A high molecular weight collagenase inhibitor made by rabbit chondrocytes in cell culture

Matrix. 1989 Mar;9(2):127-34. doi: 10.1016/s0934-8832(89)80030-7.

Abstract

A new, high molecular weight (66,000 daltons) inhibitor of collagenase (LCI) has been isolated and partially characterized. It accounted for 20% of the collagenase-inhibitory activity in the supernatants of rabbit chondrocytes cultured in 10% acid-treated fetal bovine serum (ATFBS). LCI was stable to 60 degrees C and sensitive to reduction and alkylation. Unlike a low molecular weight collagenase inhibitor, similar to Tissue Inhibitor of Metallo-Proteinases (TIMP), it did not bind to concanavalin A-Sepharose 4B.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cartilage / cytology
  • Cartilage / enzymology*
  • Cells, Cultured
  • Enzyme Inhibitors / isolation & purification*
  • Microbial Collagenase / metabolism*
  • Molecular Weight
  • Rabbits

Substances

  • Enzyme Inhibitors
  • Microbial Collagenase