ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells.
J Biol Chem
; 274(48): 33835-8, 1999 Nov 26.
Article
de En
| MEDLINE
| ID: mdl-10567338
ABSTRACT
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.
Recherche sur Google
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Apoptose
/
Cellules HL-60
/
Protéines du cytosquelette
Type d'étude:
Prognostic_studies
Langue:
En
Journal:
J Biol Chem
Année:
1999
Type de document:
Article
Pays d'affiliation:
Japon