In this paper we review current knowledge on placenta growth factor (PIGF) and summarise our data on its recombinant production in bacteria and its activity. PIGF and vascular endothelial growth factor (VEGF) are both angiogenic factors belonging to the platelet-derived growth factor (PDGF) family. PIGF is a dimeric glycoprotein which shares a number of biochemical and functional features with VEGF. The aminoacidic similarity between the two factors is high (about 50%) in the PDGF-like domain. By alternative splicing of the PIGF mRNA, three forms of PIGF protein are generated which are named PIGF-1, PIGF-2 and PIGF-3. We have focused our attention on form 1 of human PIGF (PIGF-1). A large quantity of active recombinant PIGF-1 has been obtained using a bacterial expression system. By optimising the fermentation and purification it was possible to produce about 140 mg/l of culture of active PIGF-1, which is potentially suitable for a pharmaceutical use. The angiogenic activity of two different batches of bacteria-derived PIGF-1 obtained in our laboratory was demonstrated in chick chorionallantoic membrane assays. Finally, in preliminary studies we have shown that bacteria-derived PIGF-1 has a protective effect against myocardial lesions induced by isoprenaline in rat and rabbit.