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rdf:type |
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lifeskim:mentions |
umls-concept:C0007587,
umls-concept:C0024660,
umls-concept:C0033684,
umls-concept:C0162610,
umls-concept:C0162638,
umls-concept:C0205314,
umls-concept:C0333516,
umls-concept:C0537969,
umls-concept:C0679622,
umls-concept:C1332666,
umls-concept:C1334043,
umls-concept:C1879547
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pubmed:issue |
3
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pubmed:dateCreated |
1996-3-11
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pubmed:databankReference |
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pubmed:abstractText |
Members of the ICE/ced-3 gene family have been implicated as components of the cell death pathway. Based on similarities with the structural prototype interleukin-1 beta-converting enzyme (ICE), family members are synthesized as proenzymes that are proteolytically processed to form active heterodimeric enzymes. In this report, we describe a novel member of this growing gene family, ICE-LAP3, which is closely related to the death effector Yama/CPP32/Apopain. Pro-ICE-LAP3 is a 35-kDa protein localized to the cytoplasm and expressed in a variety of tissues and cell lines. Overexpression of a truncated version of ICE-LAP3 (missing the pro-domain) induces apoptosis in MCF7 breast carcinoma cells. Importantly, upon receipt of a death stimulus, endogenous ICE-LAP3 is processed to its subunit forms, suggesting a physiological role in cell death. This is the first report to demonstrate processing of a native ICE/ced-3 family member during execution of the death program and the first description of the subcellular localization of an ICE/ced-3 family member.
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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/Antigens, CD95,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/ced-3 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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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 |
19
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1621-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8576161-Adult,
pubmed-meshheading:8576161-Amino Acid Sequence,
pubmed-meshheading:8576161-Animals,
pubmed-meshheading:8576161-Antigens, CD95,
pubmed-meshheading:8576161-Apoptosis,
pubmed-meshheading:8576161-Base Sequence,
pubmed-meshheading:8576161-Breast Neoplasms,
pubmed-meshheading:8576161-Caenorhabditis elegans,
pubmed-meshheading:8576161-Caenorhabditis elegans Proteins,
pubmed-meshheading:8576161-Caspase 7,
pubmed-meshheading:8576161-Caspases,
pubmed-meshheading:8576161-Cell Line,
pubmed-meshheading:8576161-Cysteine Endopeptidases,
pubmed-meshheading:8576161-DNA Primers,
pubmed-meshheading:8576161-Female,
pubmed-meshheading:8576161-Fetus,
pubmed-meshheading:8576161-Gene Expression,
pubmed-meshheading:8576161-Helminth Proteins,
pubmed-meshheading:8576161-Humans,
pubmed-meshheading:8576161-Molecular Sequence Data,
pubmed-meshheading:8576161-Multigene Family,
pubmed-meshheading:8576161-Polymerase Chain Reaction,
pubmed-meshheading:8576161-Protein Biosynthesis,
pubmed-meshheading:8576161-Protein Precursors,
pubmed-meshheading:8576161-Proteins,
pubmed-meshheading:8576161-Rats,
pubmed-meshheading:8576161-Recombinant Proteins,
pubmed-meshheading:8576161-Sequence Homology, Amino Acid,
pubmed-meshheading:8576161-Tumor Cells, Cultured,
pubmed-meshheading:8576161-Tumor Necrosis Factor-alpha
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pubmed:year |
1996
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pubmed:articleTitle |
ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis.
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pubmed:affiliation |
Department of Pathology, University of Michigan Medical School, Ann Arbor, 48109, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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