Characterization of Proliferin-Related Protein

Peter Colosi, Jennifer J. Swiergiel, Elizabeth L. Wildert, Angelica Oviedo, Daniel I.H. Linzer*

*Corresponding author for this work

Research output: Contribution to journalArticle

58 Scopus citations

Abstract

Proliferin-related protein (mPRP) is a member of the PRL/GH family in the mouse. We have generated an antiserum against mPRP expressed as a bacterial fusion protein; this antiserum detects mPRP in the conditioned media of placental tissue cultures as a heterogenous population of glycoproteins. We have also expressed mPRP in mammalian tissue culture cells and purified the secreted protein. N-terminal sequence analysis of the purified protein reveals that it is secreted as a 214 amino acid protein after removal of a 30 amino acid signal polypeptide. An antiserum raised against the purified protein detects high levels of mPRP in maternal serum during gestation. The site of synthesis of this protein has been localized by in situ hybridization to the basal zone of the day-10 mouse placenta, which is distinct from the site of synthesis of other placental proteins in this family.

Original languageEnglish (US)
Pages (from-to)579-586
Number of pages8
JournalMolecular Endocrinology
Volume2
Issue number6
DOIs
StatePublished - Jun 1988

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology

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    Colosi, P., Swiergiel, J. J., Wildert, E. L., Oviedo, A., & Linzer, D. I. H. (1988). Characterization of Proliferin-Related Protein. Molecular Endocrinology, 2(6), 579-586. https://doi.org/10.1210/mend-2-6-579