Open AccessBrain-derived fibroblast growth factor: identity with a fragment of the basic protein of myelin.
Author(s) -
Fred C. Westall,
Vanda A. Len,
Denis Gospodarowicz
Publication year - 1978
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.75.10.4675
Subject(s) - myelin , myelin basic protein , fibroblast growth factor , proteolysis , basic fibroblast growth factor , biochemistry , fibroblast , biology , homologous chromosome , central nervous system , chemistry , growth factor , in vitro , endocrinology , enzyme , receptor , gene
Fibroblast growth factors (FGF) isolated from bovine brain have been identified chemically and immunologically as components of the myelin basic protein. The intact bovine basic protein molecule (170 residues), prepared by the standard acid extraction procedure, lacked mitogenic activity (tested at concentrations up to 10 microgram/ml). However, the polypeptide FGF-2, identified as residues 44-153 of the basic protein, was maximally mitogenic for fibroblasts at 10 ng/ml and polypeptide 44-166 (FGF-1) was maximally active at 100 ng/ml. Pituitary-derived FGF is a potent a growth factor as FGF-2, but appears to be biochemically and immunologically distinct from brain-derived FGF. FGF released in the central or peripheral nervous system as a consequence of myelin damage and basic protein proteolysis could provide a physiological stimulus for wound healing and myelin repair.