The inflammatory mediators prostaglandin E2 (PGE2) and interleukin‐1β (IL‐1β) play critical roles in the inflammatory process leading to alveolar bone and connective tissue loss in periodontal disease. Data from a previously published 6‐month clinical study demonstrated that twice daily use of 0.1% ketorolac tromethamine oral rinse prevented alveolar bone loss in adults with periodontitis. We further analyzed data from this study to examine the relationship between PGE2, IL‐1β and bone loss. Patient mean PGE2, and IL‐1β levels in gingival crevicular fluid (M‐GCF) measured throughout the course of the study were directly compared to the maximum amount of alveolar bone height loss observed at a single study site in each patient. The maximum amount of bone loss measured was chosen for the analysis since the pattern of bone loss was clearly episodic in nature. A statistically significant correlation (r = 0.73, p = 0.001) exists between M‐GCF PGE2 concentration and the maximum amount of bone height lost at individual patient study sites. The correlation between M‐GCF IL‐1β concentration and maximum bone height lost is also statistically significant (r = 0.66, p = 0.005). Over the 6‐month duration of the study, both PGE, and IL‐1β were coordinately expressed in the placebo treatment group as reflected in the significant correlation between M‐GCF concentrations of the 2 mediators (r=0.81, p<0.001). Treatment of patients with 0.1% ketorolac tromethamine twice daily for 6 months resulted in reductions of PGE, in GCF and a negligible correlation between M‐GCF PGE, and M‐GCF IL‐1β (r=0.42, p=0.088). This lack of a strong association between the 2 mediators in the ketorolac treatment group provides a direct biochemical readout of the anti‐inflammatory efficacy of ketorolac tromethamine oral rinse in patients with periodontitis. Further studies are warranted to determine the full diagnostic potential of M‐GCF levels of PGE2, and IL‐1β for predicting risk of alveolar bone loss in patients with periodontitis and monitoring periodontal therapy effectiveness.

SummaryThe proposal that thrombospondin is the endogenous platelet lectin was evaluated using antisera and monoclonal antibodies to thrombospondin. The platelet-bound hemagglutinin activity of human platelets stimulated with A23187 was inhibited by rabbit anti-thrombospondin sera and by a monoclonal anti-thrombospondin IgG. A second monoclonal IgG did not inhibit platelet- bound agglutinin activity. Preparations of purified platelet thrombospondin differed in their hemagglutination activities. The hemagglutination activity of an active preparation of thrombospondin was inhibited by the monoclonal antibody that inhibited platelet-bound lectin activity. The hemagglutination activity of an almost inactive preparation of thrombospondin was enhanced by the anti-thrombospondin monoclonal antibody that did not block platelet-bound lectin activity. The results demonstrate that expression of the platelet-bound form of the endogenous lectin is thrombospondin-dependent and suggest that thrombospondin must become part of a larger complex, either by binding to the platelet surface or by becoming aggregated in solution, before hemagglutination activity can be expressed.