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1 Department of Pathology, Center for Research in Oral Biology, University of Washington School of Medicine, Seattle, Washington 98195
2 Department of Periodontics, Center for Research in Oral Biology, University of Washington School of Medicine, Seattle, Washington 98195
3 Departments of Pathology and Periodontics, Center for Research in Oral Biology, University of Washington School of Medicine, Seattle, Washington 98195
The effect of inflammation on the distribution of collagen types I, III, Iv, and V and type I trimer and fibronectin in human gingivae was studied after staining them with antibodies to these proteins. Gingival antibodies, and staining was visualized by indirect immunofluorescence using FITC- or rhodamine-conjugated second antibodies. The results showed that antibody to type I collagen stained normal gingival connective tissue uniformly and revealed the presence of thick fiber bundles. The staining was sparse at areas of inflammation and leukocytic infiltration. Anti-type-III antibody revealed a fine fibrillar network in the normal gingivae, especially near the epithelium; the type III was also lost at sites of inflammation. Type V collagen antibody also stained the gingival connective tissue intensely but, unlike the types I and III staining, it was retained in inflamed areas. Normal gingivae were not stained by the type I trimer antibody; however, staining occured at inflamed sites. Both normal and inflamed tissues were stained by type IV collagen antibody, and the staining was restricted to basement membrane structures. The normal and inflamed gingivae contained a thick fiber network bound anti-fibronectin antibody. We conclude that the various gingival collagen fibers are made up of collagen types I, III, and V, that the types I and III collagens are preferentially lost during inflammation, and that type I trimer appears at inflamed sites.
Submitted on March 4, 1985
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