| First Author | Smith WC | Year | 1989 |
| Journal | Mol Endocrinol | Volume | 3 |
| Issue | 6 | Pages | 984-90 |
| PubMed ID | 2739661 | Mgi Jnum | J:26921 |
| Mgi Id | MGI:74598 | Doi | 10.1210/mend-3-6-984 |
| Citation | Smith WC, et al. (1989) Mouse serum growth hormone (GH) binding protein has GH receptor extracellular and substituted transmembrane domains. Mol Endocrinol 3(6):984-90 |
| abstractText | Predicted amino acid sequences for the mouse GH receptor and the related serum GH binding protein were deducted from cDNAs. Two types of cDNA clones were isolated. Both types coded an identical peptide domain with extensive homology to the extracellular domains of the recently cloned human and rabbit GH receptors. However, while one type of clone also encoded regions with homology to the transmembrane and cytoplasmic domains of the human and rabbit GH receptors, the other encoded a short hydrophilic carboxyl-terminal region in place of the transmembrane domain. It is speculated that these two types of clones encode the high and low molecular weight variants of the mouse GH receptor/serum binding proteins, respectively. The low molecular weight variant has been previously found to constitute the majority of the serum GH binding activity in mice. It is proposed that the substitution of the hydrophilic tail for the transmembrane domain may give the low molecular weight variant its soluble nature and account for its presence in serum. |
