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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
48
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pubmed:dateCreated |
1999-12-29
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pubmed:databankReference |
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pubmed:abstractText |
The cytoskeletal and/or nuclear matrix molecules responsible for morphological changes associated with apoptosis were identified using monoclonal antibodies (mAbs). We developed mAbs against Triton X-100-insoluble components of HL-60 cells pretreated with all-trans retinoic acid. In particular, one mAb recognized a 22-kDa protein that exhibited intriguing behavior by forming an aggregate and appearing as a speck during apoptosis induced by retinoic acid and other anti-tumor drugs. Cloning and sequencing of its cDNA revealed that this protein comprises 195 amino acids and that its C-terminal half has a caspase recruitment domain (CARD) motif, characteristic of numerous proteins involved in apoptotic signaling. We referred to this protein as ASC (apoptosis-associated speck-like protein containing a CARD). The ASC gene was mapped on chromosome 16p11.2-12. The antisense oligonucleotides of ASC were found to reduce the expression of ASC, and consequently, etoposide-mediated apoptosis of HL-60 cells was suppressed. Our results indicate that ASC is a novel member of the CARD-containing adaptor protein family.
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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 |
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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 |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33835-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10567338-Amino Acid Sequence,
pubmed-meshheading:10567338-Animals,
pubmed-meshheading:10567338-Apoptosis,
pubmed-meshheading:10567338-Base Sequence,
pubmed-meshheading:10567338-COS Cells,
pubmed-meshheading:10567338-Caspases,
pubmed-meshheading:10567338-Chromosome Mapping,
pubmed-meshheading:10567338-Chromosomes, Human, Pair 16,
pubmed-meshheading:10567338-Cloning, Molecular,
pubmed-meshheading:10567338-Cytoskeletal Proteins,
pubmed-meshheading:10567338-DNA, Complementary,
pubmed-meshheading:10567338-DNA Fragmentation,
pubmed-meshheading:10567338-Female,
pubmed-meshheading:10567338-Gene Expression,
pubmed-meshheading:10567338-HL-60 Cells,
pubmed-meshheading:10567338-HeLa Cells,
pubmed-meshheading:10567338-Humans,
pubmed-meshheading:10567338-In Situ Nick-End Labeling,
pubmed-meshheading:10567338-Jurkat Cells,
pubmed-meshheading:10567338-K562 Cells,
pubmed-meshheading:10567338-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:10567338-Molecular Sequence Data,
pubmed-meshheading:10567338-Molecular Weight,
pubmed-meshheading:10567338-Protein Structure, Tertiary,
pubmed-meshheading:10567338-RNA, Messenger,
pubmed-meshheading:10567338-Recombinant Fusion Proteins,
pubmed-meshheading:10567338-Sequence Alignment,
pubmed-meshheading:10567338-Sequence Analysis, DNA,
pubmed-meshheading:10567338-Sequence Homology, Amino Acid,
pubmed-meshheading:10567338-Tissue Distribution,
pubmed-meshheading:10567338-Tumor Cells, Cultured
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pubmed:year |
1999
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pubmed:articleTitle |
ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells.
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pubmed:affiliation |
Department of Molecular Oncology, Research Center on Aging and Adaptation, Shinshu University School of Medicine, Asahi 3-1-1, Matsumoto 390-8621, Nagano, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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