Endocrinology, Vol 137, 3849-3855, Copyright © 1996 by Endocrine Society

ARTICLES

Molecular cloning and characterization of a new member of the rat placental prolactin (PRL) family, PRL-like protein D (PLP-D)

K Iwatsuki, M Shinozaki, N Hattori, K Hirasawa, S Itagaki, K Shiota and T Ogawa
Laboratory of Cellular Biochemistry, University of Tokyo, Japan.

The rat placental PRL family consists of molecules structurally similar to PRL and GH, and to date, seven members have been identified. During investigation of pregnancy stage-specific placental factors by the differential display method, we obtained a complementary DNA (cDNA) fragment (199 bp) encoding a peptide homologous to PRL-like protein (PLP)-C. By using the 3' and 5' rapid amplification of cDNA ends method, a full-length cDNA was cloned and tentatively named PLP-D. The cDNA encoded a mature protein of 240 amino acids, including a 29-amino acid signal sequence. PLP-D contains one putative N-glycosylation site and six cysteine residues that are highly conserved in the placental PRL family. Sequence comparison between PLP-D and other members of the placental PRL family showed that PLP-D is highly homologous to PLP-C (80%) and decidual PRL-related protein (73%). Northern blot analysis revealed that PLP-D messenger RNA (mRNA) first appeared at day 14 of pregnancy, and that its expression increased until term. In situ hybridization analysis indicated that PLP-D mRNA was specifically expressed in spongiotrophoblast cells and trophoblast giant cells of the placental junctional zone. Differentiated Rcho-1 cells also expressed PLP-D mRNA, whereas undifferentiated Rcho-1 cells did not.

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