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Titolo:
Calpain-mediated proteolytic cleavage of troponin I induced by hypoxia or metabolic inhibition in cultured neonatal cardiomyocytes
Autore:
Kositprapa, C; Zhang, BC; Berger, S; Canty, JM; Lee, TC;
Indirizzi:
SUNY Buffalo, Dept Biochem Med & Physiol, Buffalo, NY 14214 USA SUNY Buffalo Buffalo NY USA 14214 em Med & Physiol, Buffalo, NY 14214 USA Western New York Hlth Care Syst, Dept Vet Affairs, Buffalo, NY USA WesternNew York Hlth Care Syst Buffalo NY USA Affairs, Buffalo, NY USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOCHEMISTRY
fascicolo: 1, volume: 214, anno: 2000,
pagine: 47 - 55
SICI:
0300-8177(200011)214:1<47:CPCOTI>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
NEUTRAL PROTEASE CALPAIN; RAT CARDIAC MYOCYTES; CELL-DEATH; STUNNED MYOCARDIUM; INDUCED APOPTOSIS; ISCHEMIA/REPERFUSION INJURY; HIBERNATING MYOCARDIUM; CONTRACTILE PROTEINS; TRANSCRIPTION FACTOR; ACTIVATION;
Keywords:
calpain; myofilament; troponin I; hypoxia;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Lee, TC SUNY Buffalo, Dept Biochem, 3435 Main St, Buffalo, NY 14214 USA SUNY Buffalo 3435 Main St Buffalo NY USA 14214 ffalo, NY 14214 USA
Citazione:
C. Kositprapa et al., "Calpain-mediated proteolytic cleavage of troponin I induced by hypoxia or metabolic inhibition in cultured neonatal cardiomyocytes", MOL C BIOCH, 214(1), 2000, pp. 47-55

Abstract

While ischemic damage to myofibrillar proteins is thought to be responsible in part for depressed cardiac function, the relation between myofilament protein breakdown and chronic hypoxia has not been defined. We previously characterized a chemical hypoxia model of neonatal cardiomyocytes mediated by 1 mM azide that exhibits features of calpain activation (Mol Cell Biochem178:141-149, 1998). We here show that both hypoxia and azide-mediated metabolic inhibition induced heme oxygenase-1 expression, and caused cell deathassociated with lipid peroxidation. While blocking calcium influx or inhibiting calpain activity efficiently attenuated hypoxia-induced cell injury, it failed to prevent cell injury caused by adenoviral overexpression of thetumor suppressor protein p53. Inhibitors of caspases, on the other hand, suppressed cell injury caused by p53 overexpression. Hypoxia caused selective cleavage of troponin I (TnI), which could be suppressed by either nifedipine or calpeptin. Other myofilament proteins such as troponin T, myosin heavy chain, and actin appeared to remain largely intact. p53-mediated cell injury exhibited proteolysis of the caspase protein substrate lamin B withoutappreciable breakdown of TnI. We suggest that calpain-induced TnI breakdown may constitute a unique biochemical marker associated with chronically hypoxic cardiomyocytes.

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Documento generato il 25/09/20 alle ore 00:35:10