Journal of Capital Medical University ›› 2005, Vol. 26 ›› Issue (4): 467-470.

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Mechanisms of Recombinant Human Growth Hormone Improving Protein Malnutrition: a Study in Vitro

Wen Yubing, Liu Huilan, Huang Lirong, Yao Ying   

  1. Department of Nephrology, Fuxing Hospital, Capital University of Medical Sciences
  • Received:2004-03-01 Revised:1900-01-01 Online:2005-08-24 Published:2005-08-24

Abstract:

Objective To investigate the effects of rhGH on biosynthesis and secretion of secretory albumin, transferrin, insulin-like growth factor-Ⅰ(IGF-Ⅰ), insulin-like growth factor binding protein-1, -3(IGFBP-1, IGFBP-3) of primary cultured hepatocytes and liver non-parenchymal cells of rat.Methods Rat hepatocytes and liver non-parenchymal cells are isolated by two-step procedures in situ. RhGH is added to the medium and the vehicle is added for control. Albumin and transferrin of medium are measured with sandwich ELISA. IGF-Ⅰ, IGFBP-1, and IGFBP-3 in cells lysate are analyzed by Western Blotting.Results The medium concentrations of albumin and transferrin and the IGF-Ⅰ level in cells lysate are significantly higher in rhGH group than in control group, all P <0.01. The IGFBP-1 level in cells lysate is significantly lower and IGFBP-3 level is significantly higher in rhGH group than in control group, both P <0.05.Conclusion rhGH increases biosynthesis and/or secretion of secretory albumin, transferrin, and IGF-I et al. And rhGH inhibits biosynthesis of IGFBP-1 in hepatocytes and enhances expression of IGFBP-3 in non-parenchymal liver cell significantly.

Key words: recombinant human growth hormone, protein malnutrition, hepatocyte

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