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Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208
Address all correspondence and requests for reprints to: Dr. Daniel I. H. Linzer, Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, 2153 Sheridan Road, Evanston, Illinois 60208. E-mail: dlinzer{at}nwu.edu
Two novel members of the mouse PRL/GH family have been identified through a search of an expressed sequence tag database. The encoded proteins do not appear to be homologs of other known members of this hormone family. One of these proteins, designated PRL-like protein E (PLP-E), is predicted to be synthesized as a precursor of 265 amino acids, modified by N-linked glycosylation, and secreted as a mature glycoprotein of 236 residues. The second clone encodes a protein of 253 residues with consensus sites for N-linked glycosylation; the secreted form of the protein, designated PRL-like protein F (PLP-F), is predicted to be 223 amino acids in length. Both of these messenger RNAs are expressed specifically in the placenta, with peak levels of PLP-E on days 1012 and of PLP-F on days 1416. Expression of PLP-E is restricted to the trophoblast giant cells, whereas PLP-F is synthesized only in the spongiotrophoblasts. The genes for both of these proteins map to a 700-kilobase region of mouse chromosome 13 that includes other members of the PRL/GH family.
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