Morphological and molecular analysis of idiopathic gingival fibromatosis: a case report

• Published in: Journal of clinical periodontology Vol. 32; no. 10; pp. 1116 - 1121
• Main Authors: Gagliano, Nicoletta, Moscheni, Claudia, Dellavia, Claudia, Masiero, Silvia, Torri, Carlo, Grizzi, Fabio, Stabellini, Giordano, Gioia, Magda
• Format: Journal Article
• Language: English
• Published: Oxford, UK Munksgaard International Publishers 01.10.2005
• Subjects: Adult; Collagen - analysis; collagen turnover; Dentistry; Extracellular Matrix Proteins - analysis; Female; Fibroblasts - enzymology; Fibromatosis, Gingival - enzymology; Fibromatosis, Gingival - pathology; Gingiva - enzymology; Gingiva - pathology; gingival overgrowth; Humans; idiopathic gingival fibromatosis; Male; RNA, Messenger - analysis
• ISSN: 0303-6979; 1600-051X
• DOI: 10.1111/j.1600-051X.2005.00811.x

Aim: We analyse a case of idiopathic gingival overgrowth using morphological and molecular methods. As this overgrowth involves collagen accumulation in the gingival connective tissue, we measured the collagen turnover to clarify the pathogenic mechanisms potentially involved. Materials and Methods: The patient was a 29‐year‐old Italian woman with enlargement of the gingivae throughout the entire mandible and maxilla. Morphological analyses were carried out on haematoxylin–eosin and Sirius red‐stained paraffin‐embedded gingival sections. mRNA levels of collagen type I and III, matrix metalloproteinase (MMP)‐1, transforming growth factor‐β1 and lysyl hydroxylase (LH)2b were determined by RT‐PCR on cultured gingival fibroblasts and compared with healthy control fibroblasts. Interstitial collagen and MMP‐1 content in the supernatants were assessed, respectively, by dot blot and SDS zymography. Results and Conclusions: In Sirius red‐stained sections of the patient's overgrown gingivae, interstitial collagen content was 29% higher than controls. Her gingival fibroblasts had higher collagen type I, MMP‐1 and LH2b gene expression and unmodified interstitial collagen, type I protein levels in the supernatants. These findings would seem to suggest that in this case collagen accumulation in the gingival connective tissue was not associated with increased synthesis and decreased degradation.