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Volumn 76, Issue 6, 1995, Pages 1071-1078

Role of calcium-activated neutral protease (calpain) in cell death in cultured neonatal rat cardiomyocytes during metabolic inhibition

Author keywords

calcium activated neutral protease; cell death; metabolic inhibition; myocytes; protease inhibitors

Indexed keywords

BETA CASEIN; CALCIUM; CALPAIN; CALPASTATIN; DEOXYGLUCOSE; FLUORESCENT DYE; FURA 2 ACETOXYMETHYL ESTER; LACTATE DEHYDROGENASE; LEUPEPTIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; SODIUM CYANIDE; TECHNETIUM 99M;

EID: 0029050869     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.76.6.1071     Document Type: Article
Times cited : (87)

References (40)
  • 1
    • 0019814286 scopus 로고
    • The role of calcium in the ischemic myocardium
    • Nayler WG. The role of calcium in the ischemic myocardium. Am J Pathol. 1981;102:262-270.
    • (1981) Am J Pathol , vol.102 , pp. 262-270
    • Nayler, W.G.1
  • 2
    • 0025162269 scopus 로고
    • Correlation between cytosolic free calcium, contracture, ATP, and irreversible ischemic injury in perfused rat hearts
    • Steenbergen C, Murphy E, Watts JA, London RE. Correlation between cytosolic free calcium, contracture, ATP, and irreversible ischemic injury in perfused rat hearts. Circ Res. 1990;66:135-146.
    • (1990) Circ Res , vol.66 , pp. 135-146
    • Steenbergen, C.1    Murphy, E.2    Watts, J.A.3    London, R.E.4
  • 3
    • 0019570991 scopus 로고
    • 2+ sensitivity change and troponin loss in cardiac natural actomyosin after coronary occlusion
    • 2+ sensitivity change and troponin loss in cardiac natural actomyosin after coronary occlusion. Am J Physiol. 1981;240:H704-H708.
    • (1981) Am J Physiol , vol.240
    • Toyo-oka, T.1    Ross, J.R.2
  • 4
    • 0023257084 scopus 로고
    • Elevation of cytosolic free calcium concentration early in myocardial ischemia in perfused rat heart
    • Steenbergen C, Murphy E, Levy L, London RE. Elevation of cytosolic free calcium concentration early in myocardial ischemia in perfused rat heart. Circ Res. 1987;60:700-707.
    • (1987) Circ Res , vol.60 , pp. 700-707
    • Steenbergen, C.1    Murphy, E.2    Levy, L.3    London, R.E.4
  • 5
    • 0023038510 scopus 로고
    • Calcium activated neutral protease (milli-and microCANP) and endogenous CANP inhibitor of muscle in Duchenne muscular dystrophy (DMD)
    • Reddy PA, Anandavalli TE, Anandaraj MPJS. Calcium activated neutral protease (milli- and microCANP) and endogenous CANP inhibitor of muscle in Duchenne muscular dystrophy (DMD). Clin Chim Acta. 1986;160:281-288.
    • (1986) Clin Chim Acta , vol.160 , pp. 281-288
    • Reddy, P.A.1    Anandavalli, T.E.2    Anandaraj, M.P.J.S.3
  • 6
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • Saito KI, Elce JS, Hamos JE, Nixon RA. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A. 1993;90:2628-2632.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2628-2632
    • Saito, K.I.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 7
    • 0028098014 scopus 로고
    • Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia
    • Hong SC, Goto Y, Lanzino G, Soleau S, Kassell NF, Lee KS. Neuroprotection with a calpain inhibitor in a model of focal cerebral ischemia. Stroke. 1994;25:663-669.
    • (1994) Stroke , vol.25 , pp. 663-669
    • Hong, S.C.1    Goto, Y.2    Lanzino, G.3    Soleau, S.4    Kassell, N.F.5    Lee, K.S.6
  • 8
    • 0021721863 scopus 로고
    • Calcium-activated neutral protease (CANP) in brain and other tissues
