CAPPELLO, Francesco

ZUMMO, Giovanni

Archivio istituzionale della ricerca - Università di Palermo

ARTICLE IN PRESS0344-0338/$ - sedoi:10.1016/j.prPathology – Research and Practice 202 (2006) 401–402www.elsevier.de/prpLETTER TO THE EDITORHSP60 expression during carcinogenesis: Where is thepilot?Dear Editor,I have read with much interest the article of Mori etal. [9], who used cDNA microarray and immunohisto-chemical techniques to investigate the expression of fourupregulated genes in colorectal cancers, with HSP60among them. In particular, they showed that HSP60 isoverexpressed in the cytoplasm of neoplastic cells, thatits intensity is stronger in deep invasive area than insuperﬁcial ones, and that carcinomas show strongerimmunoreactivity than adenomas. They provided datathat are in agreement with our previous results [1]. Morerecently, we also showed that the expression of HSP60in primary tumor and lymph node metastasis iscorrelated with tumor grade [3], conﬁrming indepen-dently the results of Mori et al.In the past, we reported an analogous HSP60 over-expression also in exocervical and prostatic carcinomas[2,5]. Nevertheless, other authors [8] demonstratedthat HSP60 could also be downregulated duringcarcinogenesis, especially the vesical one. We conﬁrmedthese data in a large series of bladder transitional cellcarcinomas of different grade and stage (unpublisheddata).Moreover, we recently reported that HSP60 down-regulation may be a novel biomarker during bronchialcarcinogenesis [4]. Indeed, we analyzed a series of lungbiopsies from smokers, and showed that normal andhyperplastic mucosae displayed cytoplasmic HSP60expression in most of the epithelial cells, while onlyfew epithelial elements of patients with squamousmetaplasia showed the presence of HSP60 in epithelialcells, and its positivity completely disappeared indysplastic and tumor specimens.In this letter, we would like to express our opinion:Currently, it is unlikely to conﬁrm that HSP60 over-expression is correlated with cancer development andprogression, because it seems to depend on the site oforigin of the neoplasm. We presume that the discre-pancy of HSP60 expression during carcinogenesis maybe due to its pro- and anti-apoptotic roles in tumor cellse front matter r 2006 Elsevier GmbH. All rights reserved.p.2006.02.002[6,7], and we hypothesize that its levels are dependent onthe expression of other proteins involved in theactivation of the apoptotic pathway.In conclusion, a better knowledge of the molecularpathways, including HSP60 expression during carcino-genesis, will probably expand our prognostic tools andtherapeutic targets in the treatment of cancer.References[1] F. Cappello, M. Bellaﬁore, A. Palma, S. David, V.Marciano, T. Bartolotta, C. Sciume, G. Modica, F. Farina,G. Zummo, F. Bucchieri, 60 kDa chaperonin (HSP60) isover-expressed during colorectal carcinogenesis, Eur. J.Histochem. 47 (2003) 105–110.[2] F. Cappello, M. Bellaﬁore, A. Palma, V. Marciano, G.Martorana, P. Belﬁore, A. Martorana, F. Farina, G.Zummo, F. Bucchieri, Expression of 60-kD heat shockprotein increases during carcinogenesis in the uterineexocervix, Pathobiology 70 (2002–2003) 83–88.[3] F. Cappello, S. David, F. Rappa, F. Bucchieri, L. Marasa,T.E. Bartolotta, F. Farina, G. Zummo, The expression ofHSP60 and HSP10 in large bowel carcinomas with lymphnode metastase, BMC Cancer 5 (2005) 139.[4] F. Cappello, A. Di Stefano, S.E. D’Anna, C.F. Donner, G.Zummo, HSP60 immunopositivity as a novel biomarker ofbronchial carcinogenesis, Lancet Oncol. 6 (2005) 816.[5] F. Cappello, F. Rappa, S. David, R. Anzalone, G.Zummo, Immunohistochemical evaluation of PCNA,p53, HSP60, HSP10 and MUC-2 presence and expressionin prostate carcinogenesis, Anticancer Res. 23 (2003)1325–1331.[6] V. Di Felice, S. David, F. Cappello, F. Farina, G. Zummo,Is chlamydial heat shock protein 60 a risk factor foroncogenesis?, Cell. Mol. Life Sci. 62 (2005) 4–9.[7] A. Faried, M. Sohda, M. Nakajima, T. Miyazaki, H. Kato,H. Kuwano, Expression of heat-shock protein Hsp60correlated with the apoptotic index and patient prognosisin human oesophageal squamous cell carcinoma, Eur. J.Cancer 40 (2004) 2804–2811.[8] T. Lebret, R.W. Watson, V. Molinie, A. O’Neill, C.Gabriel, J.M. Fitzpatrick, H. Botto, Heat shock proteinsHSP27, HSP60, HSP70, and HSP90: expression in bladdercarcinoma, Cancer 98 (2003) 970–977.ARTICLE IN PRESSLETTER TO THE EDITOR / Pathology – Research and Practice 202 (2006) 401–402402[9] D. Mori, Y. Nakafusa, K. Miyazaki, O. Tokunaga,Differential expression of Janus kinase 3 (JAK3), matrixmetalloproteinase 13 (MMP13), heat shock protein 60(HSP60), and mouse double minute 2 (MDM2) in humancolorectal cancer progression using human cancer cDNAmicroarrays, Pathol. Res. Pract. 201 (2005) 777–789.Francesco Cappello, Giovanni ZummoDepartment of Experimental Medicine, Section of HumanAnatomy, University of Palermo, Via del Vespro 129,90127 Palermo, ItalyE-mail address: francapp@hotmail.com (F. Cappello)

HSP60 expression during carcinogenesis: where is the pilot?

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HSP60 expression during carcinogenesis: where is the pilot?

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Archivio istituzionale della ricerca - Università di Palermo