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J. Biol. Chem., Vol. 269, Issue 5, 3318-3324, Feb, 1994
C Bignon, E Sakal, L Belair, N Chapnik-Cohen, J Djiane and A Gertler
The cDNA of the extracellular domain of the rabbit prolactin receptor
(rbPRLR-ECD) was cloned in the prokaryotic expression vector pTrc99A to
enable its expression in Escherichia coli after induction with
isopropyl-1-thio-beta-D-galactopyranoside. The bacterially expressed
rbPRLR-ECD protein, contained within the refractile body pellet, was
solubilized in 4.5 M urea, refolded, and purified on a Q-Sepharose column
by stepwise elution with NaCl. The bioactive monomeric fraction was eluted
in 0.05 M NaCl, yielding 15-20 mg/8 liters of induced culture. The purified
protein was > 98% homogeneous, as shown by SDS- polyacrylamide gel
electrophoresis in the presence or absence of reducing agent and by
chromatography on a Superdex column. Its molecular mass was 25 kDa as
determined by SDS-polyacrylamide gel electrophoresis in the absence of
reducing agent and 22 kDa as determined by gel filtration. Binding
experiments revealed remarkable differences between rabbit and porcine
prolactins (PRLs) and the other tested lactogenic hormones. Gel filtration
was used to determine the stoichiometry of the rbPRLR-ECD interaction with
ovine, rabbit, and porcine PRLs, with human growth hormone and its
truncated des-7 analogue, and with bovine placental lactogen (bPL) and
des-13-bPL. The formation of only 1:1 complexes was indicated, except with
bPL, for which a 2:1 complex was detected. Identical stoichiometry was also
obtained using excess radiolabeled rbPRLR-ECD in gel filtration
experiments. Interaction of 125I-labeled ovine PRL with rbPRLR-ECD secreted
into conditioned medium by rbPRLR-ECD cDNA-transfected COS 7 cells also
indicated formation of 1:1 molar complexes. Despite the differences in
binding potency and stoichiometries of the interaction with rbPRLR-ECD, all
seven tested hormones were biologically active in inducing PRL
receptor-mediated casein synthesis in explants of rabbit mammary gland. We
therefore propose that the formation of the 1:2 complexes with soluble
rbPRLR-ECD is not predictive of biological activity of the different
lactogenic hormones.
Preparation of the extracellular domain of the rabbit prolactin receptor expressed in Escherichia coli and its interaction with lactogenic hormones
Unite d'Endocrinologie Moleculaire, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.
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