Mitogenic properties of a new endothelial cell growth factor related to pleiotrophin.
A growth factor was isolated from a neutral pH extract of adult bovine brain. Purification of this polypeptide was achieved by a three step procedure including cationic exchange, heparin-Sepharose affinity and Mono S chromatography. This heparin binding protein had a molecular weight of 18,000 as assessed by silver-stained SDS-PAGE and was not immunologically and structurally related to acidic or basic FGF. Freshly purified protein had a maximal mitogenic effect on bovine brain capillary cells at a concentration of 100 pM. Microsequencing revealed an unique amino-terminal sequence homologous to heparin-binding growth-associated molecule (HB-GAM), a neuronal maturation protein, to pleiotrophin (PTN), a fibroblast cell growth factor and to one form of the putative protein product of the MK gene, a retinoic acid induced-gene.
Courty
J
J
Laboratoire de Biotechnologie des Cellules Eucaryotes, Université Paris Val de Marne, Créteil, France.
Dauchel
M C
MC
Caruelle
D
D
Perderiset
M
M
Barritault
D
D
D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D002352:Carrier Proteins; D002417:Cattle; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D016207:Cytokines / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D016228:Endothelial Growth Factors / Q000737:chemistry*; D008934:Mitogens / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
D002352:Carrier Proteins; D016207:Cytokines; D016228:Endothelial Growth Factors; D008934:Mitogens; C066845:pleiotrophin