    • Zimmerman U-JP, Schlaepfer A. Calcium-activated neutral protease (CANP) in brain and other tissues. Prog Neurobiol. 1984;23:63-78.
    • (1984) Prog Neurobiol , vol.23 , pp. 63-78
    • Zimmerman, U.-J.P.1    Schlaepfer, A.2
  • 10
    • 0027229472 scopus 로고
    • pH-Dependent nonlysosomal proteolysis contributes to lethal anoxic injury of rat hepatocytes
    • Bronk SF, Gores GJ. pH-Dependent nonlysosomal proteolysis contributes to lethal anoxic injury of rat hepatocytes. Am J Physiol. 1993;264:G744-G751.
    • (1993) Am J Physiol , vol.264
    • Bronk, S.F.1    Gores, G.J.2
  • 11
    • 0028057298 scopus 로고
    • Inhibition of nonlysosomal calcium-dependent proteolysis by glycine during anoxic injury of rat hepatocytes
    • Nichols JC, Bronk SF, Mellgren RL, Gores GJ. Inhibition of nonlysosomal calcium-dependent proteolysis by glycine during anoxic injury of rat hepatocytes. Gastroenterology. 1994;106:168-176.
    • (1994) Gastroenterology , vol.106 , pp. 168-176
    • Nichols, J.C.1    Bronk, S.F.2    Mellgren, R.L.3    Gores, G.J.4
  • 13
    • 0026475808 scopus 로고
    • Comparison of cell-permeable calpain inhibitors and E64 in reduction of cataract in cultured rat lenses
    • Lampi KJ, Kadoya K, Azuma M, David LL, Shearer TR. Comparison of cell-permeable calpain inhibitors and E64 in reduction of cataract in cultured rat lenses. Toxicol Appl Pharmacol. 1992;117:53-57.
    • (1992) Toxicol Appl Pharmacol , vol.117 , pp. 53-57
    • Lampi, K.J.1    Kadoya, K.2    Azuma, M.3    David, L.L.4    Shearer, T.R.5
  • 14
    • 0022608920 scopus 로고
    • Calcium-dependent proteolysis and its inhibition in the ischemic rat myocardium
    • Tolnai S, Korecky B. Calcium-dependent proteolysis and its inhibition in the ischemic rat myocardium. Can J Cardiol. 1986;2:42-47.
    • (1986) Can J Cardiol , vol.2 , pp. 42-47
    • Tolnai, S.1    Korecky, B.2
  • 15
    • 0027313425 scopus 로고
    • Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion
    • Yoshida K, Yamasaki Y, Kawashima S. Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion. Biochim Biophys Acta. 1993;1182:215-220.
    • (1993) Biochim Biophys Acta , vol.1182 , pp. 215-220
    • Yoshida, K.1    Yamasaki, Y.2    Kawashima, S.3
  • 16
    • 0027521309 scopus 로고
    • Effects of thiol protease inhibitors on fodrin degradation during hypoxia in cultured myocytes
    • Iizuka K, Kawaguchi H, Kitabatake A. Effects of thiol protease inhibitors on fodrin degradation during hypoxia in cultured myocytes. J Mol Cell Cardiol. 1993;25:1101-1109.
    • (1993) J Mol Cell Cardiol , vol.25 , pp. 1101-1109
    • Iizuka, K.1    Kawaguchi, H.2    Kitabatake, A.3
  • 17
    • 0022624613 scopus 로고
    • Temporary salvage of ischemic myocardium by the protease inhibitor bis[ethyl(2R,3R)-3-[(S)-methyl-1-[4-(2,3,4-trimethoxyphenyl-methyl)piperazin-1- ylcarbonyl]butyl-carbonyl]oxiran-2-carboxylate]sulfate
    • Toyo-oka T, Kamishiro T, Gotoh Y, Fumino H, Masaki T, Hosoda S. Temporary salvage of ischemic myocardium by the protease inhibitor bis[ethyl(2R,3R)-3-[(S)-methyl-1-[4-(2,3,4-trimethoxyphenyl-methyl)piperazin-1- ylcarbonyl]butyl-carbonyl]oxiran-2-carboxylate]sulfate. Arzneimitlelforschung. 1986;36:671-675.
    • (1986) Arzneimitlelforschung , vol.36 , pp. 671-675
    • Toyo-oka, T.1    Kamishiro, T.2    Gotoh, Y.3    Fumino, H.4    Masaki, T.5    Hosoda, S.6
  • 18
    • 0020509885 scopus 로고
    • Role of cellular proteinases in acute myocardial infarction, II: Influence of in vivo suppression of myocardial proteolysis by antipain, leupeptin and pepstatin on myocardial infarct size in the rat
