alpha-chymotrypsin and Gingivitis

Serine proteinases have the potential to influence the degradation of connective tissue in chronic periodontitis, which may progress episodically at individual tooth sites. Elastase-, chymotrypsin- and tryptase-like proteinase activity in homogenized gingival tissue were measured using, respectively, the selective peptide substrates MeOSuc-Ala-Ala-Pro-Val-AFC. MeOSuc-Phe-Pro-Phe-AFC and Z-Ala-Arg-Arg-AFC. Each tooth site was assayed separately and divided, where appropriate, into gingival tissue and granulomata. Elastase-like activity was detected in only about half of the sites and with large variations. Chymotrypsin-like activity decreased with increasing pocket depth, clinical attachment level, gingival index and gingival bleeding index. Tryptase-like activity did not vary consistently with clinical measures. Chymotrypsin- and tryptase-like proteinase activity were much higher in gingival tissue than in granulomata. These effects are best explained by the likely influence (or lack of influence) of the endogenous serum and tissue inhibitors of serine proteinases, the different cellular origins of the enzymes, and their relative affinities for their substrates.

Topics: Adult; Chronic Disease; Chymotrypsin; Female; Gingiva; Gingival Pocket; Gingivitis; Granuloma; Humans; Male; Middle Aged; Pancreatic Elastase; Peptide Hydrolases; Periodontal Index; Periodontitis; Serine Endopeptidases

These activities were measured simultaneously, using synthetic fluorescent protease substrates, in gingival crevicular fluid collected at 6 pre-determined sites from 10 individuals with mild to moderate gingivitis. The three enzyme activities were detected in 85, 18 and 93% of the sites, respectively. The volume of fluid collected from discrete sites was significantly correlated with the total amount of substrate hydrolysed, but not with the specific rate of substrate hydrolysis. Log10 (total trypsin-like activity) was significantly correlated with the Gingival Index, Plaque Index and probing depth (r = 0.319, 0.423 and 0.336), while total glycylprolyl dipeptidase activity was significantly correlated with probing depth (r = 0.381). These findings add to knowledge of the biochemistry of gingival crevicular fluid, but the usefulness of such assays for diagnostic or monitoring purposes in periodontal diseases needs to be determined.

Topics: Adult; Chymotrypsin; Dental Plaque Index; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; Female; Gingival Crevicular Fluid; Gingival Hemorrhage; Gingival Pocket; Gingivitis; Humans; Male; Periodontal Index; Trypsin

Tissues from twenty-four patients with focal hyperplastic gingival lesions containing calcification were stained for lysozyme (muramidase), alpha-1-antitrypsin, and alpha-1-antichymotrypsin. In eighteen of the twenty-four cases the tissues stained positively for lysozyme, and in all instances the tissues stained positively for alpha-1-antitrypsin and alpha-1-antichymotrypsin. These data suggest that the fibrous components of these lesions are derived from tissue histiocytes.

Topics: alpha 1-Antichymotrypsin; alpha 1-Antitrypsin; Calcinosis; Chymotrypsin; Gingival Hyperplasia; Gingivitis; Histiocytes; Histocytochemistry; Humans; Immunochemistry; Muramidase; Odontogenic Tumors

Topics: Alveolar Process; Angiography; Anti-Inflammatory Agents; Arteriosclerosis; Arteriovenous Anastomosis; Capillary Permeability; Chymotrypsin; Endarteritis; Gingiva; Gingivitis; Humans; Maxillary Artery; Periodontal Diseases; Periodontium; Plethysmography; Protein Deficiency; Sodium Isotopes; Trypsin; Vascular Diseases

Topics: Administration, Topical; Anti-Inflammatory Agents; Chymotrypsin; Gingivitis; Microscopy, Fluorescence; Periodontal Diseases; Prednisolone; Rolitetracycline; Trypsin