Increased expression of collagen prolyl 4-hydroxylases in Chinese patients with hereditary gingival fibromatosis

• Published in: Archives of oral biology Vol. 52; no. 12; pp. 1209 - 1214
• Main Authors: Meng, LiuYan, Huang, MeiJing, Ye, XiaoQian, Fan, MingWen, Bian, Zhuan
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.12.2007
• Subjects: Adolescent; Adult; Advanced Basic Science; Collagen accumulation; Collagen Type I - metabolism; Dentistry; Female; Fibroblasts - enzymology; Fibroblasts - metabolism; Fibromatosis, Gingival - enzymology; Hereditary gingival fibromatosis; Humans; Male; Matrix Metalloproteinase 1 - metabolism; Matrix Metalloproteinase 3 - metabolism; Procollagen-Proline Dioxygenase - metabolism; Prolyl 4-hydroxylase; RNA, Messenger - analysis; Tissue Inhibitor of Metalloproteinase-1 - metabolism; Prolyl 4-hydroxylase; Collagen accumulation; Hereditary gingival fibromatosis
• ISSN: 0003-9969; 1879-1506
• DOI: 10.1016/j.archoralbio.2007.07.006

Abstract Objectives Hereditary gingival fibromatosis (HGF) is characterized by excess accumulation of interstitial collagen. However, until now, there has been controversy about the mechanism of collagen accumulation in HGF gingivae. The present study aimed to clarify the pathogenic mechanisms potentially involved. Design Gingival fibroblasts from three Chinese HGF patients and three healthy subjects were cultured. Cell proliferation was assessed by MTT assay. The mRNA levels of type I collagen, MMP-1, MMP-3, TIMP-1, prolyl 4-hydroxylase (P4H)α(I), α(II), α(III) and P4Hβ were analyzed in gingival fibroblasts by RT-PCR. The protein production of type I collagen and P4H was examined respectively by ELISA and Western blot. Results In culture, HGF gingival fibroblasts showed similar growth characteristics to fibroblasts isolated from control gingivae. The mRNA and protein levels of type I collagen and P4Hα in HGF fibroblasts were higher than those in controls. There were no detected differences in mRNA expression levels of MMP-1, MMP-3, TIMP-1, P4Hα(II), α(III) and P4Hβ between HGF and control fibroblasts. Conclusions These data suggest that increased collagen post-translational modification by P4H may be one mechanism by which increased collagen accumulation occurs in some forms of HGF.