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Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternative splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively. Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus. Human PlGF-1 shares 56%, 55%, 74% and 95% aa identity with the comparable isoform of mouse, rat, canine, and equine PlGF, respectively. PlGF is mainly found as variably glycosylated, secreted, 55-60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes, and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia.