Interaction of Lactogenic Hormones with the Soluble Extracellular Domain of Prolactin Receptors

Arieh Gertler, Christophe Bignon, Nicolas R. Staten, Edna Sakal, Amir Tchelet, Gwen G. Krivi, Jean Djiane

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)273-279
Number of pages7
JournalExperimental Biology and Medicine
Volume206
Issue number3
DOIs
StatePublished - Jul 1994

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