[HTML][HTML] The cysteine residue responsible for the release of fibroblast growth factor-1 resides in a domain independent of the domain for phosphatidylserine binding
F Tarantini, S Gamble, A Jackson, T Maciag - Journal of Biological …, 1995 - ASBMB
Fibroblast growth factor (FGF)-1 lacks a classical signal sequence to direct its secretion yet
utilizes high affinity cell surface receptors to signal its heparin-dependent angiogenic and
neurotrophic activities. We have previously reported that FGF-1 is released in response to
temperature stress as a latent homodimer through a pathway that is potentiated by the Golgi
inhibitor, brefeldin A (Jackson, A., Tarantini, F., Gamble, S., Friedman, S., and Maciag,
T.(1995) J. Biol. Chem. 270, 33-36). In an attempt to further characterize this unconventional …
utilizes high affinity cell surface receptors to signal its heparin-dependent angiogenic and
neurotrophic activities. We have previously reported that FGF-1 is released in response to
temperature stress as a latent homodimer through a pathway that is potentiated by the Golgi
inhibitor, brefeldin A (Jackson, A., Tarantini, F., Gamble, S., Friedman, S., and Maciag,
T.(1995) J. Biol. Chem. 270, 33-36). In an attempt to further characterize this unconventional …