Available on-line at this link.
Cappello, F. and Zummo, G. HSP60 expression during carcinogenesis: A molecular “Proteus” of carcinogenesis? Cell Stress Chap. 10: 263-264, 2005. Available on-line at this link.
Di Felice, V., Ardizzone, N., Marcianò, V., Bartolotta, T., Cappello, F., Farina, F., Zummo, G. Senescence-associated HSP60 expression in normal human skin fibroblasts. Anat. Rec. A Discov. Mol. Cell. Evol. Biol. 284A: 446-453, 2005. Available on-line at this link.
Di Felice, V., David, S., Cappello, F., Farina, F. and Zummo, G. Is Chlamydial Heat Shock Protein 60 a risk factor for oncogenesis? Cell. Mol. Life Sci. 62: 4-9, 2005. Available on-line at this link.
Macario, A.J.L. and Conway de Macario, E. Sick chaperones, cellular stress and disease. New Eng. J. Med. 353: 1489-1501, 2005. http://www.nejm.org/doi/full/10.1056/NEJMra050111
Macario, A.J.L., Grippo, T.M. and Conway de Macario, E. Genetic disorders involving molecular-chaperone genes: A perspective. Genet. Med. 7: 3-12, 2005. http://www.nature.com/gim/journal/v7/n1/full/gim20052a.html
Cappello, F. and Zummo, G. HSP60 expression during carcinogenesis: Where is the pilot? Path. Res. Pract. 202: 401-402, 2006. Available on-line at this link.
Cappello, F., Di Stefano, A., David, S., Rappa, F., Anzalone, R., La Rocca, G., D’Anna, S.E., Magno, F., Donner, C.F., Balbi, B. and Zummo, G. Hsp60 and Hsp10 downregulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease. Cancer 107: 2417-2424, 2006. Available on-line at this link.
Cappello, F., Ribbene, A., Campanella, C., Czarnecka, A.M., Anzalone, R., Bucchieri, F., Palma, A. and Zummo, G. The value of immunohistochemical research of PCNA, p53 and heat shock proteins in prostate cancer management: a review. Eur. J. Histochem. 50: 25-34, 2006. http://www.ncbi.nlm.nih.gov/pubmed/?term=Eur.+J.+Histochem.+50%3A+25-34%2C+2006
Czarnecka, A.M., Campanella, C., Zummo, G. and Cappello, F. Heat shock protein 10 and signal transduction: A “Capsula Eburnea” of carcinogenesis? Cell Stress Chap. 11: 287-294, 2006. Available on-line at this link.
Czarnecka, A.M., Campanella, C., Zummo, G. and Cappello, F. Mitochondrial chaperones in cancer: from molecular biology to clinical diagnostics. Cancer Biol. Ther. 5: 714-720, 2006. Available on-line at this link.
Brocchieri, L., Conway de Macario, E. and Macario, A.J.L. Chaperonomics, a new tool to study ageing and associated diseases. Mechan. Ageing Develop. 128: 125-136, 2007. http://www.sciencedirect.com/science/journal/00476374/128/1 and http://www.sciencedirect.com/science/article/pii/S0047637406002521
Cappello, F., Bucchieri, F., David, S., Campanella, C., Ribbene, A., Marino-Gammazza, A., Ardizzone, N., Merendino, A., Marcianò, V., Peri, G., Conway de Macario, E., Macario, A.J.L. and Zummo, G. Chaperonology: A novel research field for experimental medicine in XXI century. Experimental Medicine Reviews, ISBN: 978-88-89876-08-4, pp. 109-114, 2007. Available on-line at this link.
Cappello, F., Czarnecka, A.M., La Rocca, G., Di Stefano, A., Zummo, G. and Macario, A.J.L. Hsp60 and Hsp10 as antitumour molecular agents. Cancer Biol. Ther. 6: 4-6, 2007. Available on-line at this link.
Di Felice, V., Campanella, C., Marino Gammazza, A., Cappello, F. and Zummo, G. Heat shock proteins may have effects on cellular senescence and may lead to neoplastic transformation. In: New Research on Cell Aging. Edited R.B. Garvey. Nova Science Publisher Inc, 2007.
New Research on Cell Aging – Page 83 – Google Books Result
Di Felice, V., Cappello, F., Montalbano, A., Ardizzone, N.M., De Luca, A., Macaluso, F., Amelio, D., Cerra, M.C. and Zummo, G. HSP90 and eNOS partially co-localize and change cellular localization in relation to different ECM components in 2D and 3D cultures of adult rat cardiomyocytes. Biol. Cell 99: 689-699, 2007. Available on-line at this link.
Macario, A.J.L. and Conway de Macario, E. Chaperone proteins and chaperonopathies. In: The Encyclopedia of Stress. Second Edition. George Fink, Editor-in-Chief. Academic Press, Oxford, UK. Vol. 1, pp. 438-444, 2007. ISBN: 978-0-12-088503-9.
https://www.elsevier.com/books/encyclopedia-of-stress/fink/978-0-12-088503-9
http://www.sciencedirect.com/science/referenceworks/9780123739476
Macario, A.J.L. and Conway de Macario, E. Chaperonopathies. In: The Encyclopedia of Stress. Second Edition. George Fink, Editor-in-Chief. Academic Press, Oxford, UK. Vol. 1, pp. 444-448, 2007. ISBN: 978-0-12-088503-9. Available on-line at this link.
https://www.elsevier.com/books/encyclopedia-of-stress/fink/978-0-12-088503-9
http://www.sciencedirect.com/science/referenceworks/9780123739476
Macario, A.J.L. and Conway de Macario, E. Chaperonopathies and chaperonotherapy. FEBS Letters. 581: 3681-3688, 2007. http://www.febsletters.org/article/S0014-5793(07)00420-6/abstract and http://www.ncbi.nlm.nih.gov/pubmed/17475257
Macario, A.J.L. and Conway de Macario, E. Molecular chaperones: Multiple functions, pathologies, and potential applications. Front. Biosci. (Landmark Ed.) 12: 2588-2600, 2007. Available on-line at this link.
Macario, A.J.L. and Conway de Macario, E. Chaperonopathies by defect, excess, or mistake. Ann. New York Acad. Sci. 1113: 178-191, 2007. http://onlinelibrary.wiley.com/doi/10.1111/nyas.2007.1113.issue-1/issuetoc and http://onlinelibrary.wiley.com/enhanced/doi/10.1196/annals.1391.009
Brocchieri, L., Conway de Macario, E. and Macario, A.J.L. hsp-70 genes in the human genome: conservation and differentiation patterns predict a wide array of overlapping and specialized functions. BMC Evol. Biol. 2008, 8:19. DOI:10.1186/1471-2148-8-19 http://www.biomedcentral.com/1471-2148/8/19
Campanella, C., Bucchieri, F., Ardizzone, N.M., Marino Gammazza, A., Montalbano, A., Ribbene, A., Di Felice, V., Bellafiore, M., David, S., Rappa, F., Marasà, M., Peri, G., Farina, F., Czarnecka, A.M., Conway de Macario, E., Macario, A.J.L., Zummo, G. and Cappello, F. Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells. Eur. J. Histochem. 52: 221-228, 2008. http://www.ejh.it/index.php/ejh/article/view/1220/1329
Cappello, F., Conway de Macario, E., Marasà, L., Zummo, G. and Macario, A.J.L. Hsp60 expression, new locations, functions, and perspectives for cancer diagnosis and therapy. Cancer Biol. Ther. 7: 801-809, 2008. Available on-line at https://www.landesbioscience.com/journals/cbt/article/6281/.
Corrao, S., La Rocca, G., Anzalone, R., Farina, F., Marasà, L., Zummo, G. and Cappello, F. Role of CD1a and Hsp60 in the antitumoral response of oesophageal cancer. Oncol. Rev. 1: 225-232, 2008. http://link.springer.com/article/10.1007/s12156-008-0027-7
Campanella, C., Marino Gammazza, A., Mularoni, L., Cappello, F., Zummo, G. and Di Felice, V. A comparative analysis of the products of GROEL-1 gene from Chlamydia trachomatis serovar D and the HSP60 var1 transcript from Homo sapiens suggests a possible autoimmune response. Int. J. Immunogenet. 36: 73-78, 2009. Available on-line at this link.
Cappello, F., Conway de Macario, E., Di Felice, V., Zummo, G. and Macario, A.J.L. Chlamydia trachomatis infection and anti-Hsp60 immunity: The two sides of the coin. PLoS Pathogens 5:e1000552, 2009. Available on-line at this link.
