WISP-3 functions as a ligand and promotes superoxide dismutase activity

Biochem Biophys Res Commun. 2006 Mar 31;342(1):259-65. doi: 10.1016/j.bbrc.2006.01.132. Epub 2006 Feb 3.

Abstract

WISP-3 (Wnt1 inducible secreted protein-3) mutations have been linked to the connective tissue diseases progressive pseudorheumatoid dysplasia and polyarticular juvenile idiopathic arthritis, both of which are accompanied by disorders in cartilage maintenance/homeostasis. The molecular mechanism of WISP-3 mediated effects in the sustenance of cartilage has not been described in detail. Our previous study illustrates the potential role of WISP-3 in regulating the expression of cartilage-specific molecules that sustain chondrocyte growth and cartilage integrity. The present study was conducted to investigate the mode of action of WISP-3 in greater detail. Experimental results depicted here suggest that WISP-3 can function as a ligand and signal via autocrine and/or paracrine modes upon being secreted by chondrocytes. Furthermore, apart from regulating collagen II and aggrecan expression, WISP-3 may also promote superoxide dismutase expression and activity in chondrocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CCN Intercellular Signaling Proteins
  • Cell Line
  • Chondrocytes / drug effects
  • Chondrocytes / metabolism
  • Humans
  • Insulin-Like Growth Factor Binding Proteins / genetics
  • Insulin-Like Growth Factor Binding Proteins / isolation & purification
  • Insulin-Like Growth Factor Binding Proteins / metabolism*
  • Ligands
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / isolation & purification
  • Neoplasm Proteins / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / pharmacology
  • Superoxide Dismutase / metabolism*
  • Up-Regulation / drug effects

Substances

  • CCN Intercellular Signaling Proteins
  • CCN6 protein, human
  • Insulin-Like Growth Factor Binding Proteins
  • Ligands
  • Neoplasm Proteins
  • Recombinant Proteins
  • Superoxide Dismutase