Isolation of a Human Placenta cDNA Coding for a Protein Related to the Vascular Permeability Factor

• Published in: Proceedings of the National Academy of Sciences - PNAS 1991-10, Vol.88 (20), p.9267-9271
• Main Authors: Maglione, Domenico, Guerriero, Valente, Viglietto, Giuseppe, Delli-Bovi, Pasquale, Persico, M. Graziella
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Analytical, structural and metabolic biochemistry; Animals; Antibodies; Base Sequence; Biological and medical sciences; Cell Division - drug effects; Cell growth; Cell Line; Choriocarcinoma; Cloning, Molecular; Complementary DNA; COS cells; DNA - genetics; DNA - isolation & purification; Endothelial cells; Endothelial Growth Factors - genetics; Endothelium, Vascular - cytology; Endothelium, Vascular - drug effects; Female; Fundamental and applied biological sciences. Psychology; Gene Library; genes; Human growth; Humans; Lymphokines - genetics; Macromolecular Substances; Molecular Sequence Data; Molecular Weight; Oligodeoxyribonucleotides; Oligonucleotide Probes; Placenta; Placenta - physiology; Placenta Growth Factor; Plasmids; Pregnancy; Pregnancy Proteins - analysis; Pregnancy Proteins - genetics; Pregnancy Proteins - pharmacology; Protein hormones. Growth factors. Cytokines; Proteins; Recombinant Proteins - analysis; Recombinant Proteins - pharmacology; Sequence Homology, Nucleic Acid; Transfection; Uterine Neoplasms; Vascular Endothelial Growth Factor A; Vascular Endothelial Growth Factors; vascular permeability factor
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.88.20.9267

A human cDNA coding for a protein related to the vascular permeability factor (VPF) was isolated from a term placenta cDNA library; we therefore named its product placenta growth factor (PIGF). PIGF is a 149-amino-acid-long protein and is highly homologous (53% identity) to the platelet-derived growth factor-like region of human VPF. Computer analyses reveal a putative signal peptide and two probable N-glycosylation sites in the PIGF protein, one of which is also conserved in human VPF. By using N-glycosidase F, tunicamycin, and specific antibodies produced in both chicken and rabbit, we demonstrate that PIGF, derived from transfected COS-1 cells, is actually N-glycosylated and secreted into the medium. In addition, PIGF, like VPF, proves to be a dimeric protein. Finally, a conditioned medium from COS-1 cells containing PIGF is capable of stimulating specifically the growth of CPA, a line of endothelial cells, in vitro.