Calmodulin-dependent collagenase and proteoglycanase activities in chondrocytes from human osteoarthritic cartilage

• Published in: Biochemical and biophysical research communications Vol. 174; no. 3; pp. 1204 - 1207
• Main Authors: Richard, M., Broquet, P., Vignon, E., Peschard, M.J., Carret, J.P., Louisot, P.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 14.02.1991; Elsevier
• Subjects: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine; Calmodulin - antagonists & inhibitors; Calmodulin - physiology; Cartilage, Articular - enzymology; Exact sciences and technology; Humans; In Vitro Techniques; Isoquinolines - pharmacology; Kinetics; Mathematical analysis; Mathematics; Microbial Collagenase - metabolism; Middle Aged; Osteoarthritis - enzymology; Piperazines - pharmacology; Potential theory; Protein Kinase C - antagonists & inhibitors; Sciences and techniques of general use; Sulfonamides - pharmacology; Trifluoperazine - pharmacology; W-7; H-7; W-5; TFP; Human; Cell culture; Chondrocyte; Radiolabelling; Enzyme; Arthritis; Collagenase; Neutral proteinase; Binding protein; Enzymatic activity; Articular cartilage; Kinetic parameter; Calmodulin
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(91)91549-R

Chondrocyte metalloproteinases appear to play a major role in the development of osteoarthritis. The intracellular post-traductional mechanisms regulating collagenase and proteoglycanase are not known. Calmodulin antagonists including phenothiazine and sulfonamide derivatives significantly increased proteoglycanase activity and decreased collagenase activity. H-7, a specific inhibitor of protein kinase C, had no effect on the two metalloproteinase activities, and calmodulin was ineffective in in vitro assays upon metalloproteinase activities. We postulate that collagenase and proteoglycanase activities are controlled by calmodulin-dependent regulation.