Cappello, F., Di Stefano, A., Conway de Macario, E. and Macario, A.J.L. Hsp60 and Hsp10 in ageing. In: Heat shock proteins and whole body physiology. Edited by Alexzander A. A. Asea and Bente K. Pedersen, Springer-Verlag, Berlin, Heidelberg, Germany. Vol. 5, Part 3, Chapter 23, pp. 401-426, 2010. http://www.springerlink.com/content/q87536k412x74772/
Cappello, F., Marino Gammazza, A., Zummo, L., Conway de Macario, E. and Macario, A.J.L. Hsp60 and AChR cross-reactivity in myasthenia gravis: An update. J. Neurol. Sci. 292:117-8, 2010. Available on-line at this link.
Corrao, S., Campanella, C., Anzalone, R., Farina, F., Zummo, G., Conway de Macario, E., Macario, A.J.L., Cappello, F. and La Rocca, G. Human Hsp10 and early pregnancy factor (EPF) and their relationship and involvement in cancer and immunity: Current knowledge and perspectives. Life Science 86: 145-152, 2010. Available on-line at this link.
Czarnecka, A.M., Kukwa, W., Krawczyk, T., Scinska, A., Kukwa, A. and Cappello, F. Mitochondrial DNA mutations in cancer – from bench to bedside. Front. Biosci. (Landmark Ed.) 15: 437-460, 2010. To access Table of Contents, Abstract, Tables, and Figures, go to: http://www.frontbiosci.org/2010/v15/af/3629/tables.htm
Macario, A.J.L., Cappello, F., Zummo, G. and Conway de Macario, E. Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems. Ann. N.Y. Acad. Sci. 1197: 85-93, 2010. Available on-line at http://onlinelibrary.wiley.com/doi/10.1111/j.1749-6632.2010.05187.x/abstract
Merendino, A.M., Bucchieri, F., Campanella, C., Marcianò, V., Ribbene, A., David, S., Zummo, G., Burgio, G., Corona, D.F., Conway de Macario, E., Macario, A.J.L. and Cappello, F. Hsp60 is actively secreted by human tumor cells. PLoS ONE, 5: e9247, 2010. Available on-line at this link.
Mukherjee, K., Conway de Macario, E., Macario, A.J.L. and Brocchieri, L. Chaperonin genes on the rise: New divergent classes and intense duplication in human and other vertebrate genomes. BMC Evol. Biol. 2010, 10:64 http://www.biomedcentral.com/1471-2148/10/64
Pomara, C., D’Errico, S., Cappello, F., Zummo, L. and Li Volti, G. MDMA administration and heat shock proteins response: Foreseeing a molecular link. Curr. Pharm. Biotech. 11: 496-9, 2010. Available on-line at this link.
Rodolico, V., Tomasello, G., Zerilli, M., Martorana, A., Pitruzzella, A., Marino Gammazza, A., David, S., Zummo, G., Damiani, P., Accomando, S., Conway de Macario, E., Macario, A.J.L. and Cappello, F. Hsp60 and Hsp10 increase in colon mucosa of Crohn’s disease and ulcerative colitis. Cell Stress Chap. 15: 877-884, 2010. Available on-line at this link.
Cappello, F., Caramori, G., Campanella, C., Vicari, C., Gnemmi, I., Zanini, A., Spanevello, A., Capelli, A., La Rocca, G., Anzalone, R., Bucchieri, F., D’Anna, S.E., Ricciardolo, F.L.M., Brun, P., Balbi, B., Carone, M., Zummo, G., Conway de Macario, E., Macario, A.J.L. and Di Stefano, A. Convergent sets of data from in vivo and in vitro methods point to an active role of Hsp60 in chronic obstructive pulmonary disease pathogenesis. PLoS ONE, 6: e28200, 2011. Available on-line at this link.
Cappello, F., Conway de Macario, E., Zummo, G. and Macario, A.J.L. Immunohistochemistry of human Hsp60 in health and disease: from autoimmunity to cancer. In: Molecular Chaperones: Methods and Protocols. Edited by Stuart K. Calderwood and Thomas L. Prince, Methods in Molecular Biology, vol. 787, pp. 245-254. DOI 10.1007/978-1-61779-295-3_18, © Springer Science+Business Media, LLC 2011. Available on-line at this link
Cappello, F., David, S., Peri, G., Farina, F., Conway de Macario, E., Macario, A.J.L. and Zummo, G. Hsp60: molecular anatomy and role in colorectal cancer diagnosis and treatment. Front. Biosci. (Scholar Ed.) 3: 341-351, 2011. To access Table of Contents, Abstract, Tables, and Figures, go to: http://www.bioscience.org/2011/v3s/af/155/fulltext.htm
Novo, G., Cappello, F., Rizzo, M., Fazio, G., Zambuto, S., Tortorici, E., Marino Gammazza, A., Corrao, S., Zummo, G., Conway de Macario, E., Macario, A.J.L., Assennato, P., Novo, S. and Li Volti, G. Hsp60 and Heme Oxygenase-1 (Hsp32) in acute myocardial infarction. Transl. Res. 157: 285-292, 2011. Available on-line at this link.
Rizzo, M., Macario, A.J.L., Conway de Macario, E., Gouni-Berthold, I., Berthold, H.K., Rini, G.B., Zummo, G. and Cappello, F. Heat shock protein-60 and risk for cardiovascular disease. Curr. Pharm. Des. 17:3662-3668, 2011. Available on-line at this link.
Tomasello, G., Rodolico, V., Zerilli, M., Martorana, A., Bucchieri, F., Pitruzzella, A., Marino Gammazza, A., David, S., Rappa, F., Zummo, G., Damiani, P., Accomando, S., Rizzo, M., Conway de Macario, E., Macario, A.J.L. and Cappello, F. Changes in immunohistochemical levels and subcellular localization after therapy, as well as correlation and co-localization with CD68, suggest a pathogenetic role for Hsp60 in ulcerative colitis. Appl. Immunohistochem. Mol. Morph. 19: 1552-1561, 2011. Available on-line at this link.
Tomasello, G., Sciumè, C., Rappa. C., Rodolico, V., Zerilli, M., Martorana, A., Cicero, G., De Luca, R., Damiani, P., Accardo, F.M., Romeo, M., Bonaventura, G., Modica, G., Zummo, G., Conway de Macario, E., Macario, A.J.L. and Cappello, F. Hsp10, Hsp70, and Hsp90 immunohistochemical levels change in ulcerative colitis after therapy. Eur. J. Histochem. 55: e38, 2011. Available on-line at this link.
Campanella, C., Bucchieri, F., Merendino, A.M., Fucarino, A., Burgio, G., Corona, D.F., Barbieri, G., David, S., Farina, F., Zummo, G., Conway de Macario, E., Macario, A.J.L. and Cappello, F. The Odyssey of Hsp60 from tumour cells to other destinations includes membrane associated stages and Golgi and exosomal protein-trafficking modalities. PLoS ONE 7: e42008, 2012. Available on-line at this link.
Leone, A., Angelova Volponi, A., Campanella, C., Guarnotta, C., Abdallah Hajj Hussein, I., Cappello, F., Gerbino, A. and Jurjus, A. Human dental pulp cell apoptosis: Immunohistochemical study after applying orthodontic traction. J. Biol. Regul. Homeost. Agents 26: 713-720, 2012. http://www.ncbi.nlm.nih.gov/pubmed/?term=J.+Biol.+Regul.+Homeost.+Agents+26%3A+713-720%2C+2012
Macario, A.J.L., Cappello, F. and Conway de Macario. Chaperonopathies: Diseases in which mortalin and other Hsp-chaperones play a role in etiology and pathogenesis. In: Mortalin biology. Stress, life, and death. Edited by S. C. Kaul and Renu Wadhwa, Springer-Verlag, Berlin, Heidelberg, Germany. Chapter 13, pp. 209-221, 2012. http://www.springer.com/biomed/molecular/book/978-94-007-3026-7
Marino Gammazza, A., Bucchieri, F., Grimaldi, L.M.E., Benigno, A., Conway de Macario, E., Macario, A.J.L., Zummo, G. and Cappello, F. The molecular anatomy of human Hsp60 and its similarity with that of bacterial orthologs and acetylcholine receptor reveal a potential pathogenetic role of anti-chaperonin immunity in myasthenia gravis. Cell. Mol. Neurobiol. 32: 943-947, 2012. Available on-line at this link.
