D. Jackson et al., STIMULATION AND INHIBITION OF ANGIOGENESIS BY PLACENTAL PROLIFERIN AND PROLIFERIN-RELATED PROTEIN, Science, 266(5190), 1994, pp. 1581-1584
In many mammalian species, the placenta is the site of synthesis of pr
oteins in the prolactin and growth hormone family. Analysis of two suc
h proteins, proliferin (PLF) and proliferin-related protein (PRP), rev
ealed that they are potent regulators of angiogenesis; PLF stimulated
and PRP inhibited endothelial cell migration in cell culture and neova
scularization in vivo. The mouse placenta secretes an angiogenic activ
ity during the middle of pregnancy that corresponds primarily to PLF,
but later in gestation releases a factor that inhibits angiogenesis, w
hich was identified as PRP. Incubation of placental tissue with PLF le
d to the specific binding of this hormone to capillary endothelial cel
ls. Thus PLF and PRP may regulate the initiation and then the cessatio
n of placental neovascularization.