Characterization of proliferin-related protein

Mol Endocrinol. 1988 Jun;2(6):579-86. doi: 10.1210/mend-2-6-579.

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 heterogeneous 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cells, Cultured
  • Chromatography
  • Cricetinae
  • DNA, Recombinant / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / metabolism
  • Female
  • Glycosylation
  • Immunosorbent Techniques
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Molecular Weight
  • Nucleic Acid Hybridization
  • Placenta / metabolism*
  • Pregnancy
  • Pregnancy Proteins / genetics
  • Pregnancy Proteins / isolation & purification
  • Pregnancy Proteins / metabolism*
  • Protein Biosynthesis
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / immunology
  • Tissue Distribution

Substances

  • DNA, Recombinant
  • Plfr protein, mouse
  • Pregnancy Proteins
  • Recombinant Fusion Proteins