Rappa, F., Farina, F., Zummo, G., David, S., Campanella, C., Carini, F., Tomasello, G., Damiani, P., Cappello, F., Conway de Macario, E. and Macario, A.J.L. HSP-molecular chaperones in cancer biogenesis and tumor therapy: An overview. Anticancer Res. 32: 5139-5150, 2012. Available on-line at http://ar.iiarjournals.org/content/32/12/5139.long and http://ar.iiarjournals.org/content/32/12/5139.abstract
Rizzo, M., Cappello, F., Marfil, R., Nibali, L., Marino Gammazza, A., Rappa, F., Bonaventura, G., Galindo-Moreno, P., O’Valle, F., Zummo, G., Conway de Macario, E., Macario, A.J.L. and Mesa, F. Heat shock protein 60 kDa and atherogenic dyslipidemia in patients with untreated mild periodontitis: A pilot study. Cell Stress Chap. 17: 399-407, 2012. Available on-line at this link.
Barbagallo, I., Galvano, F., Frigiola, A., Cappello, F., Riccioni, G., Murabito, P., D’Orazio, N., Torella, M., Gazzolo, D. and Li Volti, G. Potential therapeutic effects of natural Heme Oxygenase-1 inducers in cardiovascular diseases. Antioxid. Redox Signal. 18: 507-521, 2013. Available on-line at this link.
Bellavia, M., Tomasello, G., Romeo, M., Damiani, P., Lo Monte, A.I., Lozio, L., Campanella, C., Marino Gammazza, A., Rappa, F., Zummo, G., Cocchi, C., Conway de Macario, E., Macario, A.J.L. and Cappello, F. Gut microbiota imbalance and chaperoning system malfunction are central to ulcerative colitis pathogenesis and can be counteracted with specifically designed probiotics: A working hypothesis. Med. Microbiol. Immunol. 202: 393-406, 2013. Available on-line at this link.
Cappello, F., Angileri, F., Conway de Macario, E. and Macario, A.J.L. Chaperonopathies and chaperonotherapy. Hsp60 as therapeutic target in cancer: Potential benefits and risks. Curr. Pharm. Des. 19: 452-457; 2013. Available on-line at this link.
Cappello, F., Conway de Macario, E., Marino Gammazza, A., Bonaventura, G., Carini, F., Czarnecka, A.M., Farina, F., Zummo, G. and Macario, A.J.L. Hsp60 and human aging: Les liaisons dangereuses. Front. Biosci. (Landmark Ed.) 18: 626-637, 2013. Available online at this link. To access Table of Contents, Abstract, Tables, and Figures, go to: http://www.bioscience.org/2013/v18/af/4126/fulltext.htm
Cappello, F., Zummo, G., Conway de Macario, E. and Macario, A.J.L. Are Heat shock proteins/molecular chaperones the link between osteoarthritis and cardiovascular risk? BMJ, November 4, 2013. Available online at http://www.bmj.com/content/347/bmj.f6187/rr/670305
David, S., Bucchieri, F., Corrao, S., Czarnecka, A.M., Campanella, C., Farina, F., Peri, G., Tomasello, G., Sciumè, C., Modica, G., La Rocca, G., Anzalone, R., Giuffrè, M., Conway de Macario, E., Macario, A.J.L., Cappello, F. and Zummo, G. Hsp10: anatomic distribution, functions, and involvement in human disease. Front. Biosci. (Elite Ed.) E5: 768-778, 2013. To access Table of Contents, Abstract, Tables, and Figures, go to: http://www.bioscience.org/2013/v5e/af/657/fulltext.htm
Giffard, R.G., Macario, A.J.L., Conway de Macario, E. The future of molecular chaperones and beyond. J. Clin. Invest. 123: 3206-3207, 2013. http://www.jci.org/articles/view/70799
Gorska, M., Marino Gammazza, A., Zmijewski, M.A., Sielicka, A., Campanella, C., Wasiewicz, T., Kuban-Jankowska, A., Daca, A., Popowska, U., Knap, N., Antoniewicz, J., Cappello, F., Wakabayashi, T. and Wozniak, M. Geldanamycin-induced osteosarcoma cell death is associated with hyperacetylation and loss of mitochondrial pool of heat shock protein Hsp60. PLoS ONE 8: e71135, 2013. Available on-line at this link.
Kast, R.E., Boockvar, J.A., Brüning, A., Cappello, F., Chang, W.W., Cvek, B., Dou, Q.P., Duenas, A., Efferth, T., Focosi, D., Ghaffari, S.H., Karpel-Massler, G., Ketola, K., Khoshnevisan, A., Keizman, D., Magné, N., Marosi, C., McDonald, T., Muñoz, M., Paranjpe, A., Pourgholami, M.H., Sardi, I., Sella, A., Srivenugopal, K.S., Tuccori, M., Wang, W., Wirtz, C.R. and Halatsch, M.E. A conceptually new treatment approach for relapsed glioblastoma: Coordinated undermining of survival paths with nine repurposed drugs (CUSP9) by the International Initiative for Accelerated Improvement of Glioblastoma Care. Oncotarget 4: 502-30, 2013. Available online at this link.
Macario, A.J.L., Cappello, F. and Conway de Macario. Hsp60: key clinico-pathological factor and a promising therapeutic target. World Biomedical Frontiers. ISSN: 2328-0166. Cancer 2013 July-22. http://biomedfrontiers.org/cancer-2013-july-22/
Macario, A.J.L. and Conway de Macario, E. Chaperonopathies: Impact on protein folding and beyond. Proceedings 10th Internactional Congress on Cell Biology-16th Congress of the Brazilian Society for Cell Biology. Rio de Janeiro, Brazil, VII/12. Pp. 119-124, 2013.
http://www.medimond.com/ebook/P726.pdf
Pace, A., Barone, G., Lauria, A., Martorana, A., Piccionello, A.P., Pierro, P., Terenzi, A., Almerico, A.M., Buscemi, S., Campanella, C., Angileri, F., Carini, F., Zummo, G., Conway de Macario, E., Cappello, F. and Macario, A.J.L. Hsp60, a novel target for antitumor therapy: Structure-function features and prospective drugs design. Curr. Pharm. Des. 19: 2757-2764, 2013. Available online at this link.
Rappa, F., Cappello, F., Halatsch, M.E., Scheuerle, A. and Kast, R.E. Aldehyde dehydrogenase and HSP90 co-localize in human glioblastoma biopsy cells. Biochimie 95: 782-786, 2013. Available on-line at this link.
Rappa, F., Unti, E., Baiamonte, P., Cappello, F. and Scibetta, N. Different immunohistochemical levels of Hsp60 and Hsp70 in a subset of brain tumors and putative role of Hsp60 in neuroepithelial tumorigenesis. Eur. J. Histochem. 57: e20, 2013. Available on-line at this link.
Cappello, F., Marino Gammazza, A., Palumbo Piccionello, A., Campanella, C., Pace, A., Conway de Macario, E. and Macario, A.J.L. Hsp60 chaperonopathies and chaperonotherapy: targets and agents. Expert Opin. Ther. Targets 18: 185-208, 2014. Available on-line at this link.
Marino Gammazza, A., Rizzo, M., Citarrella, R., Rappa, F., Campanella, C., Bucchieri, F., Patti, A., Nikolic, D., Cabibi, D., Amico, G., Conaldi, P.G., San Biagio, P.L., Montalto, G., Farina, F., Zummo, G., Conway de Macario, E., Macario, A.J.L. and Cappello, F. Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes point to the chaperonin as an immunopathogenic factor in Hashimoto’s thyroiditis. Cell Stress Chap. 19: 343-53, 2014. Available on-line at this link.
