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Biology of Reproduction, Vol 40, 27-32, Copyright © 1989 by Society for the Study of Reproduction

ARTICLES

Purification, cloning, and expression of the prolactin receptor

PA Kelly, JM Boutin, C Jolicoeur, H Okamura, M Shirota, M Edery, I Dusanter- Fourt and J Djiane
Laboratory of Molecular Endocrinology, McGill University, Royal Victoria Hospital, Montreal, Quebec, Canada.

The rat liver prolactin receptor has been purified to homogeneity, and partial amino acid sequences have been obtained. The structure of the receptor has been deduced from a single complementary DNA clone. The mature protein of 291 amino acids has a relatively long extracellular region, a single transmembrane segment, and a short (57 amino acids) cytoplasmic domain. With the rat cDNA used as a probe, the prolactin receptor in rabbit mammary gland and human hepatoma cells has also been isolated. These tissues contain a second, longer form of the receptor (592 and 598 amino acids, respectively). 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 receptors originate from a common ancestor.


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J. N. C. Mao, J. Burnside, L. Li, J. Tang, C. Davolos, and L. A. Cogburn
Characterization of Unique Truncated Prolactin Receptor Transcripts, Corresponding to the Intracellular Domain, in the Testis of the Sexually Mature Chicken
Endocrinology, March 1, 1999; 140(3): 1165 - 1174.
[Abstract] [Full Text]


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