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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
31
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pubmed:dateCreated |
1993-11-29
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pubmed:abstractText |
We studied the abundance, subcellular distribution of a non-receptor protein-tyrosine kinase p72syk (Taniguchi, T., Kobayashi, T., Kondo, J., Takahashi, K., Nakamura, H., Suzuki, J., Nagai, K., Yamada, T., Nakamura, S., and Yamamura, H. (1991) J. Biol. Chem. 266, 15790-15796) in porcine polymorphonuclear neutrophils and the activation upon the stimulation with concanavalin A. The abundance was about 0.1% of total proteins and mainly distributed in the particulate fraction. Upon concanavalin A stimulation, the activity of p72syk increased within 30 s, attained to the maximum level at 1 min, and then returned to the basal level within 6 min. This activation was observed in a dose-dependent manner and abrogated by simultaneous addition of methyl alpha-mannopyranoside. When both extra- and intracellular Ca2+ were depleted, the activation of p72syk was still persistent; in contrast, the deactivation process was completely abrogated even at 6 min after stimulation. The replenishment of Ca2+ in the presence of A23187 resulted in a similar deactivation pattern as seen in the Ca(2+)-rich condition. In addition, genistein and herbimycin A, potent protein-tyrosine-kinase inhibitors, were capable of reducing concanavalin A-evoked p72syk activation and Ca2+ mobilization as well as the aggregation and lysozyme release. Furthermore, A23187-induced Ca2+ accumulation in inhibitor-treated cells resulted in the restoration of those cellular responses. These lines of evidence suggest that p72syk is activated with concanavalin A in a Ca(2+)-independent manner, participating in a mechanism of Ca2+ recruitment, and negatively regulated by a feedback mechanism through Ca2+ in neutrophils.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Concanavalin A,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Genistein,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Isoflavones,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
268
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pubmed:geneSymbol |
syk
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23334-8
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:8226857-Animals,
pubmed-meshheading:8226857-Calcium,
pubmed-meshheading:8226857-Cell Compartmentation,
pubmed-meshheading:8226857-Concanavalin A,
pubmed-meshheading:8226857-Enzyme Activation,
pubmed-meshheading:8226857-Enzyme Precursors,
pubmed-meshheading:8226857-Genistein,
pubmed-meshheading:8226857-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:8226857-Isoflavones,
pubmed-meshheading:8226857-Neutrophils,
pubmed-meshheading:8226857-Protein-Tyrosine Kinases,
pubmed-meshheading:8226857-Swine
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pubmed:year |
1993
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pubmed:articleTitle |
Activation of protein-tyrosine kinase p72syk with concanavalin A in polymorphonuclear neutrophils.
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pubmed:affiliation |
Department of Biochemistry, Fukui Medical School, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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