The 20-Kilodalton (kDa) Human Growth Hormone (hGH) Differs from the 22-kDa hGH in the Complex Formation with Cell Surface hGH Receptor and hGH-Binding Protein Circulating in Human Plasma
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چکیده
منابع مشابه
The 20-kilodalton (kDa) human growth hormone (hGH) differs from the 22-kDa hGH in the complex formation with cell surface hGH receptor and hGH-binding protein circulating in human plasma.
In spite of recent advance in understanding of the stoichiometry of 22-kDa human GH (22K-hGH) with cell surface hGH receptor (hGHR) and hGH-binding protein (hGH-BP) circulating in human plasma, that of 20-kDa hGH (20K-hGH) is poorly understood. To clarify this, mouse pro-B Ba/F3 cells stably expressing the full-length hGHR (Ba/F3-hGHR) and both recombinant and native hGH-BP were used in this st...
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Human growth hormone (HGH) (1, 2) has been used experimentally and therapeutically in man since 1957 (3-5). The metabolic and growth-promoting effects of the parenterally administered hormone in humans (3-5) and the antigenicity of various HGH preparations in rabbits and in guinea pigs (6, 7) are well documented. This paper describes the appearance of specific antibodiesto HGH in the plasma of ...
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It has recently been shown that 20 kDa human growth hormone (hGH) forms the 1:2 hGH:hGH receptor (hGHR) complex and expresses full agonistic activity, although it hardly forms the 1:1 GH:GHR complex as compared with 22 kDa hGH. To clarify this mechanism, we analyzed the mode of receptor dimerization of 20 kDa hGH using the intact form and mutants. Complex formation analysis between hGHR extrace...
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Placental human growth hormone-variant (hGH-V) and pituitary human growth hormone-N (hGH-N) are of identical size (22 kDa) but differ in 13 residues scattered throughout the protein. Several isoforms of GH are produced by the hGH-N and hGH-V genes including a 20-kDa hGH-V resulting from a 45-bp deletion caused by the use of an alternative acceptor site within exon 3. To date, the biological pro...
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ژورنال
عنوان ژورنال: Molecular Endocrinology
سال: 1998
ISSN: 0888-8809,1944-9917
DOI: 10.1210/mend.12.1.0054