Human growth hormone binding protein structure and function of.docVIP

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Human growth hormone binding protein structure and function of.doc

Human growth hormone binding protein structure and function of

 PAGE \* MERGEFORMAT 17 Human growth hormone binding protein structure and function of [Keywords:] human growth hormone binding protein As the medical profession on human growth hormone (human gowth hormone, hGH) to promote growth, development and other physiological mechanism of the in-depth, growth hormone and insulin  like growth factor (insulin  like growth factor, IGF) axis function, mechanisms have an increased Vietnam has been one of the pie. Has now been confirmed, GH physiological functions in the body mainly through a combination of human growth hormone receptor (human growth hormone receport, hGHR), receptor dimerization signal transduction start to finish. But it addresses issues related to human growth hormone binding protein (human growth hormone binding protein, hGHBP) functional linkages, it would take further explored. hGHBP paragraph from the hGHR extracellular hydrolysis by proteolytic enzymes to obtain [1,2]. The exact physiological function is not very clear, it is generally believed that hGH is mainly with the combination of hGH extended half-life, lower clearance rate of GH in vivo [3]. The growing number of studies have shown that with GH, GHR functions among closely linked, in addition to be able to regulate the biological activity of GH, but also may be involved in regulating GHR gene expression and transcription, the nucleus signal transduction [4]. In this paper, hGHBP the formation, structure and functions have done a review. A human growth hormone receptor Have been people, rabbits, mice, rats, sheep, cattle, pigs, pigeons, monkeys and other species were more than a dozen GH receptor cDNA clone. People GHRcDNA encodes 638 amino acids, including a 18 amino acid signal peptide. Mature human GHR molecules containing a single chain of 620 amino acid glycoprotein, in which N terminal 246 amino acids with five potential glycosylation sites, located outside of the cell constitutes a hormone binding domain; Article 247  270 for t

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