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Titolo:
Crucial role of calpain in hypoxic PC12 cell death: Calpain, but not caspases, mediates degradation of cytoskeletal proteins and protein kinase C-alpha and -delta
Autore:
Yamakawa, H; Banno, Y; Nakashima, S; Yoshimura, S; Sawada, M; Nishimura, Y; Nozawa, Y; Sakai, N;
Indirizzi:
Gifu Univ, Sch Med, Dept Neurosurg, Gifu 5008705, Japan Gifu Univ Gifu Japan 5008705 ch Med, Dept Neurosurg, Gifu 5008705, Japan Gifu Univ, Sch Med, Dept Biochem, Gifu 500, Japan Gifu Univ Gifu Japan 500 fu Univ, Sch Med, Dept Biochem, Gifu 500, Japan Gifu Int Inst Biotechnol, Gifu, Japan Gifu Int Inst Biotechnol Gifu Japan fu Int Inst Biotechnol, Gifu, Japan Inst Appl Biochem, Gifu, Japan Inst Appl Biochem Gifu JapanInst Appl Biochem, Gifu, Japan
Titolo Testata:
NEUROLOGICAL RESEARCH
fascicolo: 5, volume: 23, anno: 2001,
pagine: 522 - 530
SICI:
0161-6412(200107)23:5<522:CROCIH>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRIMARY SEPTOHIPPOCAMPAL CULTURES; PROTEOLYTIC ACTIVATION; CERAMIDE FORMATION; INDUCED APOPTOSIS; NEUTROPHIL APOPTOSIS; NEUROBLASTOMA-CELLS; DNA FRAGMENTATION; INHIBITION; PHOSPHORYLATION; DIFFERENTIATION;
Keywords:
hypoxia; neuronal death; Ca2+; protein kinase C; calpain; caspase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Yamakawa, H Gifu Univ, Sch Med, Dept Neurosurg, Tsukasa Machi 40, Gifu 5008705, Japan Gifu Univ Tsukasa Machi 40 Gifu Japan 5008705 5008705, Japan
Citazione:
H. Yamakawa et al., "Crucial role of calpain in hypoxic PC12 cell death: Calpain, but not caspases, mediates degradation of cytoskeletal proteins and protein kinase C-alpha and -delta", NEUROL RES, 23(5), 2001, pp. 522-530

Abstract

Ca2+ influx is one of the main causative events in hypoxic PC12 cell death, because an extracellular Ca2+ chelator:, ethylene glycol bis (2-aminoethyl ether)-N,N,N ' ,N ' -tetraacetic acid (EGTA) inhibited and Ca2+ ionophoreA23187 mimicked the hypoxic cell death. The hypoxic cell death was markedly prevented by a broad spectrum caspase inhibitor, benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone (z-VAD-FMK) as well as a calpain inhibitor, calpeptin, as assessed by nuclear staining with Hoechst 33258 and lactate dehydrogenase release. The processing of procaspase-3 was inhibited by z-VAD-FMK, bot not by calpeptin. in contrast, z-VAD-FMK failed to block the proteolytic cleavage of fodrin-alpha a preferential substrate for calpain. On the other hand, degradation of actin and fodrin-alpha was prevented by calpeptin but nor by z-VAD-FMK. In addition, not only protein kinase C (PKC)-alpha butalso PKC-delta were cleaved to generate similar to 46 kDa fragments The PKC fragmentation was inhibited by calpeptin but not by z-VAD-FMK. These findings suggest that the extracellular Ca2+ influx induced by hypoxic stress activates calpain, resulting in the degradation of cytoskeletal proteins andgeneration of PKC fragments almost independently of caspase activation. Therefore, calpain may play an important role in hypoxic PC12 cell death.

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Documento generato il 05/07/20 alle ore 13:31:12