Open AccessStructural evidence that endothelial cell growth factor beta is the precursor of both endothelial cell growth factor alpha and acidic fibroblast growth factor.
Author(s) -
Wilson H. Burgess,
Tevie Mehlman,
Daniel R. Marshak,
Blair A. Fraser,
Thomas Maciag
Publication year - 1986
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.83.19.7216
Subject(s) - amino acid , peptide sequence , biology , beta (programming language) , growth factor , fibroblast , alpha (finance) , fibroblast growth factor , biochemistry , basic fibroblast growth factor , microbiology and biotechnology , gene , receptor , medicine , construct validity , nursing , patient satisfaction , computer science , in vitro , programming language
Two endothelial cell growth factors (ECGF) have been purified from bovine brain and termed alpha- and beta-ECGF [Burgess, W. H., Mehlman, T., Friesel, R., Johnson, W. V. & Maciag, T. (1985) J. Biol. Chem. 260, 11389-11392]. Amino acid sequence analysis indicates that beta-ECGF represents a 20 amino acid amino-terminal extension of alpha-ECGF and a 14 amino acid amino-terminal extension of acidic fibroblast growth factor. These data indicate that both alpha-ECGF and acidic fibroblast growth factor may be derived from beta-ECGF by posttranslational processing. Analysis of the amino-terminal 14 residues of beta-ECGF by fast-atom-bombardment mass spectrometry established the amino acid sequence of this region and the identity of the blocking group at the amino terminus (acetyl).