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(Received for publication, February 1, 1996, and in revised form, April 1, 1996)
From the Prolactin (PRL) is essential for progesterone
biosynthesis and luteal cell hypertrophy of the rat corpus luteum
during pregnancy. Both the long and short form of the PRL receptor have
been identified in the corpus luteum of pregnant rat. The long form has
been shown to transduce PRL signal in other cells, whereas no
information is available on the role of the short form, especially in
the corpus luteum. In the present study, we have cloned a rat
ovarian-specific phosphoprotein, PRAP (
Volume 271, Number 26,
Issue of June 28, 1996
pp. 15602-15607
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Department of Physiology & Biophysics,
University of Illinois, Chicago, Illinois 60612 and the
§ Department of Biochemistry, Molecular Biology, and
Cell Biology, Northwestern University, Evanston, Illinois 60208
RL
eceptor
ssociated
rotein), which
has no significant homology to other known proteins. We have
demonstrated that this protein is immunoprecipitated by anti-PRL
receptor and anti-phosphotyrosine antibodies. To determine whether PRAP
associates with either the long or the short form of the PRL receptor,
fusion proteins with glutathione S-transferase containing
the cytoplasmic domain of the long or short form of the PRL receptor
were produced, purified, and incubated with luteal proteins. Our
results indicate that PRAP preferentially binds to the short form of
the PRL receptor. Thus, the long form and short forms of the PRL
receptor may signal through distinct pathways. These data provide
evidence for the involvement of a novel protein in PRL signal
transduction and suggest that PRAP may contribute to the luteotropic
effects of PRL on the corpus luteum during pregnancy.
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