Expression of multiple forms of the prolactin receptor in mouse liver.
We have characterized the PRL receptor (PRL-R) present in mouse liver by purification, cross-linking, and immunological analysis of the protein, and by the isolation of PRL-R cDNA clones. Analysis of the cDNA clones indicates that the liver receptor is actually a family of proteins. Two of these proteins are predicted to be synthesized as precursors of 303 and 292 amino acids, with common signal sequences, extracellular domains, and transmembrane domains; a portion of their cytoplasmic domains are also identical, but these proteins differ markedly in the terminal region of this domain. A third PRL-R protein is predicted to be a truncated form and may be secreted. These multiple PRL-R mRNAs appear to be encoded by at least two genes, with the sequence variation for the two full-length proteins likely due to alternative RNA splicing. These results suggest that the varied actions of PRL may involve multiple receptors that are part of distinct signal transduction pathways.
Davis
J A
JA
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208.
Linzer
D I
DI
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005786:Gene Expression Regulation; D008099:Liver; D051379:Mice; D008969:Molecular Sequence Data; D011981:Receptors, Prolactin / Q000235:genetics*
D011981:Receptors, Prolactin; D004247:DNA