Molecular characterization of plasminogen activator in human supragingival plaque.
Extravascular participation of the serine protease plasminogen activator (PA) in tissue remodelling and cell migration may be relevant in the regulation of periodontal homeostasis and the pathogenesis of periodontal disease. The molecular nature of authentic PA in crevicular fluid has been characterized, and this study has sought to determine whether human supragingival plaque also contains PA; if so, of which molecular species and from what source. Thirty samples of supragingival plaque plaque from 10 individuals, extensively washed to remove adherent saliva, were all found by substrate analysis to have tissue-type PA (tPA) activity. Unstimulated parotid or mixed saliva also showed tPA activity, but submandibular saliva had no measurable PA activity. Freshly isolated plaque microbes cultured under aerobic or anaerobic conditions contained no PA activity (preliminary investigation). PA activity was restricted to individual epithelial cells suggesting that the origin of PA activity in human supragingival plaque is in part from plaque-adherent epithelial cells.
Schmid
J
J
Center for Research in Periodontal Diseases and Oral Molecular Biology, University of Illinois, Chicago 60612.
Chambers
D A
DA
D000328:Adult; D003773:Dental Plaque / Q000032:analysis*; D005260:Female; D005342:Fibrinolysis; D006801:Humans; D008297:Male; D008856:Microscopy, Fluorescence; D008858:Microscopy, Phase-Contrast; D012463:Saliva / Q000032:analysis; D010959:Tissue Plasminogen Activator / Q000032:analysis*
D010959:Tissue Plasminogen Activator