Effect of ascorbic acid on prolyl hydroxylase activity, collagen hydroxylation and collagen synthesis in human synovial cells in culture
Kuttan, R.; Parrott, D.P.; Kaplan, S.R.; Fuller, G.C.
Research Communications in Chemical Pathology and Pharmacology 26(2): 337-345
1979
ISSN/ISBN: 0034-5164 PMID: 230553 Document Number: 145888
Synovial cells derived from patients with either rheumatoid arthritis, or simple joint-trauma were grown in tissue culture. The rheumatoid osteoarthritic and non-arthritic synovial cells in cultured all had similar levels of prolyl hydroxylase activity. Following a 3 hour incubation with ascorbate (10(-4)M), prolyl hydroxylase activity was elevated to a similar extent in all synovial cell cultures examined. The activation of prolyl hydroxylase by ascorbate (10(-4)M) was accompanied by increased radioactive hydroxyproline formation and secretion into the media. Increased amounts of collagenase degradable radioactive protein were also secreted into the media, but no changes in total collagen synthesis (media plus cell layer) were observed as a result of ascorbate supplementation using this assay system.