Effect of Inflammation on the of Collagen Types, I, III, IV, and V and Type I Trimer and Fibronectin in Human Gingivae

Narayanan, A. Sampath; Clagett, James; Page, Roy C.

doi:10.1177/00220345850640090201

Cited by 56 publications

(34 citation statements)

References 14 publications

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“…The expression of the laminin receptor by these epithehal cells does not underline that they were the target for a cytotoxic immune reaction. Whereas the integrins in OLP showed a more non-specific pattern typical for a chronic inflammatory reaction, the most intense changes of the ECM pattern as compared with normal oral mucosa were noted in the subepithehal connective tissue, resembling the pattern of severe inflammation observed in gingivitis (34). This loss of ECM proteins, especially in the atrophic variant of OLP, is probably due to cytokines released from immunocompetent cells such as interferon y and TNFalpha that induce the expression of collagenases and that are found in LP (3,35).…”

Section: Discussionmentioning

confidence: 87%

Altered expression of extracellular matrix proteins and integrins in oral lichen planus (OLP)

Becker

Schuppan²

1995

J Oral Pathology Medicine

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The immunohistochemical distribution of collagens type I, III, IV, V, VI, of undulin and tenascin, and of integrins alpha 2, alpha 3, alpha 4, alpha 5, alpha 6 and beta 4, was studied in 14 biopsies of oral lichen planus (OLP), 5 biopsies of orthokeratinized gingiva and 4 biopsies of oral fibrous hyperplasia. The localization of extracellular matrix proteins showed altered expression in OLP when compared to normal oral mucosa, with two principal patterns corresponding to the reticular or atrophic type. Whereas in the reticular type a focal loss of immunoreactivity for collagen types I, III, V, VI and undulin was noted in areas with a cellular infiltrate, in the atrophic variant almost complete loss of immunoreactivity of the subepithelial extracellular matrix was found. There was no clear correlation between the distribution of extracellular matrix proteins and their integrin receptors. The present findings suggest that the autoimmune reaction in OLP might not be primarily targeted to oral keratinocytes but to an unknown antigen in the connective tissue stroma. The changes in the subepithelial extracellular matrix associated with the inflammatory reaction might, especially in the atrophic variant, impair the cross-talk between epithelium and mesenchyme and favour both the loss of barrier function and the development of erosions in the clinical course of the disease.

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Section: Discussionmentioning

confidence: 87%

Altered expression of extracellular matrix proteins and integrins in oral lichen planus (OLP)

Becker

Schuppan²

1995

J Oral Pathology Medicine

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“…Narayanan & Page (1983b) have shown that though total collagen content of the gingiva fell sharply, the proportions of eollagens type I and III remain roughly constant in disease, whilst collagen type V increases markedly. Narayanan et al (1985) also identify the appearance of a unique type I collagen trimcr (composed of three a chains) in inflamed gingiva. Ko et al (1977) showed a sub-population of fibroblasts which were selectively inhibited in terms of growth and synthetic activity by prostaglandin E, (PGE2) though how this effect is mediated is unelear.…”

Section: Connective Tissue Dynamics and Repairmentioning

confidence: 85%

The role of histopathology in the diagnosis and prognosis of periodontal diseases

et al. 1992

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and Wilton JMA: The role of histopathology in the diagnosis and prognosis of periodontal diseases. J Clin Periodontol 1990; 17: 673-684. Abstract. The histological evaluation of surgical biopsies from affected tissues is a standard way of assessing pathological change and determining treatment in many diseases. In most forms of periodontal disease, however, this approach fmds limited apphcation. Here, we review what uses the histopathological approach has in the study and evaluation of the periodontal diseases. Current understanding of the changes in epithelial anatomy during pocket formation, the cellular composition and dynamics of the inflammatory infiltrate and the mechanisms of bone resorption and repair are reviewed from the perspective of the information available from microscopical investigation, including the uses and potential application of modern immunocytochemical methods to these questions. The usefulness of histological study of biopsy material is reassessed in the light of advances made in immunohistochemical techniques and their application to gingival inflammatory infiltrates and epithelia. Such techniques offer immediately valuable research opportunities with potential for diagnostic applications, noteably the recognition of phases of destructive activity and their differentiation from periods of effective host defence.

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“…It has been found in inflamed tissues and in the first stages of healing. 44,45 This kind of extracellular matrix formation may be of importance in wound-healing processes because of the matrix stability in collagenolytic mechanisms by bacteria.…”

Section: Discussionmentioning

confidence: 99%

Effect of Tissucol� on connective tissue matrix during wound healing: An immunohistochemical study in rat skin

Romanos

Strub

1998

J. Biomed. Mater. Res.

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Fibrin sealants are very useful in different surgical fields. Fixation of free gingival grafts, root coverage procedures, and other techniques increasing connective tissue attachment may be associated with the application of Tissucol in periodontology. The aim of this study was to evaluate the influence of the fibrin sealant in the extracellular matrix, as well as alterations of the connective tissue matrix during wound-healing processes. In the back dermis of 15 Net male rats, Tissucol was implanted after intraperitoneal anesthesia. The implant material was placed in subcutaneous pockets (2 cm in length) which were sutured with interproximal sutures (test and control pockets). At 4, 7, 14, 21, and 28 days after surgery, biopsies of the healed and surrounding tissues were taken, frozen in liquid nitrogen, and examined histologically and immunohistochemically with antibodies against collagen types I, III, IV, V, VI, and VII. The findings showed thick and thin collagen type I and III fibers, respectively, with different orientations localized around the implant material. An increased amount of blood vessels and capillaries (their basement membranes containing collagen type IV) was observed during wound healing which may be associated with the implantation of the sealant. Collagen type V fibers were localized from the first days to the 4th postoperative week and, without any inflammatory reaction (according to histologic staining), formed a fibrillar extracellular matrix with high collagenase resistance. Collagen type VI showed a microfibrillar pattern of distribution, and collagen type VII was localized in the dermo epidermo junction and very deep in the connective tissue in the form of anchoring fibers (only in the test group) during the 4 postoperative weeks of healing. The data showed that Tissucol is a biocompatible component which cannot produce any extensive inflammatory reaction in the matrix. New blood vessel formation, an epithelial-connective tissue interface with high stability, as well as matrix alterations with high resistance in the proteolytic enzymes (i.e., collagenases) can be induced in the connective tissue after use of a fibrin sealant. All of these characteristics may be of great importance in connective tissue healing in periodontal surgical procedures.

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Effect of Inflammation on the of Collagen Types, I, III, IV, and V and Type I Trimer and Fibronectin in Human Gingivae

Cited by 56 publications

References 14 publications

Altered expression of extracellular matrix proteins and integrins in oral lichen planus (OLP)

Altered expression of extracellular matrix proteins and integrins in oral lichen planus (OLP)

The role of histopathology in the diagnosis and prognosis of periodontal diseases

Effect of Tissucol� on connective tissue matrix during wound healing: An immunohistochemical study in rat skin

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