Vilasi S, Carrotta R, Mangione MR, Campanella C, Librizzi F, Randazzo L, Martorana V, Marino Gammazza A, Ortore MG, Vilasi A, Pocsfalvi G, Burgio G, Corona D, Palumbo Piccionello A, Zummo G, Bulone D, Conway de Macario E, Macario AJ, San Biagio PL, Cappello F. Human Hsp60 with its mitochondrial import signal occurs in solution as heptamers and tetradecamers remarkably stable over a wide range of concentrations. PLoS One. 2014 May 15;9(5):e97657. doi: 10.1371/journal.pone.0097657. eCollection 2014. PMID: 24830947 [PubMed – in process] http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0097657
Cappello, F., Conway de Macario, E. and Macario, A.J.L. HSPD1 (Heat Shock 60kDa Protein 1). Atlas of Genetics and Cytogenetics in Oncology and Haematology. 2014
http://atlasgeneticsoncology.org/Genes/GC_HSPD1.html
http://AtlasGeneticsOncology.org/Genes/HSPD1ID40888ch2q33.html
http://documents.irevues.inist.fr/handle/2042/15655
Min W, Angileri F, Luo H, Lauria A, Shanmugasundaram M, Almerico AM, Cappello F, de Macario EC, Lednev IK, Macario AJ, Robb FT.A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model. Sci Rep. 2014 Oct 27;4:6688. doi: 10.1038/srep06688.
http://www.ncbi.nlm.nih.gov/pubmed/25345891 http://www.nature.com/srep/2014/141027/srep06688/full/srep06688.html
Corrao S, Anzalone R, Lo Iacono M, Corsello T, Di Stefano A, D’Anna SE, Balbi B, Carone M, Sala A, Corona D, Timperio AM, Zolla L, Farina F, Conway de Macario E, Macario AJ, Cappello F, La Rocca G. Hsp10 nuclear localization and changes in lung cells response to cigarette smoke suggest novel roles for this chaperonin. Open Biol. 2014 Oct;4(10). pii: 140125. doi: 10.1098/rsob.140125.
http://www.ncbi.nlm.nih.gov/pubmed/25355063
http://rsob.royalsocietypublishing.org/content/4/10/140125.long
Marino Gammazza, A., Colangeli, R., Orban, G., Pierucci, M., Di Gennaro, G., Lo Bello, M., D’Aniello, A., Bucchieri, F., Pomara, C., Valentino, M., Muscat, R. Benigno, A, Zummo, G., Conway de Macario, E., Cappello, F., Di Giovanni, G. and Macario, A.J.L. Hsp60 response in experimental and human temporal lobe epilepsy. Sci. Rep. (Nature) 2015 Mar 24;5:9434. doi: 10.1038/srep09434. PMID: 25801186
http://www.nature.com/srep/2015/150324/srep09434/full/srep09434.html
http://www.ncbi.nlm.nih.gov/pubmed/25801186
http://www.nature.com/srep/2015/150324/srep09434/extref/srep09434-s1.pdf
Campanella, C., Rappa, F., Sciumè, C., Marino Gammazza, A., Barone, R., Bucchieri, F., David, S., Curcurù, G., Caruso Bavisotto, C., Pitruzzella, A., Geraci, G., Modica, G., Farina, F., Zummo, G., Fais, S., Conway de Macario, E., Macario, A.J.L. and Cappello, F. Heat shock protein 60 levels in tissue and circulating exosomes in human large bowel cancer before and after ablative surgery. Cancer. 2015 Jun 8. doi: 10.1002/cncr.29499. [Epub ahead of print] PMID: 26060090
http://www.ncbi.nlm.nih.gov/pubmed/26060090;
http://onlinelibrary.wiley.com/doi/10.1002/cncr.29499/abstract;jsessionid=7DC0E0CB9455E1B546BC8B0F287E8AFD.f02t03
Cabibi, D., Conway de Macario, E., Ingrao, S., Porcasi, R., Zucco, F., Macario, A.J.L., Cappello, F. and Rappa, F. CD1A positive cells and Hsp60 (HSPD1) levels in keratoacanthoma and squamous cell carcinoma. Cell Stress & Chaperones DOI 10.1007/s12192-015-0646-4.
http://link.springer.com/article/10.1007/s12192-015-0646-4?wt_mc=internal.event.1.SEM.ArticleAuthorOnlineFirst
Leonardi, A., Tarricone, E., Corrao, S., Alaibac, M., Corso, A.J., Zavan, B., Venier, P., Conway de Macario, E., Macario, A.J.L., Di Stefano, A., Cappello, F. and Brun P. Chaperone patterns in vernal keratoconjunctivitis are distinctive of cell and Hsp type, and are modified by inflammatory stimuli. Allergy. 2015 Nov 27. doi: 10.1111/all.12814. [Epub ahead of print] PMID: 26613380.
http://www.ncbi.nlm.nih.gov/pubmed/26613380
Campanella C, D’Anneo A, Gammazza AM, Bavisotto CC, Barone R, Emanuele S, Lo Cascio F, Mocciaro E, Fais S, Conway de Macario E, Macario AJL, Cappello F, Lauricella M.
The histone deacetylase inhibitor SAHA induces HSP60 nitration and its extracellular release by exosomal vesicles in human lung-derived carcinoma cells. Oncotarget. 2015 Dec 19. doi: 10.18632/oncotarget.6680. [Epub ahead of print] PMID: 26700624
http://www.ncbi.nlm.nih.gov/pubmed/26700624 and
http://www.impactjournals.com/oncotarget/index.php?journal=oncotarget&page=article&op=view&path[]=6680&pubmed-linkout=1
Barone R, Rappa F, Macaluso F, Caruso Bavisotto C, Sangiorgi C, Di Paola G, Tomasello G, Di Felice V, Marcianò V, Farina F, Zummo G, Conway de Macario E, Macario A J L, Cocchi M, Cappello F, Marino Gammazza A.
Alcoholic liver disease: a mouse model reveals protection by Lactobacillus fermentum. Clin Transl Gastroenterol. 2016 Jan 21;7:e138. doi: 10.1038/ctg.2015.66. PMID: 26795070
http://www.nature.com/doifinder/10.1038/ctg.2015.66
Bellipanni G, Cappello F, Scalia F, Conway de Macario E, Macario AJL, Giordano A.
Zebrafish as a model for the study of chaperonopathies. J Cell Physiol. 2016 Jan 27. doi: 10.1002/jcp.25319. [Epub ahead of print] Review. PMID: 26812965.
Barone R, Macaluso F, Sangiorgi C, Campanella C, Marino Gammazza A, Moresi V, Coletti D, Conway de Macario E, Macario AJL, Cappello F, Adamo S, Farina F, Zummo G, Di Felice V. Skeletal muscle Heat shock protein 60 increases after endurance training and induces peroxisome proliferator-activated receptor gamma coactivator 1 α1 expression. Sci Rep. (NATURE) 2016 Jan 27;6:19781. doi: 10.1038/srep19781. PMID: 26812922.
Marino Gammazza A, Caruso Bavisotto C, Barone R, Conway de Macario E and Macario, AJL. Alzheimer’s disease and molecular chaperones: Current knowledge and the future of chaperonotherapy. Current Pharmaceutical Design, 22(26): 4040-4049. May 18, 2016 [Epub ahead of print] PMID: 27189602 [PubMed – in process]
http://www.ncbi.nlm.nih.gov/pubmed/27189602
http://benthamscience.com/journals/current-pharmaceutical-design/volume/22/issue/26/page/4040/
Macario AJL, Conway de Macario E. The chaperoning and the immune systems with the microbiome integrate a matrix that supports health: when one of them is disturbed the others suffer and disease ensues. Life Safety and Security (LiSS). 4(6):101-123, 2016. DOI: 10.12882/2283-7604.2016.4.6.
https://www.iemest.eu/life-safety-and-security/index.php and https://www.iemest.eu/life-safety-and-security/images/Doc/ARTICOLI/2016/macario_24/Macario04.pdf
Rappa F, Pitruzzella A, Marino Gammazza A, Barone R, Mocciaro E, Tomasello G, Carini F, Farina F, Zummo G, Conway de Macario E, Macario AJL, Cappello F. Quantitative patterns of Hsps in tubular adenoma compared with normal and tumor tissues reveal the value of Hsp10 and Hsp60 in early diagnosis of large bowel cancer. Cell Stress Chaperones. 2016 Sep;21(5):927-33. doi: 10.1007/s12192-016-0721-5. Epub 2016 Aug 4. PMID: 27491302.
http://www.ncbi.nlm.nih.gov/pubmed/27491302
http://link.springer.com/article/10.1007%2Fs12192-016-0721-5
Marino Gammazza A, Campanella C, Barone R, Caruso Bavisotto C, Gorska M, Wozniak M, Carini F, Cappello F, D’Anneo A, Lauricella M, Zummo G, Conway de Macario E, Macario AJL, Di Felice V. Doxorubicin anti-tumor mechanisms include Hsp60 post-translational modifications leading to the Hsp60/p53 complex dissociation and instauration of replicative senescence. Cancer Lett. 2016 Nov 9;385:75-86, 2017. doi: 10.1016/j.canlet.2016.10.045. [Epub ahead of print] PMID: 27836734.
https://www.ncbi.nlm.nih.gov/pubmed/27836734
http://www.cancerletters.info/article/S0304-3835(16)30676-0/abstract
Conway de Macario E, Robb FT, Macario AJL. Prokaryotic chaperonins as experimental models for elucidating structure-function abnormalities of human pathogenic mutant counterparts. Front Mol Biosci. 2017 Jan 9;3:84. doi: 10.3389/fmolb.2016.00084.
