Linked Life Data

9712834

Source:http://linkedlifedata.com/resource/pubmed/id/9712834

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1998-9-24
pubmed:abstractText
The heparin-binding fibroblast growth factor (FGF) prototypes lack a classical signal sequence, yet their presence is required in the extracellular compartment for the activation of cell-surface receptor-dependent signaling. Early studies with FGF-1 demonstrated its presence in bovine brain as a novel high molecular weight complex, and subsequent studies identified a second heparin-binding protein that co-purified with FGF-1. Polypeptide sequence analysis revealed that this heparin-binding protein corresponded to the extravesicular domain of bovine synaptotagmin (Syn)-1, a transmembrane component of synaptic vesicles involved in the regulation of organelle traffic. Since FGF-1 is released in response to heat shock as a mitogenically inactive Cys-30 homodimer, we sought to determine whether this heparin-binding protein was involved in the release of FGF-1. We report that a proteolytic fragment of the extravesicular domain of Syn-1 is associated with FGF-1 in the extracellular compartment of FGF-1-transfected NIH 3T3 cells following temperature stress. By using heparin-Sepharose affinity to discriminate between the monomer and homodimer forms of FGF-1 and resolution by conventional and limited denaturant gel shift immunoblot analysis, it was possible to identify FGF-1 and Syn-1 as potential components of a denaturant- and reducing agent-sensitive extracellular complex. It was also possible to demonstrate that the expression of an antisense-Syn-1 gene represses the release of FGF-1 in response to heat shock. These data indicate that FGF-1 may be able to utilize the cytosolic face of conventional exocytotic vesicles to traffic to the inner surface of the plasma membrane where it may gain access to the extracellular compartment as a complex with Syn-1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22209-16
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9712834-3T3 Cells, pubmed-meshheading:9712834-Ammonium Sulfate, pubmed-meshheading:9712834-Animals, pubmed-meshheading:9712834-Base Sequence, pubmed-meshheading:9712834-Brain, pubmed-meshheading:9712834-Calcium-Binding Proteins, pubmed-meshheading:9712834-Cattle, pubmed-meshheading:9712834-Culture Media, Conditioned, pubmed-meshheading:9712834-DNA Primers, pubmed-meshheading:9712834-Dimerization, pubmed-meshheading:9712834-Fibroblast Growth Factors, pubmed-meshheading:9712834-Heat-Shock Response, pubmed-meshheading:9712834-Heparin, pubmed-meshheading:9712834-Membrane Glycoproteins, pubmed-meshheading:9712834-Mice, pubmed-meshheading:9712834-Nerve Tissue Proteins, pubmed-meshheading:9712834-Oxidation-Reduction, pubmed-meshheading:9712834-Protein Denaturation, pubmed-meshheading:9712834-Synaptotagmin I, pubmed-meshheading:9712834-Synaptotagmins
pubmed:year
1998
pubmed:articleTitle
The extravesicular domain of synaptotagmin-1 is released with the latent fibroblast growth factor-1 homodimer in response to heat shock.
pubmed:affiliation
Center for Molecular Medicine, Maine Medical Center Research Institute, South Portland, Maine 04106, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.