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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
27
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pubmed:dateCreated |
1999-8-17
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pubmed:abstractText |
Ligation of Fas with its natural ligand or with anti-Fas antibodies induces an apoptotic program in Fas sensitive cells. We report here the identification of the tyrosine kinase p59Fyn as a substrate for CPP32-like proteinases and more particularly caspase 3 during Fas-mediated apoptosis in Jurkat T cells. Inhibition of CPP32-like proteinases by Ac-Asp-Glu-Val-Asp-aldehyde but not by Ac-Tyr-Val-Ala-Asp-aldehyde prevents CPP32, PARP and p59Fyn cleavage indicating that CPP32 or CPP32-like proteinases are responsible for the cleavage of p59Fyn. Cleavage occurs in the N-terminal domain of p59Fyn between Asp19 and Gly20 and is accompanied by relocation of an active p57Fyn kinase to cytoplasm of Fas-stimulated Jurkat cells as judged by both biochemical and confocal microscopy experiments. Thus, p59Fyn relocation and activity may play an important role during Fas-mediated cell death in human T lymphocytes.
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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/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CASP9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 8,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/FYN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fyn,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3963-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10435619-Antigens, CD95,
pubmed-meshheading:10435619-Apoptosis,
pubmed-meshheading:10435619-Caspase 3,
pubmed-meshheading:10435619-Caspase 8,
pubmed-meshheading:10435619-Caspase 9,
pubmed-meshheading:10435619-Caspases,
pubmed-meshheading:10435619-Clone Cells,
pubmed-meshheading:10435619-Humans,
pubmed-meshheading:10435619-Hydrolysis,
pubmed-meshheading:10435619-Jurkat Cells,
pubmed-meshheading:10435619-Myristic Acid,
pubmed-meshheading:10435619-Palmitic Acid,
pubmed-meshheading:10435619-Peptide Fragments,
pubmed-meshheading:10435619-Precipitin Tests,
pubmed-meshheading:10435619-Protein Processing, Post-Translational,
pubmed-meshheading:10435619-Protein-Tyrosine Kinases,
pubmed-meshheading:10435619-Proto-Oncogene Proteins,
pubmed-meshheading:10435619-Proto-Oncogene Proteins c-fyn,
pubmed-meshheading:10435619-Signal Transduction,
pubmed-meshheading:10435619-Substrate Specificity,
pubmed-meshheading:10435619-T-Lymphocytes,
pubmed-meshheading:10435619-src-Family Kinases
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pubmed:year |
1999
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pubmed:articleTitle |
Cleavage and relocation of the tyrosine kinase P59FYN during Fas-mediated apoptosis in T lymphocytes.
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pubmed:affiliation |
CJF 96.05 Activation des Cellules Hematopoietiques Faculté de Médecine, Nice, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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