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Effects of Glucose on Insulin-like Growth Factor Binding-5 Expression in Human Fibroblasts.

사람의 섬유아세포에서 Glucose 농도가 Insulin-like Growth Factor Binding Protein-5의 발현에 미치는 영향

  • Ryu, Hye-Young (Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • Hwang, Hye-Jung (Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • Kim, In-Hye (Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • Ryu, Hong-Soo (Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • Nam, Taek-Jeong (Faculty of Food Science and Biotechnology, Pukyong National University)
  • 류혜영 (부경대학교 식품생명공학부) ;
  • 황혜정 (부경대학교 식품생명공학부) ;
  • 김인혜 (부경대학교 식품생명공학부) ;
  • 류홍수 (부경대학교 식품생명공학부) ;
  • 남택정 (부경대학교 식품생명공학부)
  • Published : 2007.09.30

Abstract

Insulin-like growth factor-I (IGF-I) and IGF-II have structure like insulin. In contrast to insulin, however, the bioavaility of IGFs is modulated by the IGF-binding protein (IGFBPs). Each of IGFBPs was different with molecular masses, biological characteristics, and immunological properties.. Human fibroblasts secrete IGFBPs that can modify IGF-I action. In diabetes mellitus, the most study of IGF systems have been investigated in insulin-dependent diabetes mellitus, non-insulin-dependent diabetes mellitus, and streptozotocin-in-duced animals in vivo. Recently, a little research regarding the IGFs system has been proposed in por-tion of cell in vitro. In this study, effects of low or high glucose condition on IGFBP-5 in GM10 was investigated. By western blotting analysis, IGFBP-5 level decreased in cells cultured at high glucose, but IGFBP-5 level of mRNA didn't change. IGFBP-5 protease that cleaves IGFBP-5 in conditioned me-dium had was inhibited by EDTA and heparin, like serine protease and metalloprotease. Furthermore, the protease activity was increased in high glucose cultivated condition. In results of gelatin zymog-raphy, molecular weight of proteolytic metalloenzymes was indentified 69-kDa and protease activity was increased in time-dependent manner. Although the mechanism has yet to be determined, IGFBP-5 proteolysis in GM10 cells cultured with high glucose may increase effects of IGFs to decrease the glu-cose level through dissociation of IGFs from IGFBPs. Therefore, we suggest that IGF- I and IGFBPs could be potential models in study of pathophysiology such as diabetes mellitus.

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