The dermcidin gene in cancer: role in cachexia, carcinogenesis and tumour cell survival

Curr Opin Clin Nutr Metab Care. 2008 May;11(3):208-13. doi: 10.1097/MCO.0b013e3282fb7b8d.

Abstract

Purpose of review: The diverse protein products of the dermcidin gene are relevant to immunity, cancer cell progression and cancer cachexia. This article evaluates recent developments/controversies around dermcidin.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cachexia / genetics*
  • Cachexia / metabolism
  • Cell Survival
  • Gene Expression Regulation, Neoplastic*
  • Glycosylation
  • Humans
  • Neoplasms / genetics*
  • Peptides / genetics*
  • Peptides / metabolism
  • Peptides / physiology
  • Proteoglycans / genetics*
  • Proteoglycans / metabolism
  • Proteoglycans / physiology
  • Tumor Cells, Cultured

Substances

  • Peptides
  • Proteoglycans
  • dermcidin
  • proteolysis-inducing peptide