TY - JOUR
T1 - Interaction of Lactogenic Hormones with the Soluble Extracellular Domain of Prolactin Receptors
AU - Gertler, Arieh
AU - Bignon, Christophe
AU - Staten, Nicolas R.
AU - Sakal, Edna
AU - Tchelet, Amir
AU - Krivi, Gwen G.
AU - Djiane, Jean
PY - 1994/7
Y1 - 1994/7
N2 - Two variants of rabbit prolactin receptor extracellular domain (rbPRLR-ECD) were prepared using insect/baculovirus (amino acids 1-198) and E. coli (amino acids 4-210) expression systems. Bovine PRLR-ECD (bPRPL-ECD amino acids 1-210) and human growth hormone receptor ECD (hGHR-ECD amino acids 1-246) were also prepared using E. coli expression system. All four proteins were purified as monomers with >95% homogeneity. Their affinity for various lactogenic and somatogenic hormones was determined by binding assays. The stoichiometry of complex formation with these hormones was studied by gel filtration on a Superdex 75 column, and bioactivity was determined by in vitro bioassays. The results summarized in this paper indicate that, in contrast to hGHR-ECD, in which the ability to form a 2:1 complex with hGH is indicative of the biological activity of the hormone, the ability or inability of prolactin and placental lactogen to form 2:1 complexes with rb or bPRLR-ECD cannot predict their biological activity. This conclusion does not preclude however, hormoneor antibody-induced dimerization of the membrane-embedded receptor.
AB - Two variants of rabbit prolactin receptor extracellular domain (rbPRLR-ECD) were prepared using insect/baculovirus (amino acids 1-198) and E. coli (amino acids 4-210) expression systems. Bovine PRLR-ECD (bPRPL-ECD amino acids 1-210) and human growth hormone receptor ECD (hGHR-ECD amino acids 1-246) were also prepared using E. coli expression system. All four proteins were purified as monomers with >95% homogeneity. Their affinity for various lactogenic and somatogenic hormones was determined by binding assays. The stoichiometry of complex formation with these hormones was studied by gel filtration on a Superdex 75 column, and bioactivity was determined by in vitro bioassays. The results summarized in this paper indicate that, in contrast to hGHR-ECD, in which the ability to form a 2:1 complex with hGH is indicative of the biological activity of the hormone, the ability or inability of prolactin and placental lactogen to form 2:1 complexes with rb or bPRLR-ECD cannot predict their biological activity. This conclusion does not preclude however, hormoneor antibody-induced dimerization of the membrane-embedded receptor.
UR - http://www.scopus.com/inward/record.url?scp=0028103957&partnerID=8YFLogxK
U2 - 10.3181/00379727-206-43758
DO - 10.3181/00379727-206-43758
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C2 - 8016164
AN - SCOPUS:0028103957
SN - 0037-9727
VL - 206
SP - 273
EP - 279
JO - Experimental Biology and Medicine
JF - Experimental Biology and Medicine
IS - 3
ER -