title: Cathepsin G in gingival tissue and crevicular fluid in adult periodontitis.
abstract: The presence, localization and activities of cathepsin G in gingival tissue specimens and crevicular fluid (GCF) from 9 adult periodontitis patients and 6 controls with clinically healthy periodontium were studied by use of avidinbiotin-peroxidase complex method, Western and dot blotting, and spectrophotometric activity assay. In contrast to healthy gingival tissue specimens, gingival tissue specimens collected from adult periodontitis patients contained inflammatory cells in lamina propria, beneath the oral sulcular epithelium, 10-50% of which were cathepsin G positive polymorphonuclear neutrophilic leukocytes (PMNs) and monocyte/macrophage-like cells. Cathepsin G activities were increased in adult periodontitis GCF when compared to periodontally healthy controls' GCF (p < 0.05). In adult periodontitis GCF, Western blotting disclosed free cathepsin G but also clear complexes of cathepsin G with its predominant endogenous inhibitor alpha 1-antichymotrypsin (alpha 1-ACT). The present results demonstrate that part of the cathepsin G, despite the presence of increased concentrations of alpha 1-ACT, was in an uncomplexed, free and functionally active form. Our results suggest that GCF cathepsin G reflects the disease process in adjacent inflamed gingiva and also increased host response to microbiota and/or dental plaque in the periodontitis lesions. Cathepsin G may contribute to periodontal tissue destruction directly and indirectly, via proteolytic activation of latent neutrophil procollagenase (promatrix metalloproteinase-8 [proMMP-8]).
authors.affiliation: Department of Anatomy, University of Helsinki, Finland.
authors.forename: T
authors.initials: T
authors.lastname: Tervahartiala
authors.forename: Y T
authors.initials: YT
authors.lastname: Konttinen
authors.forename: T
authors.initials: T
authors.lastname: INgman
authors.forename: R
authors.initials: R
authors.lastname: Häyrinen-Immonen
authors.forename: Y
authors.initials: Y
authors.lastname: Ding
authors.forename: T
authors.initials: T
authors.lastname: Sorsa
mesh_terms: D000328:Adult; D000368:Aged; D018407:Bacterial Physiological Phenomena; D015153:Blotting, Western; D056649:Cathepsin G; D002403:Cathepsins / Q000032:analysis* / Q000037:antagonists & inhibitors; D017364:Collagenases / Q000378:metabolism; D003773:Dental Plaque / Q000201:enzymology / Q000382:microbiology; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism; D004848:Epithelium / Q000473:pathology; D005881:Gingiva / Q000201:enzymology* / Q000473:pathology; D005883:Gingival Crevicular Fluid / Q000166:cytology / Q000201:enzymology*; D005891:Gingivitis / Q000201:enzymology / Q000473:pathology; D006801:Humans; D015151:Immunoblotting; D007124:Immunoenzyme Techniques; D008264:Macrophages / Q000473:pathology; D008875:Middle Aged; D009000:Monocytes / Q000473:pathology; D009504:Neutrophils / Q000473:pathology; D010518:Periodontitis / Q000201:enzymology* / Q000473:pathology; D010519:Periodontium / Q000201:enzymology; D012697:Serine Endopeptidases / Q000032:analysis*; D015842:Serine Proteinase Inhibitors / Q000032:analysis; D013053:Spectrophotometry; D000514:alpha 1-Antichymotrypsin / Q000032:analysis
chemical_list: D004792:Enzyme Precursors; D015842:Serine Proteinase Inhibitors; D000514:alpha 1-Antichymotrypsin; D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D017364:Collagenases; C022440:procollagenase