Growth hormone receptor and serum binding protein: purification, cloning and expression

  title={Growth hormone receptor and serum binding protein: purification, cloning and expression},
  author={D. W. Leung and Steven A. Spencer and George Cachianes and R. Glenn Hammonds and C Collins and William J. Henzel and Ross Barnard and Michael J. Waters and William I. Wood},
A putative growth hormone receptor from rabbit liver and the growth hormone binding protein from rabbit serum have the same ammo-terminal amino-acid sequence, indicating that the binding protein corresponds to the extracellular hormone-binding domain of the liver receptor. The complete amino-acid sequences derived from complementary DNA clones encoding the putative human and rabbit growth hormone receptors are not similar to other known proteins, demonstrating a new class of transmembrane… 
The growth hormone-binding protein in rat serum is an alternatively spliced form of the rat growth hormone receptor.
The results suggest that the mechanism for production of the rat serum GH-binding protein is by alternative splicing of the gene for the rat GH receptor.
Mouse growth hormone-binding protein and growth hormone receptor transcripts are produced from a single gene by alternative splicing.
The hypothesis that a growth hormone-binding protein messenger RNA is produced in other species by alternative splicing of nascent growth hormone receptors transcripts was confirmed by analysis of the mouse growth hormone receptor gene.
Growth hormone receptor and binding protein.
Purification, cloning, and expression of the prolactin receptor.
Both the short and long forms of the Prolactin receptor show regions of strong sequence identity with the human and rabbit growth hormone receptors, suggesting that the prolactin and growth hormone receptor originate from a common ancestor.
Growth hormone receptor: structure and signal transduction.
Growth hormone-induced dimerization of the cell surface GHR appears to be a prerequisite for biological activity of the hormone, and JAK2 has been identified as a tyrosine kinase associated with GHR and other receptors of the superfamily.
Cloning and expression of the growth hormone-dependent insulin-like growth factor-binding protein.
The deduced protein sequence of BP-53 has 33% amino acid identity including conservation of all 18 cysteine residues with the recently cloned BP-28, a smaller human IGF-binding protein identified in amniotic fluid and also secreted by the cell line HEP G2.
Evidence for generation of the growth hormone-binding protein through proteolysis of the growth hormone membrane receptor.
The results strongly suggest that, in rabbit and probably in man, the GHBP could, at least in part, be produced by proteolytic cleavage of the GHR.