Review. PMID: 28119916. https://www.ncbi.nlm.nih.gov/pubmed/28119916
http://journal.frontiersin.org/article/10.3389/fmolb.2016.00084/full
Caruso Bavisotto C, Nikolic D, Marino Gammazza A, Barone R, Lo Cascio F, Mocciaro E, Zummo G, Conway de Macario E, Macario AJL, Cappello F, Giacalone V, Pace A, Barone G, Palumbo Piccionello A, Campanella C. The dissociation of the Hsp60/pro-Caspase-3 complex by bis(pyridyl)oxadiazole copper complex (CubipyOXA) leads to cell death in NCI-H292 cancer cells. J Inorg Biochem. 2017 Feb 10;170:8-16. doi: 10.1016/j.jinorgbio.2017.02.004. [Epub ahead of print] PMID: 28212901
https://www.ncbi.nlm.nih.gov/pubmed/28212901
http://www.sciencedirect.com/science/article/pii/S0162013417300776
Caruso Bavisotto, C., Cappello, F., Macario, A.J.L., Conway de Macario, E., Logozzi, M., Fais, S. and Campanella, C. Exosomal HSP60: a potentially useful biomarker for diagnosis, assessing prognosis, and monitoring response to treatment. Expert Review of Molecular Diagnostics. 2017 Sep;17(9):815-822. doi: 10.1080/14737159.2017.1356230. Epub 2017 Jul 25. PMID: 28718351.
http://www.tandfonline.com/doi/abs/10.1080/14737159.2017.1356230
Marino Gammazza, A, Caruso Bavisotto, C., David, S., Barone, R., Rappa, F., Campanella, C., Conway de Macario, E., Cappello, F. and Macario, A.J.L. HSP60 is a ubiquitous player in the physiological and pathogenic interactions between the chaperoning and the immune systems. Curr. Immunol. Rev. 13(1); 44-55, 2017. DOI:10.2174/1573395513666170412170540
http://www.eurekaselect.com/151566
Macario, A.J.L. and Conway de Macario, E. Archaeal chaperonins: a cornucopia of information and tools to understand the human chaperoning system and its diseases. In: Prokaryotic Chaperonins. Multiple Copies and Multitude of Functions. Edited by C. M. Santosh Kumar and Shekhar C. Mande. Springer Nature Singapore Pte Ltd. 2017 129. Heat Shock Proteins 11, DOI 10.1007/978-981-10-4651-3_9. Pp. 129-146, 2017.
https://link.springer.com/book/10.1007/978-981-10-4651-3
Sangiorgi, C., Vallese, D., Gnemmi, I., Bucchieri, F., Balbi, B., Brun, P., Leone, A., Giordano, A., Conway de Macario, E., Macario, A. J. L., Cappello, F., and Di Stefano, A. HSP60 activity on human bronchial epithelial cells. Int. J. Immunopathol. Pharmacol. 2017 Dec;30(4):333-340. doi: 10.1177/0394632017734479. Epub 2017 Oct 4. PMID:28976240.
https://doi.org/10.1177/0394632017734479
http://journals.sagepub.com/eprint/xShztAYqDIqmR3ghGfDx/full
Spigolon D, Gallagher DT, Velazquez-Campoy A, Bulone D, Narang J, San Biagio PL, Cappello F, Macario AJL, Conway de Macario E, Robb FT. Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog. Biochem Biophys Rep. 2017 Sep 1;12:66-71. doi: 10.1016/j.bbrep.2017.07.011. eCollection 2017 Dec. PMID:29552646.
https://www.sciencedirect.com/science/article/pii/S2405580817301176?via%3Dihub
Cappello F, Conway de Macario E, Rappa F, Zummo G, Macario AJL. Immunohistochemistry of human Hsp60 in health and disease: From autoimmunity to cancer. Methods Mol. Biol. 2018;1709:293-305. doi: 10.1007/978-1-4939-7477-1_21. PMID: 29177667.
Vilasi S, Bulone D, Caruso Bavisotto C, Campanella C, Marino Gammazza A, San Biagio PL, Cappello F, Conway de Macario E, Macario AJL. Chaperonin of Group I: Oligomeric spectrum and biochemical and biological implications. Front Mol Biosci. 2018 Jan 25;4:99. doi: 10.3389/fmolb.2017.00099. eCollection 2017. PMID:29423396.
https://www.ncbi.nlm.nih.gov/pubmed/29423396
Macario AJL, Conway de Macario E. Editorial: Pathologic conditions of the human nervous and muscular systems associated with mutant chaperones: molecular and mechanistic aspects. Front Mol Biosci. 2018 Feb 16;5:14. doi: 10.3389/fmolb.2018.00014. eCollection 2018. PMID:29503823.
https://www.ncbi.nlm.nih.gov/pubmed/29503823
Macario AJL, Conway de Macario E. Advances in the understanding and management of neuromuscular diseases. Life Safety and Security (LiSS) 6(1):109-118, 2018. DOI: 10.12882/2283-7604.2018.6.1.
https://www.iemest.eu/life-safety-and-security/index.php and https://www.iemest.eu/life-safety-and-security/images/Doc/ARTICOLI/2018/Macario%2041/Macario06.pdf
Graziano F, Bavisotto CC, Gammazza AM, Rappa F, Conway de Macario E, Macario AJL, Cappello F, Campanella C, Maugeri R, Iacopino DG. Chaperonology: The third eye on brain gliomas. Brain Sci. 2018 Jun 14;8(6). pii: E110. doi: 10.3390/brainsci8060110. PMID:29904027
Abstract: http://www.mdpi.com/2076-3425/8/6/110
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Caruso Bavisotto C, Graziano F, Rappa F, Marino Gammazza A, Logozzi M, Fais S, Maugeri R, Bucchieri F, Conway de Macario E, Macario AJL, Cappello F, Iacopino DG, Campanella C. Exosomal chaperones and miRNAs in gliomagenesis: State-of-art and theranostics perspectives. Int J Mol Sci. 2018 Sep 5;19(9). pii: E2626. doi: 10.3390/ijms19092626. PMID:30189598
http://www.mdpi.com/journal/ijms/special_issues/Intracranial
Marino Gammazza A, Restivo V, Baschi R, Bavisotto CC, Cefalù AB, Accardi G, Conway de Macario E, Macario AJL, Cappello F, Monastero R. Circulating molecular chaperones in subjects with Amnestic Mild Cognitive Impairment and Alzheimer’s Disease: Data from the Zabùt Aging Project. J Alzheimers Dis. 2018 Dec 20. doi: 10.3233/JAD-180825. [Epub ahead of print] PMID:30584145.
https://content.iospress.com/articles/journal-of-alzheimers-disease/jad180825
Bulone D, San Biagio PL, Quiñones-Ruiz T, Rosario-Alomar M, Lednev IK, Robb FT, Conway de Macario E, Macario AJL. A multipronged method for unveiling subtle structural-functional defects of mutant chaperone molecules causing human chaperonopathies.
