Abstract | PURPOSE OF REVIEW: RECENT FINDINGS:
Dermcidin has recently been shown to act as a survival/proliferation factor in hepatoma and prostate cancer cell lines. Recent studies suggest that the Y-P30 subunit of the dermcidin polypeptide offers a survival advantage in such cancer cells. Nevertheless, the relevance of Y-P30 to cancer growth in vivo, and mechanisms of action remain unknown. In mice, tumour cells appear to glycosylate the Y-P30 subunit, transforming it into a potent skeletal muscle proteolysis-inducing factor. Recent work has described a receptor and signal transduction pathways for murine glycosylated proteolysis-inducing factor. The absence of classical N-glycosylation sites in the human proteolysis-inducing factor peptide and the lack of specific tools for the detection of the key carbohydrate moieties conferring the proteolysis-inducing activity, however, remain barriers to confirming glycosylated proteolysis-inducing factor as a pro-cachectic factor in humans. SUMMARY: There is a growing body of evidence illustrating dermcidin as an oncogene and Y-P30 as a survival factor. The biology of murine proteolysis-inducing factor as a pro-cachectic factor continues to evolve; however, its role in human biology remains speculative.
|
Authors | Grant D Stewart, Richard Je Skipworth, James A Ross, Kenneth Ch Fearon, Vickie E Baracos |
Journal | Current opinion in clinical nutrition and metabolic care
(Curr Opin Clin Nutr Metab Care)
Vol. 11
Issue 3
Pg. 208-13
(May 2008)
ISSN: 1363-1950 [Print] England |
PMID | 18403914
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
|
Chemical References |
- Peptides
- Proteoglycans
- dermcidin
- proteolysis-inducing peptide
|
Topics |
- Animals
- Cachexia
(genetics, metabolism)
- Cell Survival
- Gene Expression Regulation, Neoplastic
- Glycosylation
- Humans
- Neoplasms
(genetics)
- Peptides
(genetics, metabolism, physiology)
- Proteoglycans
(genetics, metabolism, physiology)
- Tumor Cells, Cultured
|