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Characterization of Proliferin-Related Protein

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

Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University Evanston, Illinois 60208

Address requests for reprints to: Dr. Daniel Linzer, Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, 2153 Sheridan Road, Evanston, Illinois 60208.

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

FOOTNOTES

This research was supported by NIH Grant GM-34238, a Basil O'Conner Award from the March of Dimes, and by an award from the Searie Scholars Program.

^* Present address: Genentech, Inc., South San Francisco, CA 94080.

Present address: Boehringer-Mannheim, Inc., Indianapolis, IN 46250.

NIH predoctoral trainee.

Received for publication February 1, 1988. Accepted for publication March 3, 1988.

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