Methods Mol Biol. 2019;1873:69-92. doi: 10.1007/978-1-4939-8820-4_5. PMID:30341604.
https://link.springer.com/protocol/10.1007%2F978-1-4939-8820-4_5
Caruso Bavisotto C, Scalia F, Marino Gammazza A, Carlisi D, Bucchieri F, Conway de Macario E, Macario AJL, Cappello F, Campanella C. Extracellular vesicle-mediated cell-cell communication in the nervous system: Focus on neurological diseases. Int J Mol Sci. 2019 Jan 20;20(2). pii: E434. doi: 10.3390/ijms20020434. PMID:30669512
Abstract: http://www.mdpi.com/1422-0067/20/2/434
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Cappello F, Mazzola M, Jurjus A, Zeenny MN, Jurjus R, Carini F, Leone A, Bonaventura G, Tomasello G, Bucchieri F, Conway de Macario E, Macario AJL. Hsp60 as a novel target in IBD management: A Prospect. Front Pharmacol. 2019 Feb 8;10:26. doi: 10.3389/fphar.2019.00026. eCollection 2019. Review. PMID:30800066. https://www.frontiersin.org/articles/10.3389/fphar.2019.00026/full
Cappello F, Macario AJL. Depleted uranium induces human carcinogenesis involving the immune and chaperoning systems: Realities and working hypotheses. Med Hypotheses. 2019 Mar;124:26-30. doi: 10.1016/j.mehy.2019.01.018. Epub 2019 Jan 24. PMID:30798910 https://www.sciencedirect.com/science/article/pii/S0306987718311940
Conway de Macario E, Yohda M, Macario AJL, Robb FT. Bridging human chaperonopathies and microbial chaperonins. Commun Biol. (NATURE) 2019 Mar 15;2:103. doi: 10.1038/s42003-019-0318-5. eCollection 2019. PMID:30911678. https://www.nature.com/articles/s42003-019-0318-5
Marino Gammazza A, Caruso Bavisotto C, Macario AJL. Physiology and pathophysiology of heat shock protein 60. Front. Mol. Biosc., 2019. https://www.frontiersin.org/research-topics/10435/physiology-and-pathophysiology-of-heat-shock-protein-60
Cappello F, Macario AJL, Conway de Macario E. Hsp60: a story as long as Life on the Earth. Chapter 1, pp. 3-14, in: Heat Shock Protein 60 in Human Diseases and Disorders, edited by Alexzander A. A. Asea and Punit Kaur. Volume 18 of the Book Series Heat Shock Proteins, edited by Alexzander A. A. Asea and Stuart K. Calderwood, and published by © Springer Nature Switzerland AG 2019 https://doi.org/10.1007/978-3-030-23154-5_1
Barone R, Di Felice V, Coletti D, Macario AJL. Hsp60 in skeletal muscle: from molecular anatomy to pathophysiology. Chapter 17, pp. 269-276, in: Heat Shock Protein 60 in Human Diseases and Disorders, edited by Alexzander A. A. Asea and Punit Kaur. Volume 18 of the Book Series Heat Shock Proteins, edited by Alexzander A. A. Asea and Stuart K. Calderwood, and published by © Springer Nature Switzerland AG 2019 https://doi.org/10.1007/978-3-030-23154-5_17
Marino Gammazza A, Caruso Bavisotto C, Rappa F, Scalia F, Conway de Macario E, Macario AJL, Cappello F. Hsp60 friend and foe of the Nervous System. Chapter 1, pp. 1-21, in: Heat Shock Proteins in Neuroscience, edited by Alexzander A. A. Asea and Punit Kaur. Volume 20 of the Book Series Heat Shock Proteins, edited by Alexzander A. A. Asea and Stuart K. Calderwood, and published by © Springer Nature Switzerland AG 2019 https://doi.org/10.1007/978-3-030-24285-5_1
Caruso Bavisotto C, Cipolla C, Graceffa G, Barone R, Bucchieri F, Bulone D, Cabibi D, Campanella C, Marino Gammazza A, Pitruzzella A, Porcasi R, San Biagio PL, Tomasello G, Conway de Macario E, Macario AJL, Cappello F, Rappa F. Immunomorphological pattern of molecular chaperones in normal and pathological thyroid tissues and circulating exosomes: Potential use in clinics. Int J Mol Sci. 2019 Sep 11;20(18). pii: E4496. doi: 10.3390/ijms20184496. PMID:31514388
https://www.mdpi.com/1422-0067/20/18/4496
https://www.mdpi.com/journal/ijms/special_issues/chaperones_II
https://www.mdpi.com/1422-0067/20/18/4496/pdf
https://www.mdpi.com/1422-0067/20/18/4496
https://www.mdpi.com/1422-0067/20/18/4496?type=check_update&version=2
Pitruzzella A, Paladino L, Vitale A, Martorana S, Cipolla C, Gracefa G, Cabibi D, David S, Fucarino A, Bucchieri F, Cappello F, Conway de Macario E, Macario AJL, Rappa F. Quantitative immunomorphological analysis of heat shock proteins in thyroid follicular adenoma and carcinoma tissues reveals their potential for differential diagnosis and points to a role in carcinogenesis. Applied Sciences, 2019,9(20), 4324.https://doi.org/10.3390/app9204324″>https://doi.org/10.3390/app9204324
Abstract: https://www.mdpi.com/2076-3417/9/20/4324
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Scalia F, Marino Gammazza A, Conway de Macario E, Macario AJL, Cappello F. Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy. Brain Sci. 2019 Oct 30;9(11). pii: E297. doi: 10.3390/brainsci9110297.
PMID:31671529 https://doi.org/10.3390/brainsci9110297
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Macario AJL, Conway de Macario E. Molecular mechanisms in chaperonopathies: clues to understanding the histopathological abnormalities and developing novel therapies. J Pathol. 2019 Oct 3. doi: 10.1002/path.5349. J Pathol. January 2020; 250(1):9-18 Review. PMID:31579936 https://onlinelibrary.wiley.com/doi/abs/10.1002/path.5349
https://doi.org/10.1002/path.5349
Macario AJL, Conway de Macario E. Hidden chaperonopathies: alerting physicians and pathologists on the possibility that uncharacteristic, baffling clinical features in otherwise known diseases may be due to failure of the chaperoning system. Life Safety and Security (LiSS) 8.1 53 8(1):189-193, 2020. DOI: 10.12882/2283-7604.2020.8.1
Conway de Macario E, Pitruzzella A, D’Amico AG. Role of molecular chaperones in carcinogenesis: mechanism, diagnosis, and treatment. Editorial. J Oncol. 2020; Volume 2020: Article ID 7437629. Published online 2020 Apr 20. doi:10.1155/2020/7437629. PMCID:PMC7189313. PMID:32377195
https://doi.org/10.1155/2020/7437629
https://www.hindawi.com/journals/jo/2020/7437629/
Basset CA, Cappello F, Rappa F, Lentini VL, Jurjus AR, Conway de Macario E, Macario AJL, Leone A. Molecular chaperones in tumors of salivary glands. J Mol Histol. 2020 Apr 16. doi: 10.1007/s10735-020-09871-y. Review. PMID:32300923.
Caruso Bavisotto C, Alberti G, Vitale AM, Paladino L, Campanella C, Rappa F, Gorska M, Conway de Macario E, Cappello F, Macario AJL, Marino Gammazza A. Hsp60 Post-translational modifications: functional and pathological consequences. Front Mol Biosci. 2020; 7: 95. Published online 2020 Jun 4.doi:10.3389/fmolb.2020.00095. PMCID:PMC7289027. PMID:32582761
https://www.frontiersin.org/articles/10.3389/fmolb.2020.00095/full
Basset CA, Cappello F, Rappa F, Jurjus AA, Conway de Macario E, Macario AJL, Leone A. “Chaperonin Hsp60 and cancer therapies.” In “Heat shock proteins and cancer therapies,” edited by Alexzander A. A. Asea and Dr. Punit Kaur. Volume 21 of the Book Series “Heat Shock Proteins,” edited by Alexzander A. A. Asea and Stuart K. Calderwood, and published by Springer Nature Publishers (Dordrecht, Netherlands), First Online: 23 July 2020; DOI https://doi.org/10.1007/7515_2020_1
https://link.springer.com/chapter/10.1007/7515_2020_1
Marino Gammazza A, Légaré S, Lo Bosco G, Fucarino A, Angileri F, Conway de Macario E, Macario AJL, Cappello F. Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19. Cell Stress Chaperones. 2020 Aug 4:1-5. doi: 10.1007/s12192-020-01148-3. Online ahead of print. PMID:32754823
Vitale AM, Conway de Macario E, Alessandro R, Cappello F, Macario AJL, Marino Gammazza A. Missense mutations of human Hsp60: a computational analysis to unveil their pathological significance. Front Genetics, section Genetics of Common and Rare Diseases. Article type: Original Research. Published on 18 August 2020 Front. Genet. doi: https://doi.org/10.3389/fgene.2020.00969
https://www.frontiersin.org/journals/genetics/sections/genetics-of-common-and-rare-diseases#
https://www.frontiersin.org/articles/10.3389/fgene.2020.00969/full
D’Anneo A, Bavisotto CC, Gammazza AM, Paladino L, Carlisi D, Cappello F, Conway de Macario E, Macario AJL, Lauricella M. Lipid chaperones and associated diseases: a group of chaperonopathies defining a new nosological entity with implications for medical research and practice. Cell Stress Chaperones. 2020 Aug 27. doi: 10.1007/s12192-020-01153-6. Online ahead of print. PMID:32856199 Review.
https://doi.org/10.1007/s12192-020-01153-6
https://link.springer.com/article/10.1007/s12192-020-01153-6
Vitale AM, Santonocito R, Vergilio G, Marino Gammazza A, Campanella C, Conway de Macario E, Bucchieri F, Macario AJL, Caruso Bavisotto C. Brain tumor-derived extracellular vesicles as carriers of disease markers: molecular chaperones and microRNAs. Applied Sciences. 2020; 10(19):6961.
