Source:http://linkedlifedata.com/resource/pubmed/id/16300929
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2006-5-15
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pubmed:abstractText |
Platelets express, among others, initiator caspase 9 and effector caspase 3. Upon activation by physiological agonists, calcium ionophores or under shear stress they might develop apoptotic events. Although it is well known that the cytoskeletal network plays a crucial role in apoptosis, the relationship between caspases 3 and 9 and the cytoskeleton is poorly understood. Here we demonstrate that the physiological agonist thrombin is able to induce activation of caspases 3 and 9 in human platelets and significantly increases the amount in the cytoskeleton of the active forms of both caspases and the procaspases 3 and 9. After stimulation with thrombin the amount of active caspases 3 and 9 in the cytosolic and cytoskeletal fractions were significantly reduced in Ro-31-8220-treated cells, which demonstrates that caspases activation and association with the cytoskeleton needs the contribution of PKC. Inhibition of actin polymerization by cytochalasin D inhibits translocation and activation of both caspases, suggesting that thrombin stimulates caspase 3 and 9 activation and association with the reorganizing actin cytoskeleton. Finally, our results show that inhibition of thrombin-induced caspase activation has no effect on their translocation to the cytoskeleton although impairment of thrombin-evoked caspase translocation has negative effects on caspase activity, suggesting that translocation to the cytoskeleton might be important for caspase activation by thrombin in human platelets.
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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/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 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 9,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin D,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0898-6568
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pubmed:author | |
pubmed:issnType |
Print
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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 |
1252-61
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:16300929-Actin Cytoskeleton,
pubmed-meshheading:16300929-Biopolymers,
pubmed-meshheading:16300929-Blood Platelets,
pubmed-meshheading:16300929-Caspase 3,
pubmed-meshheading:16300929-Caspase 9,
pubmed-meshheading:16300929-Caspases,
pubmed-meshheading:16300929-Cytochalasin D,
pubmed-meshheading:16300929-Cytosol,
pubmed-meshheading:16300929-Enzyme Activation,
pubmed-meshheading:16300929-Humans,
pubmed-meshheading:16300929-Protein Kinase C,
pubmed-meshheading:16300929-Protein Transport,
pubmed-meshheading:16300929-Thrombin
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pubmed:year |
2006
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pubmed:articleTitle |
Caspases 3 and 9 are translocated to the cytoskeleton and activated by thrombin in human platelets. Evidence for the involvement of PKC and the actin filament polymerization.
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pubmed:affiliation |
Unité de Recherche de Biochimie, Inst. Superieur de Biotechnologie, Monastir, Tunisia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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