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rdf:type |
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lifeskim:mentions |
umls-concept:C0014239,
umls-concept:C0027540,
umls-concept:C0030685,
umls-concept:C0054543,
umls-concept:C0162610,
umls-concept:C0182953,
umls-concept:C0391871,
umls-concept:C0542341,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1546857,
umls-concept:C1963578
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pubmed:issue |
6
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pubmed:dateCreated |
2001-10-2
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pubmed:abstractText |
In C. elegans, a hyperactivated MEC-4(d) ion channel induces necrotic-like neuronal death that is distinct from apoptosis. We report that null mutations in calreticulin suppress both mec-4(d)-induced cell death and the necrotic cell death induced by expression of a constitutively activated Galpha(S) subunit. RNAi-mediated knockdown of calnexin, mutations in the ER Ca(2+) release channels unc-68 (ryanodine receptor) or itr-1 (inositol 1,4,5 triphosphate receptor), and pharmacological manipulations that block ER Ca(2+) release also suppress death. Conversely, thapsigargin-induced ER Ca(2+) release can restore mec-4(d)-induced cell death when calreticulin is absent. We conclude that high [Ca(2+)](i) is a requirement for necrosis in C. elegans and suggest that an essential step in the death mechanism is release of ER-based Ca(2+) stores. ER-driven Ca(2+) release has previously been implicated in mammalian necrosis, suggesting necrotic death mechanisms may be conserved.
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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/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calnexin,
http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ITPR1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Mec-4 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ryanodine Receptor Calcium Release...,
http://linkedlifedata.com/resource/pubmed/chemical/Thapsigargin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
957-71
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11580896-Amino Acid Sequence,
pubmed-meshheading:11580896-Animals,
pubmed-meshheading:11580896-Animals, Genetically Modified,
pubmed-meshheading:11580896-Caenorhabditis elegans,
pubmed-meshheading:11580896-Caenorhabditis elegans Proteins,
pubmed-meshheading:11580896-Calcium Channels,
pubmed-meshheading:11580896-Calcium Signaling,
pubmed-meshheading:11580896-Calcium-Binding Proteins,
pubmed-meshheading:11580896-Calnexin,
pubmed-meshheading:11580896-Calreticulin,
pubmed-meshheading:11580896-Cell Size,
pubmed-meshheading:11580896-Chromosome Mapping,
pubmed-meshheading:11580896-Endoplasmic Reticulum,
pubmed-meshheading:11580896-Helminth Proteins,
pubmed-meshheading:11580896-Heterotrimeric GTP-Binding Proteins,
pubmed-meshheading:11580896-Homeostasis,
pubmed-meshheading:11580896-Humans,
pubmed-meshheading:11580896-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:11580896-Ion Transport,
pubmed-meshheading:11580896-Larva,
pubmed-meshheading:11580896-Membrane Proteins,
pubmed-meshheading:11580896-Molecular Sequence Data,
pubmed-meshheading:11580896-Mutation,
pubmed-meshheading:11580896-Necrosis,
pubmed-meshheading:11580896-Nerve Degeneration,
pubmed-meshheading:11580896-Nerve Tissue Proteins,
pubmed-meshheading:11580896-Neurons,
pubmed-meshheading:11580896-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:11580896-Recombinant Fusion Proteins,
pubmed-meshheading:11580896-Ribonucleoproteins,
pubmed-meshheading:11580896-Ryanodine Receptor Calcium Release Channel,
pubmed-meshheading:11580896-Sequence Alignment,
pubmed-meshheading:11580896-Sequence Homology, Amino Acid,
pubmed-meshheading:11580896-Structure-Activity Relationship,
pubmed-meshheading:11580896-Thapsigargin,
pubmed-meshheading:11580896-Touch
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pubmed:year |
2001
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pubmed:articleTitle |
Necrotic cell death in C. elegans requires the function of calreticulin and regulators of Ca(2+) release from the endoplasmic reticulum.
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pubmed:affiliation |
Department of Molecular Biology and Biochemistry, A232, Nelson Biological Laboratories, Rutgers, The State University of New Jersey, 604 Allison Road, Piscataway, NJ 08855, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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