Mitogenic properties of a new endothelial cell growth factor related to pleiotrophin

Biochem Biophys Res Commun. 1991 Oct 15;180(1):145-51. doi: 10.1016/s0006-291x(05)81267-7.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain Chemistry
  • Carrier Proteins*
  • Cattle
  • Chromatography, Affinity
  • Chromatography, Ion Exchange
  • Cytokines / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel
  • Endothelial Growth Factors / chemistry*
  • Mitogens / isolation & purification*
  • Molecular Sequence Data
  • Sequence Homology, Nucleic Acid


  • Carrier Proteins
  • Cytokines
  • Endothelial Growth Factors
  • Mitogens
  • pleiotrophin