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Phospholipase A 2 in rat gingival tissue
Author(s) -
Shinohara H.,
Ishida H.,
Fernandezf E. J.,
Amabe Y.,
Nagata T.,
Wakano Y.
Publication year - 1992
Publication title -
journal of periodontal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.31
H-Index - 83
eISSN - 1600-0765
pISSN - 0022-3484
DOI - 10.1111/j.1600-0765.1992.tb01827.x
Subject(s) - phospholipase a2 , periodontitis , enzyme , chemistry , gingivitis , rheumatoid arthritis , pathogenesis , phosphatidylethanolamine , proinflammatory cytokine , cytosol , synovial fluid , phospholipase , tissue transglutaminase , substrate (aquarium) , enzyme assay , phosphatidylcholine , phospholipase a , biochemistry , phospholipid , immunology , medicine , inflammation , pathology , biology , dentistry , ecology , osteoarthritis , alternative medicine , membrane
Phospholipase A 2 (PLA 2 ) is a proinflammatory enzyme in the synovial fluids of all ‐ and sera of some ‐ patients with rheumatoid arthritis. Due to the similarities in pathogenesis between rheumatoid arthritis and periodontitis, we sought to study the enzymatic properties of PLA 2 in periodontal tissue. In this study, we demonstrated PLA 2 activity in rat gingival tissue, about 80% of which was present in the cytosolic fraction. We characterized the cytosolic PLA 2 enzyme with respect to substrate specificity, sensitivity to detergent, Ca 2+ ion dependency and optimum pH. We found that phosphatidylethanolamine, rather than phosphatidylcholine, was the preferred substrate, the Ca 2+ ion was essential for the expression of PLA 2 activity, the enzyme was active over a broad pH range, with the optimum at pH 9.0, and sodium‐deoxycholate inhibited the enzyme activity strongly in a concentration‐dependent manner. These results are consistent with those which have been obtained with synovial fluid PLA 2 and suggest that gingival PLA 2 may be involved in the pathogenic processes of gingivitis and periodontitis.