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J. Biol. Chem., Vol. 269, Issue 42, 26076-26082, 10, 1994
KD O'Neal and LY Yu-Lee
An Nb2 prolactin receptor (PRL-R) cDNA has been cloned from the PRL-
dependent Nb2-11C cell line, and the protein-coding region is identical to
that of the PRL-R isolated from the PRL-independent cell line Nb2- Sp.
Short, Nb2, and long forms of the PRL-R were analyzed for signal
transduction to the immediate-early gene, interferon regulatory factor- 1
(IRF-1) and for cellular proliferation. Receptor and IRF-1-CAT reporter
constructs were transiently cotransfected into the interleukin- 3-dependent
cell lines FDC-P1 and BaF3. The Nb2 PRL-R induced IRF-1-CAT 14.3-fold on
addition of PRL, while the long PRL-R induced IRF-1-CAT 5.6-fold in FDC-P1
cells. The short PRL-R did not activate the IRF-1 promoter. Stable
transfectants were also generated by selecting for growth in PRL. Only the
Nb2 and long forms were able to convert the IL- 3-dependent cells to
PRL-dependence. IRF-1-CAT was induced in these cell lines by the Nb2 PRL-R
10- to 12-fold and long PRL-R 3- to 3.5- fold. Overall, the Nb2 form is
more efficient than the long form by about 3-fold at inducing IRF-1-CAT. A
PRL dose-response growth curve showed that the Nb2 form requires 20-fold
less PRL for half maximal growth than the long form. A PRL dose-response
for IRF-1-CAT activity gave similar results, indicating a tight correlation
between IRF-1 induction and cell proliferation. These results show that the
short PRL- R does not signal to IRF-1 or for growth, and that the Nb2 PRL-R
signals more efficiently than the long PRL-R.
Differential signal transduction of the short, Nb2, and long prolactin receptors. Activation of interferon regulatory factor-1 and cell proliferation
Department of Microbiology and Immunology, Baylor College of Medicine, Houston, Texas 77030.
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