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Marino Gammazza A, Caruso Bavisotto C, Macario AJL. Physiology and pathophysiology of heat shock protein 60. Front Mol Biosci. Editorial article.Front. Mol. Biosci., 30 October 2020 |https://doi.org/10.3389/fmolb.2020.604476 https://www.frontiersin.org/articles/10.3389/fmolb.2020.604476/full https://www.frontiersin.org/research-topics/10435/physiology-and-pathophysiology-of-heat-shock-protein-60#articles
Antona V, Scalia F, Giorgio E, Radio FC, Brusco A, Oliveri M, Corsello G, Lo Celso F, Vadalà M, Conway de Macario E, Macario AJL, Cappello F, Giuffrè M. A novel CCT5 missense variant associated with early onset motor neuropathy. .Int J Mol Sci. 2020 Oct 15;21(20):E7631. doi: 10.3390/ijms21207631.PMID:33076433
Journal: International Journal of Molecular Sciences. Section: Molecular Pathology, Diagnostics, and Therapeutics. Special Issue: Protein Folding Diseases-Molecular Mechanisms and Therapeutic Approaches
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Supplementary data: http://www.mdpi.com/1422-0067/21/20/7631/s1, Table S1: Biochemical data for both mutations. Table S2: Homozygous variants in proband.
Paladino L, Vitale AM, Caruso Bavisotto C, Conway de Macario E, Cappello F, Macario AJL, Marino Gammazza A. The role of molecular chaperones in virus infection and implications for understanding and treating COVID-19. J Clin Med. 2020 Oct 30;9(11):E3518. doi: 10.3390/jcm9113518.PMID:33143379.. https://pubmed.ncbi.nlm.nih.gov/33143379/
Abstract: https://www.mdpi.com/2077-0383/9/11/3518
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Alberti G, Paladino L, Vitale AM, Caruso Bavisotto C, Conway de Macario E, Campanella C, Macario AJL, Marino Gammazza A. Functions and therapeutic potential of extracellular Hsp60, Hsp70, and Hsp90 in neuroinflammatory disorders. Applied Sciences. 2021, 11(2), 736; https://doi.org/10.3390/app11020736
Abstract: https://www.mdpi.com/2076-3417/11/2/736
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Scalia F, Vitale AM, Santonocito R, Conway de Macario E, Macario AJL, Cappello F. The neurochaperonopathies: Anomalies of the chaperone system with pathogenic effects in neurodegenerative and neuromuscular disorders. Applied Sciences. 2021; 11(3):898. https://doi.org/10.3390/app11030898
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David S, Vitale AM, Fucarino F, Scalia F, VergilioG, Conway de Macario E, Macario AJL, Caruso Bavisotto C, Pitruzzella A. The challenging riddle about the Janus-type role of Hsp60 and related extracellular vesicles and miRNAs in carcinogenesis and the promises of its solution. Applied Sciences. 2021; 11(3):1175. https://doi.org/10.3390/app11031175
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Graziano F, Iacopino DG, Cammarata G, Scalia G, Campanella C, Giannone AG, Porcasi R, Florena AM, Conway de Macario E, Macario AJL, Nicoletti GF, Caruso Bavisotto C. The triad Hsp60-miRNAs-Extracellular Vesicles in brain tumors: Assessing its components for understanding tumorigenesis and monitoring patients. Applied Sciences. 2021; 11(6):2867. https://doi.org/10.3390/app11062867
Abstract: https://www.mdpi.com/2076-3417/11/6/2867
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Special Issue: https://www.mdpi.com/journal/applsci/special_issues/exosomal_molecular_chaperones
D’Amico D, Fiore R, Caporossi D, Di Felice V, Cappello F, Dimauro I, Barone R. Function and fiber-type specific distribution of Hsp60 and αB-Crystallin in skeletal muscles: Role of physical exercise. Biology (Basel) 2021 Feb; 10(2):77. Published online 2021 Jan 21. doi:10.3390/biology10020077. PMCID:PMC7911561
Pitruzzella A, Burgio S, Lo Presti P, Ingrao S, Fucarino A, Bucchieri F, Cabibi D, Cappello F, Conway de Macario E, Macario AJL, David S, Rappa F. Hsp60 quantification in human gastric mucosa shows differences between pathologies with various degrees of proliferation and malignancy grade. Applied Sciences. 2021; 11(8):3582. https://doi.org/10.3390/app11083582
Paladino L, Vitale AM, Santonocito R, Pitruzzella A, Cipolla C, Graceffa G, Bucchieri F, Conway de Macario E, Macario AJL, Rappa F. Molecular chaperones and thyroid cancer. Int. J. Mol. Sci. 2021 Apr; 22(8): 4196.Published online 2021 Apr 18. doi:10.3390/ijms22084196. PMCID:PMC8073690.
Burgio S, Conway de Macario E, Macario AJL, Cappello F. SARS-CoV-2 in patients with cancer: possible role of mimicry of human molecules by viral proteins and the resulting anti-cancer immunity. Cell Stress and Chaperones 2021 May 11: 1–6. doi:10.1007/s12192-021-01211-7. PMCID:PMC8112475. https://doi.org/10.1007/s12192-021-01211-7.
Macario AJL, Conway de Macario E. Chaperonins in cancer: Expression, function, and migration in extracellular vesicles. Semin Cancer Biol. 2021 Jun 1:S1044-579X(21)00159-0. doi: 10.1016/j.semcancer.2021.05.029. Online ahead of print. PMID:34087417
https://doi.org/10.1016/j.semcancer.2021.05.029 https://pubmed.ncbi.nlm.nih.gov/34087417/
https://www.sciencedirect.com/science/article/abs/pii/S1044579X21001590?via%3Dihub
Cappello F, Burgio S, Conway de Macario E, Macario A.J.L. Unexpected tumor reduction in metastatic colorectal cancer patients during SARS-Cov-2 infection: effect of ACE-2 expression on tumor cells or molecular mimicry phenomena? Two not mutually exclusive hypotheses. Ther Adv Med Oncol (TAM). 2021, Vol. 13: 1–2. doi:10.1177/17588359211027825 https://doi.org/10.1177/17588359211027825
https://journals.sagepub.com/doi/full/10.1177/17588359211027825
Zummo L, Vitale AM, Caruso Bavisotto C, De Curtis M, Garbelli R, Giallonardo AT, Di Bonaventura C, Fanella M, Conway de Macario E, Cappello F, Macario AJL, Marino Gammazza A. Molecular chaperones and miRNAs in epilepsy: Pathogenic implications and therapeutic prospects. Int J Mol Sci. 2021 Aug; 22(16): 8601. Published online 2021 Aug 10. doi:10.3390/ijms22168601. PMCID: PMC8395327 https://doi.org/10.3390/ijms22168601 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8395327/
Basset CA, Rappa F, Lentini VL, Barone R, Pitruzzella A, Unti E, Cappello F, Conway de Macario E, Macario AJL, Leone A. Hsp27 and Hsp60 in human submandibular salivary gland: Quantitative patterns in healthy and cancerous tissues with potential implications for differential diagnosis and carcinogenesis. Acta Histochem. 2021 Sep;123(6):151771. doi: 10.1016/j.acthis.2021.151771. Epub 2021 Aug 19. PMID:34419757. https://pubmed.ncbi.nlm.nih.gov/34419757/
Alberti G, Campanella C, Paladino L, Porcasi R, Bavisotto CC, Pitruzzella A, Graziano F, Florena AM, Argo A, Conway de Macario E, Macario AJL, Cappello F, Bucchieri F, Barone R, Rappa F. The chaperone system in glioblastoma multiforme and derived cell lines: diagnostic and mechanistic implications. Front Biosci (Landmark Ed). 2022 Mar 15;27(3):97. DOI:10.31083/j.fbl2703097. PMID:35345329. https://www.imrpress.com/journal/FBL/27/3/10.31083/j.fbl2703097/htm
