Abstract
Growth hormone receptors are found in a wide variety of tissues and are thought to mediate the various actions of growth hormone. Recently, a growth hormone binding protein was demonstrated in serum and shown to have antigenic identity with the liver growth hormone receptor by use of a panel of monoclonal antibodies to the receptor. Here we describe the purification, part sequence and cloning of the rabbit liver growth hormone receptor. Purification and N terminal sequence analysis of the rabbit serum binding protein for GH showed it to be identical to the extracellular region of the rabbit liver GH receptor. Rabbit liver receptor and human binding protein sequences were expressed in COS-7 cells and shown to display predicted hormone specificity and antigenic characteristics. Finally, the rabbit mammary gland prolactin receptor was purified and part sequenced. This showed 34% homology with the rabbit liver GH receptor, and therefore constitutes the second member of a new class of transmembrane receptors regulating growth and lactation.
Original language | English |
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Title of host publication | Biotechnology in Growth Regulation |
Editors | R. B. Heap, C. G. Prosser, G. E. Lamming |
Place of Publication | London |
Publisher | Butterworths |
Pages | 15-25 |
Number of pages | 11 |
ISBN (Print) | 978-0-407-01473-2, 040701473X |
DOIs | |
Publication status | Published - 1989 |
Externally published | Yes |