A mutant lactogenic hormone binds, but does not activate, the prolactin receptor

Janine A. Davis, Daniel I.H. Linzer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

We have generated mutations in mouse placental lactogen II, a hormone in the PRL/GH family that binds to the PRL receptor, to investigate the role of the conserved cysteine residues in hormone function. Disruption of the small C-terminal disulfide loop did not significantly alter hormone activity. Substitution of serine for cysteine-51, which prevents formation of the large disulfide loop, results in a protein equivalent to placental lactogen II in receptor-binding activity; however, this mutant protein is not mitogenic in an assay for lactogenic hormones. These results indicate that PRL receptor occupancy and activation are distinct events.

Original languageEnglish (US)
Pages (from-to)949-953
Number of pages5
JournalMolecular Endocrinology
Volume3
Issue number6
DOIs
StatePublished - Jun 1989

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology

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