Protein phosphorylation and metalloproteinase synthesis by lapine articular chondrocytes

K. I. Hulkower, Christopher H Evans

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Interleukin 1 (IL-1) increases the synthesis of neutral metalloproteinases (NMP) and prostaglandin E2 (PGE2) by primary monolayer cultures of lapine articular chondrocytes. Two-dimensional gel electrophoresis of 32P-labelled cells confirmed that IL-1 strongly altered the pattern of phosphorylated proteins in chondrocytes. This presumably reflects modulation of the activities of protein phosphatases, kinases or both. Despite considerable experimental effort, it proved impossible to implicate activation of protein kinase C (PKC) in the responses of these cells to IL-1. Additional evidence appears also to eliminate protein kinases activated by cyclic AMP and Ca2+/calmodulin. Moreover, recent data further suggest that the 80 kDa IL-1 receptor is not a protein kinase. These findings increase the likelihood that a novel kinase is involved in IL-1 signalling in chondrocytes, as proposed previously for fibroblasts.

Original languageEnglish (US)
Pages (from-to)110-113
Number of pages4
JournalJournal of Rheumatology
Volume18
Issue numberSUPPL. 27
StatePublished - 1991
Externally publishedYes

Fingerprint

Metalloproteases
Chondrocytes
Interleukin-1
Joints
Phosphorylation
Protein Kinases
Proteins
Interleukin-1 Receptors
Phosphoprotein Phosphatases
Electrophoresis, Gel, Two-Dimensional
Calmodulin
Dinoprostone
Cyclic AMP
Protein Kinase C
Phosphotransferases
Fibroblasts

Keywords

  • Chondrocyte
  • Interleukin 1
  • Neutral metalloproteinase
  • Protein kinase
  • Protein phosphorylation

ASJC Scopus subject areas

  • Immunology
  • Medicine(all)
  • Rheumatology

Cite this

Protein phosphorylation and metalloproteinase synthesis by lapine articular chondrocytes. / Hulkower, K. I.; Evans, Christopher H.

In: Journal of Rheumatology, Vol. 18, No. SUPPL. 27, 1991, p. 110-113.

Research output: Contribution to journalArticle

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