    • Bolli R, Cannon RO, Speir E, Goldstein RE, Epstein SE. Role of cellular proteinases in acute myocardial infarction, II: influence of in vivo suppression of myocardial proteolysis by antipain, leupeptin and pepstatin on myocardial infarct size in the rat. J Am Coll Cardiol. 1983;2:681-686.
    • (1983) J Am Coll Cardiol , vol.2 , pp. 681-686
    • Bolli, R.1    Cannon, R.O.2    Speir, E.3    Goldstein, R.E.4    Epstein, S.E.5
  • 19
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function and regulation
    • Croall DE, Demartino GN. Calcium-activated neutral protease (calpain) system: structure, function and regulation. Physiol Rev. 1991;71:813-847.
    • (1991) Physiol Rev , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 20
    • 0021683468 scopus 로고
    • Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic substrates
    • Sasaki T, Kikuchi T, Yumoto N, Yoshimura N, Murachi T. Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic substrates. J Biol Chem. 1984;259:12489-12494.
    • (1984) J Biol Chem , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5
  • 21
    • 0018761375 scopus 로고
    • Release of alpha-hydroxybutyrate dehydrogenase from neonatal rat heart cell cultures exposed to anoxia and reoxygenation: Comparison with impairment of structure and function of damaged cardiac cells
    • Van der Laarse A, Hollaar L, Van der Valk EJM. Release of alpha-hydroxybutyrate dehydrogenase from neonatal rat heart cell cultures exposed to anoxia and reoxygenation: comparison with impairment of structure and function of damaged cardiac cells. Cardiovasc Res. 1979;13:345-353.
    • (1979) Cardiovasc Res , vol.13 , pp. 345-353
    • Van Der Laarse, A.1    Hollaar, L.2    Van Der Valk, E.J.M.3
  • 22
    • 0015224609 scopus 로고
    • Heart cells in culture: A simple method for increasing the proportion of myoblasts
    • Blondel B, Royen J, Cheneval JP. Heart cells in culture: a simple method for increasing the proportion of myoblasts. Experimentia. 1971;27:356-358.
    • (1971) Experimentia , vol.27 , pp. 356-358
    • Blondel, B.1    Royen, J.2    Cheneval, J.P.3
  • 25
    • 0025823806 scopus 로고
    • A continuous fluorescent assay for measuring protease activity using natural protein substrate
    • Farmer W, Yuan Z. A continuous fluorescent assay for measuring protease activity using natural protein substrate. Anal Biochem. 1991;197:347-352.
    • (1991) Anal Biochem , vol.197 , pp. 347-352
    • Farmer, W.1    Yuan, Z.2
  • 26
    • 0027182332 scopus 로고
    • The labeling of proteins and LDL with 99m-Tc: A new direct method employing KBH4 and stannous chloride
    • Pauwels EKJ, Welling MM, Feitsma RIJ, Atsma DE, Nieuwenhuizen W. The labeling of proteins and LDL with 99m-Tc: a new direct method employing KBH4 and stannous chloride. Nucl Med Biol. 1993;20:825-833.
    • (1993) Nucl Med Biol , vol.20 , pp. 825-833
    • Pauwels, E.K.J.1    Welling, M.M.2    Feitsma, R.I.J.3    Atsma, D.E.4    Nieuwenhuizen, W.5
  • 27
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J Biol Chem. 1985;260:3440-3450.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 29
    • 0026012279 scopus 로고
    • Application of stereological analysis of cell volume to isolated myocytes in culture with and without adrenergic innervation
    • Atkins DL, Rosenthal JK, Krumm PA, Marvin WJ. Application of stereological analysis of cell volume to isolated myocytes in culture with and without adrenergic innervation. Anal Rec. 1991;231:209-217.
    • (1991) Anal Rec , vol.231 , pp. 209-217
    • Atkins, D.L.1    Rosenthal, J.K.2    Krumm, P.A.3    Marvin, W.J.4