Scalia F, Barone R, Rappa F, Marino Gammazza A, Lo Celso F, Lo Bosco G, Barone G, Antona V, Vadalà M, Vitale AM, Mangano GD, Amato D, Sentiero G, Macaluso F, Myburgh KH, Conway de Macario E, Macario AJL, Giuffrè M, Cappello F. Muscle histopathological abnormalities in a patient with a CCT5 mutation predicted to affect the apical domain of the chaperonin subunit. Front Mol Biosci. 2022 Jun 2;9:887336. DOI:10.3389/fmolb.2022.887336. eCollection 2022. PMID:35720129. PMCID:PMC9201415. https://pubmed.ncbi.nlm.nih.gov/35720129/
Alberti G, Vergilio G, Paladino L, Barone R, Cappello F, Conway de Macario E, Macario AJL, Bucchieri F, Rappa F. The Chaperone System in breast cancer: Roles and therapeutic prospects of the molecular chaperones Hsp27, Hsp60, Hsp70, and Hsp90. Int J Mol Sci. 2022 Jul 14;23(14):7792. DOI:10.3390/ijms23147792. PMID:35887137. PMCID:PMC9324353 https://doi.org/10.3390/ijms23147792
Basset CA, Rappa F, Barone R, Florena AM, Porcasi R, Conway de Macario E, Macario AJL, Leone A. The Chaperone System in salivary glands: Hsp90 prospects for differential diagnosis and treatment of malignant tumors. Int J Mol Sci. 2022 Aug 18;23(16):9317. DOI:10.3390/ijms23169317. PMID:36012578. https://doi.org/10.3390/ijms23169317
Scalia F, Lo Bosco G, Paladino L, Vitale AM, Noori L, Conway de Macario E, Macario AJL, Bucchieri F, Cappello F, Lo Celso F. Structural and dynamic disturbances revealed by molecular dynamics simulations predict the impact on function of CCT5 chaperonin mutations associated with rare severe distal neuropathies. Int J Mol Sci. 2023 Jan 19;24(3):2018. DOI:10.3390/ijms24032018. PMID:36768350. PMCID:PMC9917133 https://pubmed.ncbi.nlm.nih.gov/36768350/
Burko P, D’Amico G, Miltykh I, Scalia F, Conway de Macario E, Macario AJL, Giglia G, Cappello F, Caruso Bavisotto C. Molecular pathways implicated in radioresistance of glioblastoma multiforme: What is the role of extracellular vesicles? Int J Mol Sci. 2023 Mar 2;24(5):4883. DOI:10.3390/ijms24054883. PMID:36902314. PMCID:PMC10003080. https://pubmed.ncbi.nlm.nih.gov/36902314/
Basset CA, Conway de Macario E, Leone LG, Macario AJL, Leone A. The chaperone system in cancer therapies: Hsp90. J Mol Histol. 2023 Apr;54(2):105-118. DOI:10.1007/s10735-023-10119-8. Epub 2023 Mar 18. PMID:36933095. PMCID:PMC10079721 https://pubmed.ncbi.nlm.nih.gov/36933095/. https://link.springer.com/article/10.1007/s10735-023-10119-8
Paladino L, Santonocito R, Graceffa G, Cipolla C, Pitruzzella A, Cabibi D, Cappello F, Conway de Macario E, Macario AJL, Bucchieri F, Rappa F. Immunomorphological patterns of chaperone system components in rare thyroid tumors with promise as biomarkers for differential diagnosis and providing clues on molecular mechanisms of carcinogenesis. Cancers (Basel) 2023 Apr;15(8): 2403. Published online 2023 Apr 21. doi:10.3390/cancers15082403. PMC10136750.
Scalia F, Conway de Macario E, Bonaventura G, Cappello F, Macario AJL. Histopathology of skeletal muscle in a distal motor neuropathy associated with a mutant CT5 subunit: Clues for future developments to improve differential diagnosis and personalized therapy. Biology 2023, 12 (15), 641. https://doi.org/10.3390/biology12050641 biology12050641. https://www.mdpi.com/2079-7737/12/5/641/htm
Caruso Bavisotto C, Cappello C, Conway de Macario E, Macario AJL, Rappa F. Immunohistochemistry of human Hsp60 in health and disease: Recent advances in immuno-morphology and methods for assessing the chaperonin in extracellular vesicles. In: Calderwood, S.K. and Prince, T.L. (editors) Chaperones: Methods and Protocols, Methods in Molecular Biology (MiMB), Volume 2693. Chapter 20, pp. 263-279. Springer Nature 2023 https://doi.org/10.1007/978-1-0716-3342-7_20
Macario AJL, Conway de Macario E. The chaperone system in autoimmunity, inflammation, and virus-induced diseases: Role of chaperonins. In: Fink, G. (ed) Stress: Immunology and Inflammation. Handbook of Stress Series, Volume 5. Chapter 13. Elsevier/Academic Press, San Diego, CA USA, pp. 119-128, 2023. https://shop.elsevier.com/books/stress-immunology-and-inflammation/fink/978-0-12-817558-3
Paladino L, Rappa F, Barone R, Macaluso F, Zummo FP, David S, Szychlinska MA, Bucchieri F, Conway de Macario E, Macario AJL, Cappello F, Marino Gammazza A. NF-kB regulation and the Chaperone System mediate restorative effects of the probiotic Lactobacillus fermentum LF31 in the small intestine and cerebellum of mice with ethanol-induced damage. Biology (Basel) 2023 Nov; 12(11): 1394. Published online 2023 Nov 1. doi:10.3390/biology12111394. PMID:37997993. PMCID:PMC10669058 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10669058/
Basset CA, Hussein IH, Jurjus AR, Cappello F, Conway de Macario E, Macario AJL, Leone A. The chaperone Hsp90, a key player in salivary gland tumorigenesis. Appl. Biosci. 2023, 2(4), 607-616; https://doi.org/10.3390/applbiosci2040038
Noori L, Saqagandomabadi V, Di Felice V, David S, Caruso Bavisotto C, Bucchieri F, Cappello F, Conway de Macario E, Macario AJL, Scalia F. Putative roles and therapeutic potential of the Chaperone System in Amyotrophic Lateral Sclerosis and Multiple Sclerosis. Cells. 2024 Jan 24;13(3):217. DOI:10.3390/cells13030217. PMID:38334609. PMCID:PMC10854686 https://pubmed.ncbi.nlm.nih.gov/38334609/ https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10854686/
Alberti G, Sánchez-López CM, Marcilla A, Barone R, Caruso Bavisotto C, Graziano F, Conway de Macario E, Macario AJL, Bucchieri F, Cappello F, Campanella C, Rappa F. Hsp70 and Calcitonin Receptor Protein in Extracellular Vesicles from Glioblastoma Multiforme: Biomarkers with putative roles in carcinogenesis and potential for differentiating tumor types. Int J Mol Sci. 2024 Mar 18;25(6):3415. doi:10.3390/ijms25063415. PMID: 38542389; PMCID: PMC10969952. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10969952/
Vitale AM, Paladino L, Caruso Bavisotto C, Barone R, Rappa F, Conway de Macario E, Cappello F, Macario AJL, Marino Gammazza A. Interplay between the Chaperone System and gut microbiota dysbiosis in Systemic Lupus Erythematosus pathogenesis: Is molecular mimicry the missing link between those two factors?. Int J Mol Sci. 2024Jun; 25(11): 5608. Publishedonline 2024May 21. doi:10.3390/ijms25115608. PMID:38891798. PMCID: PMC11171487. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11171487/
C. Web talks.
Cappello, F. and Macario, A.J.L. (2012). Mitochondrial chaperonin Hsp60: locations, functions and pathology. The Biomedical & Life Sciences Collection, Henry Stewart Talks Ltd, London (online at http://hstalks.com/bio). Direct talk access links:
http://hstalks.com/lib.php?t=HST142.3142&c=252;
http://hstalks.com/?t=BL1423142-Macario
Macario, A.J.L. (2014). The chaperonopathies: Diseases with defective molecular chaperones. Meeting: STRESS, PATOLOGIE CORRELATE E LORO TERAPIA, 26 maggio 2014, Sala Martorana, Palazzo Comitini, Palermo, Italy. May 26, 2014.
https://www.youtube.com/watch?v=dl8ySsIyBSQ
Cappello, F. and Macario, A.J.L. UPDATE 2021. Mitochondrial chaperonin Hsp60: locations, functions and pathology [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved June 22, 2021, from https://hstalks.com/bs/2231/.