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rdf:type |
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lifeskim:mentions |
umls-concept:C0009968,
umls-concept:C0030685,
umls-concept:C0079349,
umls-concept:C0149784,
umls-concept:C0205263,
umls-concept:C0332621,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1706853,
umls-concept:C1879748,
umls-concept:C1963578
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pubmed:issue |
27
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pubmed:dateCreated |
2001-7-2
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pubmed:abstractText |
Fibroblast growth factor (FGF) 1 is known to be released in response to stress conditions as a component of a multiprotein aggregate containing the p40 extravescicular domain of p65 synaptotagmin (Syt) 1 and S100A13. Since FGF1 is a Cu2+-binding protein and Cu2+ is known to induce its dimerization, we evaluated the capacity of recombinant FGF1, p40 Syt1, and S100A13 to interact in a cell-free system and the role of Cu2+ in this interaction. We report that FGF1, p40 Syt1, and S100A13 are able to bind Cu2+ with similar affinity and to interact in the presence of Cu2+ to form a multiprotein aggregate which is resistant to low concentrations of SDS and sensitive to reducing conditions and ultracentrifugation. The formation of this aggregate in the presence of Cu2+ is dependent on the presence of S100A13 and is mediated by cysteine-independent interactions between S100A13 and either FGF1 or p40 Syt1. Interestingly, S100A13 is also able to interact in the presence of Cu2+ with Cys-free FGF1 and this observation may account for the ability of S100A13 to export Cys-free FGF1 in response to stress. Lastly, tetrathiomolybdate, a Cu2+ chelator, significantly represses in a dose-dependent manner the heat shock-induced release of FGF1 and S100A13. These data suggest that S100A13 may be involved in the assembly of the multiprotein aggregate required for the release of FGF1 and that Cu2+ oxidation may be an essential post-translational intracellular modifier of this process.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Fibroblast Growth Factor 2,
http://linkedlifedata.com/resource/pubmed/chemical/Molybdenum,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/S100 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/S100A13 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SYT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Dodecyl Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmin I,
http://linkedlifedata.com/resource/pubmed/chemical/tetrathiomolybdate
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25549-57
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11432880-Animals,
pubmed-meshheading:11432880-Cell-Free System,
pubmed-meshheading:11432880-Copper,
pubmed-meshheading:11432880-Cysteine,
pubmed-meshheading:11432880-Detergents,
pubmed-meshheading:11432880-Dimerization,
pubmed-meshheading:11432880-Fibroblast Growth Factor 1,
pubmed-meshheading:11432880-Fibroblast Growth Factor 2,
pubmed-meshheading:11432880-Humans,
pubmed-meshheading:11432880-Molybdenum,
pubmed-meshheading:11432880-Nerve Tissue Proteins,
pubmed-meshheading:11432880-Oxidation-Reduction,
pubmed-meshheading:11432880-Peptide Fragments,
pubmed-meshheading:11432880-Rabbits,
pubmed-meshheading:11432880-S100 Proteins,
pubmed-meshheading:11432880-Sodium Dodecyl Sulfate,
pubmed-meshheading:11432880-Stress, Physiological,
pubmed-meshheading:11432880-Synaptotagmin I
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pubmed:year |
2001
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pubmed:articleTitle |
Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress.
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pubmed:affiliation |
Center for Molecular Medicine, Maine Medical Center Research Institute, Scarborough, Maine 04074, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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