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Kumho Life and Environmental Science Laboratory (Y.H.L, I.T.H., J.Y.C.); Chonnam National University Research Institute of Medical Science and Department of Anatomy, Chonnam National University Medical School (B.C.M., K.Y.A.), Kwangju 506-712, Korea; and Clon Biotech Laboratory (S.W.L.), Seoul 143-721, Korea
Address all correspondence and requests for reprints to: Dr. Jong-Yoon Chun, Kumho Life and Environmental Science Laboratory, 572 Sangam-Dong, Kwangsan-Gu, Kwangju 506–712, Korea. E-mail: jychun{at}ksc.kumho.co.kr
We have isolated a complementary DNA (cDNA) clone that encodes a new
member of the PRL-like protein-C (PLP-C) subfamily of the PRL gene
family. The clone was amplified from a 13.5-day-old mouse conceptus
cDNA library by PCR using primers based on conserved regions of PLP-C
sequences. The full-length cDNA encodes a predicted protein of 241
residues, which contains a putative signal sequence and 2 putative
N-linked glycosylation sites. The predicted protein
shares 55–66% amino acid identity with mouse PLP-C
and rat PLP-D,
PLP-H, PLP-Cv, and PLP-C and also contains 6 homologously positioned
cysteine residues. Thus, we named this protein PLP-Cß for
consistency. We have also isolated rat PLP-Cß from rat placenta cDNA
library. Surprisingly, two messenger RNA (mRNA) isoforms of rat
PLP-Cß were isolated: one mRNA (rPLP-Cß) encodes a 241-amino acid
product, but another mRNA (rPLP-Cß
39) lacks 39 bases that encode
for a region rich in aromatic amino acids. The 39-bp region corresponds
to exon 3 of other PLP-C subfamily members, such as PLP-C, PLP-Cv,
and d/tPRP. It suggests that the two isoforms are probably generated by
an alternative splicing from a single gene. RT-PCR analysis revealed
that the rPLP-Cß form was dominantly expressed in placenta, although
both isoforms are coexpressed during placentation. The mouse PLP-Cß
mRNA expression, which was specific to the placenta, was first detected
by Northern analysis on embryonic day 11.5 (E 11.5) and persisted until
birth. However, in situ hybridization analysis revealed
mPLP-Cß expression on E 10.5 in specific trophoblast subsets, such as
giant cells and spongiotrophoblast cells. mPLP-Cß mRNA was detected
in the labyrinthine zone on E 18.5, suggesting that spongiotrophoblast
cells had penetrated the labyrinthotrophoblast zone. Consistent with
the observed expression in trophoblast giant cells, PLP-Cß expression
was also detected in in vitro differentiated Rcho-1
cells, which express the trophoblast giant cell phenotype. In summary,
overall high amino acid identity (79%), the locations of
cysteine residues, and consensus sites for N-linked
glycosylation between mouse and rat PLP-Cß clearly indicate that
PLP-Cß is a bona fide member of the PLP-C subfamily.
The conservation between mouse and rat, the presence of alternative
isoforms, and the pattern of expression during gestation suggest the
biological significance of PLP-Cß during pregnancy.
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