Ultrastructural localization of cathepsin B in gingival tissue from chronic periodontitis patients

• Published in: Journal of Molecular Histology 1997-10, Vol.29 (10), p.727-734
• Main Authors: Kennett, C N, Cox, S W, Eley, B M
• Format: Article
• Language: English
• Subjects: Cathepsin B - metabolism; Chronic Disease; Collagen; Gingiva - metabolism; Gingiva - pathology; Gingiva - ultrastructure; Humans; Immunohistochemistry; Labeling; Periodontitis - metabolism; Periodontitis - pathology; Proteins; Tumors
• ISSN: 0018-2214; 1567-2379; 1567-2387; 1573-6865
• DOI: 10.1023/A:1026465118281

Loss of tooth support during chronic periodontitis is very likely to involve tissue proteases such as cathepsin B. The distribution of this enzyme was, therefore, examined in ultrathin sections of gingival tissue embedded in acrylic resin and labelled with a sheep polyclonal antibody and gold-conjugated secondary antibody. Macrophages and fibroblasts in both inflamed and non-inflamed areas of tissue showed labelling, and this was strongest in lysosomes, corresponding to the normal intracellular location of cathepsin B. However, additional gold particles were found on the surface of these cells. Monocytes in inflamed areas also had surface labelling, some of which was present on microvilli. Labelled collagen fibres adjacent to all three cell types indicated that cathepsin B had been released into the immediate extracellular environment. Plasma membrane cathepsin B has previously been associated with cancers, but enzyme redistribution and release in the gingiva may have been linked to the inflammatory response, since fibroblasts and macrophages in non-inflamed areas showed less labelling of their surface and adjacent collagen. The collagen labelling added to evidence that cathepsin B can function extracellularly as well as intracellularly in connective tissue degradation. This destructive role for the enzyme is supported by our earlier measurements of increased biochemical activity in chronic periodontitis.