Document Detail


Novel variants of muscle calpain 3 identified in human melanoma cells: cisplatin-induced changes in vitro and differential expression in melanocytic lesions.
MedLine Citation:
PMID:  19386580     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Calpains are cysteine proteases comprising members ubiquitously expressed in human tissues and other tissue-specific isoforms. Alterations of calpain 3 (p94), the muscle-specific isoform that contains three peculiar sequences (NS, IS1 and IS2), are strictly associated to the limb-girdle muscular dystrophy type 2A, in which a myonuclear apoptosis has been documented. Our recent demonstration of a proapoptotic role of ubiquitous calpains in drug-induced apoptosis of melanoma cells prompted us to investigate the expression of calpain 3 in human melanoma cell lines undergoing apoptosis and in melanocytic lesions. In melanoma cell lines, we have identified two novel splicing variants of calpain 3 (hMp78 and hMp84): they have an atypical initiation exon and a putative nuclear localization signal, the shorter one lacks IS1 inset and both proteins are extremely unstable. Virtually, both isoforms (prevalently as cleavage forms) are localized in cytoplasm and in nucleoli. In cisplatin-treated preapoptotic cells, an increase of both transcription and autoproteolytic cleavage of the novel variants is observed; the latter event is prevented by the inhibitor of ubiquitous calpains, calpeptin, which is also able to protect from apoptosis. Interestingly, among melanocytic lesions, the expression of these novel variants is significantly downregulated, compared with benign nevi, in the most aggressive ones, i.e. in vertical growth phase melanoma and, even more, in metastatic melanoma cells, characterized by invasiveness properties and usually highly resistant to apoptosis. On the whole, our observations suggest that calpain 3 variants can play a proapoptotic role in melanoma cells and its downregulation, as observed in highly aggressive lesions, could contribute to melanoma progression.
Authors:
D Moretti; B Del Bello; E Cosci; M Biagioli; C Miracco; E Maellaro
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-04-21
Journal Detail:
Title:  Carcinogenesis     Volume:  30     ISSN:  1460-2180     ISO Abbreviation:  Carcinogenesis     Publication Date:  2009 Jun 
Date Detail:
Created Date:  2009-06-04     Completed Date:  2009-06-26     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008055     Medline TA:  Carcinogenesis     Country:  England    
Other Details:
Languages:  eng     Pagination:  960-7     Citation Subset:  IM    
Affiliation:
Department of Physiopathology, Experimental Medicine and Public Health, University of Siena, Italy.
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MeSH Terms
Descriptor/Qualifier:
Alternative Splicing
Antineoplastic Agents / pharmacology*
Apoptosis
Biopsy
Calpain / antagonists & inhibitors,  metabolism*
Cell Line, Tumor
Cell Nucleolus / metabolism
Cisplatin / pharmacology*
Cytoplasm / metabolism
Dipeptides / pharmacology
Dysplastic Nevus Syndrome / metabolism
Gene Expression Regulation, Neoplastic
Humans
Melanoma / metabolism*,  pathology
Muscle Proteins / antagonists & inhibitors,  metabolism*
Neoplasm Metastasis
Nevus / metabolism*
RNA, Messenger / metabolism
Skin Neoplasms / metabolism*,  pathology
Chemical
Reg. No./Substance:
0/Antineoplastic Agents; 0/Dipeptides; 0/Muscle Proteins; 0/RNA, Messenger; 117591-20-5/calpeptin; 15663-27-1/Cisplatin; EC 3.4.22.-/CAPN3 protein, human; EC 3.4.22.-/Calpain

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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