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Titolo:
Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2 alpha
Autore:
Gotzmann, J; Vlcek, S; Foisner, R;
Indirizzi:
Univ Vienna, Bioctr, Dept Biochem & Mol Cell Biol, A-1030 Vienna, Austria Univ Vienna Vienna Austria A-1030 Mol Cell Biol, A-1030 Vienna, Austria Univ Vienna, Inst Canc Res, A-1090 Vienna, Austria Univ Vienna Vienna Austria A-1090 Inst Canc Res, A-1090 Vienna, Austria
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 21, volume: 113, anno: 2000,
pagine: 3769 - 3780
SICI:
0021-9533(200011)113:21<3769:CCOTCD>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENVELOPE INNER MEMBRANE; DREIFUSS MUSCULAR-DYSTROPHY; NUCLEAR-ENVELOPE; CHROMODOMAIN PROTEINS; DYNAMIC ORGANIZATION; APOPTOTIC THYMOCYTES; DNA FRAGMENTATION; TARGETING DOMAIN; INTEGRAL PROTEIN; CELL-CYCLE;
Keywords:
apoptosis; caspase; chromatin organization; lamina-associated polypeptide; nuclear lamina;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Foisner, R Univ Vienna, Bioctr, Dept Biochem & Mol Cell Biol, Waehringer Guertel 18, A-1030 Vienna, Austria Univ Vienna Waehringer Guertel 18 ViennaAustria A-1030 ustria
Citazione:
J. Gotzmann et al., "Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2 alpha", J CELL SCI, 113(21), 2000, pp. 3769-3780

Abstract

Lamina-associated polypeptide 2 alpha (LAP2 alpha) is a nonmembrane-bound isoform of the LAP2 family involved in nuclear structure organization. Using various cell systems, including Jurkat, HL-60, and HeLa cells, and different death-inducing agents, such as anti-Fas antibody, topoisomerase inhibitors, and staurosporine, we found that LAP2 alpha was cleaved during apoptosis as rapidly as lamin B in a caspase-dependent manner yielding stable N- and C-terminal fragments of approximately 50 and 28 kDa, respectively. Basedon fragment size and localization of immunoreactive epitopes, four potential cleavage sites were mapped between amino acids 403-485, These sites werelocated within a domain that has previously been described to be essentialand sufficient for association of LAP2 alpha with chromosomes, suggesting that LAP2 alpha cleavage impairs its chromatin-binding properties. Immunofluorescence microscopy demonstrated that, unlike full length protein, apoptotic fragments did not colocalize with condensed chromatin, but remained in the nuclear compartment as long as a single nucleus was visible. Subfractionation analyses:showed that the N-terminal LAP2 alpha fragment was extracted from intranuclear structures in detergent/salt buffers, whereas the C-terminal fragment remained associated with a residual framework devoid of chromatin, Our data suggest that early cleavage of LAP2 alpha is important for chromatin reorganization during apoptosis.

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Documento generato il 02/06/20 alle ore 20:34:02