  • 30
    • 85047677306 scopus 로고
    • A method to quantitate cell numbers of muscle cells and non-muscle cells in homogenised heart cell cultures
    • Van der Laarse A, Hollaar L, Van der Valk EJM, Hamers S. A method to quantitate cell numbers of muscle cells and non-muscle cells in homogenised heart cell cultures. Cardiovasc Res. 1989;23: 928-933.
    • (1989) Cardiovasc Res , vol.23 , pp. 928-933
    • Van Der Laarse, A.1    Hollaar, L.2    Van Der Valk, E.J.M.3    Hamers, S.4
  • 33
    • 0024433794 scopus 로고
    • Enzyme release from chick myocytes during hypoxia and reoxygenation: Dependence on pH
    • Bhatti S, Zimmer G, Bereiter HJ. Enzyme release from chick myocytes during hypoxia and reoxygenation: dependence on pH. J Mol Cell Cardiol. 1989;21:995-1008.
    • (1989) J Mol Cell Cardiol , vol.21 , pp. 995-1008
    • Bhatti, S.1    Zimmer, G.2    Bereiter, H.J.3
  • 34
    • 0021270207 scopus 로고
    • Ultrastructure of cultured adult myocardial cells during anoxia and reoxygenation
    • Schwartz P, Piper HM, Spahr R, Spieckermann PG. Ultrastructure of cultured adult myocardial cells during anoxia and reoxygenation. Am J Pathol. 1984;115:349-361.
    • (1984) Am J Pathol , vol.115 , pp. 349-361
    • Schwartz, P.1    Piper, H.M.2    Spahr, R.3    Spieckermann, P.G.4
  • 36
    • 0028210773 scopus 로고
    • Distribution of electrical potential, pH, free Ca(2)+, and volume inside cultured adult rabbit cardiac myocytes during chemical hypoxia: A multiparameter digitized confocal microscopic study
    • Chacon E, Reece JM, Nieminen AL, Zahrebelski G, Herman B, Lemasters JJ. Distribution of electrical potential, pH, free Ca(2)+, and volume inside cultured adult rabbit cardiac myocytes during chemical hypoxia: a multiparameter digitized confocal microscopic study. Biophys J. 1994;66:942-952.
    • (1994) Biophys J , vol.66 , pp. 942-952
    • Chacon, E.1    Reece, J.M.2    Nieminen, A.L.3    Zahrebelski, G.4    Herman, B.5    Lemasters, J.J.6
  • 37
    • 0023686985 scopus 로고
    • Myocyte deenergization and intracellular free calcium dynamics
    • Li Q, Altschuld RA, Stokes BT. Myocyte deenergization and intracellular free calcium dynamics. Am J Physiol. 1988;255:C162-C168.
    • (1988) Am J Physiol , vol.255
    • Li, Q.1    Altschuld, R.A.2    Stokes, B.T.3
  • 38
    • 0025970794 scopus 로고
    • Cell-penetrating inhibitors of calpain
    • Mehdi S. Cell-penetrating inhibitors of calpain. Trends Biochem Sci. 1991;16:150-153.
    • (1991) Trends Biochem Sci , vol.16 , pp. 150-153
    • Mehdi, S.1
  • 39
    • 0020456259 scopus 로고
    • Reduction of experimentally produced acute myocardial infarction by a new synthetic inhibitor, NCO700, against calcium activated neutral protease
    • Toyo-oka T, Kamishiro T, Masaki M, Masaki T. Reduction of experimentally produced acute myocardial infarction by a new synthetic inhibitor, NCO700, against calcium activated neutral protease. Jpn Heart J. 1982;23:829-834.
    • (1982) Jpn Heart J , vol.23 , pp. 829-834
    • Toyo-oka, T.1    Kamishiro, T.2    Masaki, M.3    Masaki, T.4
  • 40
    • 0021997081 scopus 로고
    • Effect of NCO-700, an inhibitor of protease, on myocardial pH decreased by coronary occlusion in dogs
    • Haga N, Ishibashi T, Abiko Y. Effect of NCO-700, an inhibitor of protease, on myocardial pH decreased by coronary occlusion in dogs. Pharmacology. 1985;31:208-217.
    • (1985) Pharmacology , vol.31 , pp. 208-217
    • Haga, N.1    Ishibashi, T.2    Abiko, Y.3


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