Abstract
Two lambda gt11 clones containing fragments of cDNA encoding the prolactin receptor from rabbit mammary gland were isolated using a rat liver prolactin receptor cDNA probe. An 1848-base-pair open reading frame encodes a mature prolactin-binding protein of 592 amino acids that contains three domains: (i) the extracellular, amino-terminal, prolactin-binding region of 210 residues; (ii) the transmembrane region of 24 residues; and (iii) the intracellular, carboxyl-terminal domain of 358 residues. This latter domain is much longer than the cytoplasmic domain (57 residues) previously described for the rat liver prolactin receptor. In addition, the sequence identity of this form of prolactin receptor with the growth hormone receptor is extended in the cytoplasmic domain.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Cell Line
Cell Membrane/metabolism
Cloning, Molecular
DNA/genetics
DNA Probes
Female
Gene Expression Regulation
Glycosylation
Liver/analysis
Mammary Glands, Animal/analysis
Molecular Sequence Data
Nucleic Acid Hybridization
Pregnancy
Prolactin/metabolism
Rabbits
Rats
Receptors, Prolactin/genetics
Sequence Homology, Nucleic Acid
Transfection
Chemicals
DNA Probes
Receptors, Prolactin
Prolactin
DNA
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Edery M
Unité d'Endocrinologie Moléculaire, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.
Jolicoeur C
Levi-Meyrueis C
Dusanter-Fourt I
Pétridou B
Boutin J M
Lesueur L
Kelly P A
Djiane J
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