Stimulation and inhibition of angiogenesis by placental proliferin and proliferin-related protein

Dowdy Jackson, Olga V. Volpert, Noël Bouck, Daniel I H Linzer*

*Corresponding author for this work

Research output: Contribution to journalArticle

197 Scopus citations

Abstract

In many mammalian species, the placenta is the site of synthesis of proteins in the prolactin and growth hormone family. Analysis of two such proteins, proliferin (PLF) and proliferin-related protein (PRP), revealed that they are potent regulators of angiogenesis; PLF stimulated and PRP inhibited endothelial cell migration in cell culture and neovascularization in vivo. The mouse placenta secretes an angiogenic activity during the middle of pregnancy that corresponds primarily to PLF, but later in gestation releases a factor that inhibits angiogenesis, which was identified as PRP. Incubation of placental tissue with PLF led to the specific binding of this hormone to capillary endothelial cells. Thus PLF and PRP may regulate the initiation and then the cessation of placental neovascularization.

Original languageEnglish (US)
Pages (from-to)1581-1584
Number of pages4
JournalScience
Volume266
Issue number5190
DOIs
StatePublished - Jan 1 1994

ASJC Scopus subject areas

  • General

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