TIMP‐1 association with collagen type I overproduction in hereditary gingival fibromatosis

• Published in: Oral diseases Vol. 24; no. 8; pp. 1581 - 1590
• Main Authors: Gawron, Katarzyna, Ochała‐Kłos, Anna, Nowakowska, Zuzanna, Bereta, Grzegorz, Łazarz‐Bartyzel, Katarzyna, Grabiec, Aleksander M., Plakwicz, Paweł, Górska, Renata, Fertala, Andrzej, Chomyszyn‐Gajewska, Maria, Potempa, Jan
• Format: Journal Article
• Language: English
• Published: Denmark Wiley Subscription Services, Inc 01.11.2018
• Subjects: Adolescent; Adult; Cells, Cultured; Child; Collagen; Collagen (type I); collagen I; Collagen Type I - metabolism; Connective tissue growth factor; Connective Tissue Growth Factor - genetics; Connective Tissue Growth Factor - metabolism; Enzyme-linked immunosorbent assay; Female; Fibrils; Fibroblasts; Fibromatosis, Gingival - genetics; Fibromatosis, Gingival - metabolism; Fibromatosis, Gingival - pathology; Fibrosis; Gene Expression; Gingiva; Gingiva - cytology; Gingival fibromatosis; Growth factors; Hereditary gingival fibromatosis; HSP47 Heat-Shock Proteins - genetics; HSP47 Heat-Shock Proteins - metabolism; Humans; Male; Matrix metalloproteinase; Matrix Metalloproteinase 1 - metabolism; Metalloproteinase; TIMP‐1; Tissue Inhibitor of Metalloproteinase-1 - metabolism; Tissue inhibitor of metalloproteinases; Transforming growth factor; Transforming Growth Factor beta1 - genetics; Transforming Growth Factor beta1 - metabolism; Transforming growth factor-b1; Western blotting; fibrosis; TIMP-1; hereditary gingival fibromatosis; collagen I
• ISSN: 1354-523X; 1601-0825; 1601-0825
• DOI: 10.1111/odi.12938

Objectives To investigate the processes associated with the excessive production of collagen I in hereditary gingival fibromatosis (HGF). Materials and Methods Three HGF subjects and five controls were enrolled in the study. Histomorphological and immunohistological analyses were performed on gingival tissues. The expression of heat‐shock protein 47 (HSP47), collagen I, transforming growth factor‐β1 (TGF‐β1), connective tissue growth factor (CTGF), matrix metalloproteinase‐1 (MMP‐1) and tissue inhibitor of matrix metalloproteinase‐1 (TIMP‐1) by gingival fibroblasts isolated from HGF and controls was analysed using qRT–PCR, Western blotting and ELISA. Results Considerable accumulation of fibrotic fibrils and increased synthesis of HSP47 were noted in HGF gingival tissues. The synthesis of collagen I, HSP47, TGF‐β1, CTGF and TIMP‐1 was significantly elevated in HGF gingival fibroblasts compared with controls, while the production of MMP‐1 was decreased. Conclusions We report that fibrosis in HGF gingival tissues is associated with increased synthesis of HSP47. This finding was confirmed by an in vitro study, where excessive production of collagen I was associated with increased synthesis of HSP47, TGF‐β1 and CTGF by HGF gingival fibroblasts. Moreover, the shift in the TIMP‐1/MMP‐1 ratio identifies increased synthesis of TIMP‐1 as one of the processes associated with collagen I overproduction in HGF fibroblasts.