Modification of ischemia-reperfusion-induced changes in cardiac sarcoplasmic reticulum by preconditioning

Osada, Mitsuru; Netticadan, Thomas; Tamura, Kohji; Dhalla, Naranjan S.

doi:10.1152/ajpheart.1998.274.6.h2025

Cited by 76 publications

(80 citation statements)

References 24 publications

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“…The perfusion procedures ( Fig. 1) were similar to those in our previous reports (9,16). The experimental protocol in the present investigation was approved by the Animal Care Committee of the University of Manitoba and conformed with the Canadian Council on Animal Care concerning the "Care and Use of Experimental Animals" (Vol.…”

Section: Methodsmentioning

confidence: 83%

“…The I/Rinduced alterations in cardiac performance, SR function, and mRNA levels for SR genes were also prevented by different treatments such as antioxidants (26) and ␤-adrenergic receptor blockers (25). Likewise, IP has been shown to be an effective intervention for attenuating I/R-induced changes in infarct size, arrhythmias, cardiac performance, and SR function (4,8,9,15,16,19). Furthermore, IP has been documented to reduce the rise in intracellular acidosis as well as intracellular Na ϩ and Ca 2ϩ concentrations due to I/R (21) in addition to inhibiting glycolysis and maintaining glucose oxidation (6).…”

Section: Discussionmentioning

confidence: 99%

“…ischemic preconditioning; ischemia-reperfusion; cardiac mRNA levels; Ca 2ϩ paradoxic heart ISCHEMIC PRECONDITIONING (IP) was first defined by Murry et al (14) as repetitive cycles of brief ischemia and reperfusion that protected the heart against a subsequent period of prolonged ischemic injury. IP has been shown to enhance the recovery of cardiac function (4,16), decrease the incidence of arrhythmias (8,19), and reduce infarct size (8) in hearts subjected to ischemia-reperfusion (I/R) injury. Several endogenous mediators such as adenosine, norepinephrine, protein kinase C, and free radicals have been proposed to mediate the beneficial effects of IP (11).…”

mentioning

confidence: 99%

“…We (25,26) reported that I/R depressed mRNA levels for the SR Ca 2ϩ -cycling proteins such as the ryanodine receptor (RyR) or Ca 2ϩ release channel, Ca 2ϩ pump ATPase [sarco(endo)plasmic Ca 2ϩ -ATPase (SERCA2a)], phospholamban (PLB), and calsequestrin (CQS). In view of the protective effect of IP at the level of SR function in I/R and CP hearts (9,16), this study was designed to examine the effect of IP in preventing changes in SR gene expression due to I/R and CP.…”

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confidence: 99%

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Preconditioning prevents alterations in cardiac SR gene expression due to ischemia-reperfusion

Temsah

Kawabata

Chapman

et al. 2002

American Journal of Physiology-Heart and Circulatory Physiology

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Temsah, Rana M., Kenichi Kawabata, Donald Chapman, and Naranjan S. Dhalla. Preconditioning prevents alterations in cardiac SR gene expression due to ischemiareperfusion. Am J Physiol Heart Circ Physiol 282: H1461-H1466, 2002; 10.1152/ajpheart.00447.2001.-We have previously shown that ischemic preconditioning (IP) improves cardiac performance and sarcoplasmic reticulum (SR) function in hearts subjected to ischemia-reperfusion (I/R). In this study, we examined the effect of IP on I/R-induced changes in gene expression for SR proteins such as the Ca 2ϩ release channel, Ca 2ϩ pump ATPase, phospholamban, and calsequestrin in the isolated rat heart. Normal isolated rat hearts exposed to three brief cycles of IP (5-min ischemia and 5-min reperfusion) exhibited a significant decrease in the transcript levels of SR genes. Nonpreconditioned I/R hearts when subjected to 30-min ischemia and 30-min reperfusion showed a marked decrease in mRNA levels for the SR proteins compared with normal hearts; this decrease was attenuated by preconditioning. Although hearts subjected to Ca 2ϩ paradox (CP) have been shown to exhibit intracellular Ca 2ϩ overload and SR dysfunction like those in I/R hearts, virtually nothing is known regarding the effect of CP on cardiac SR gene expression. Accordingly, CP (5-min Ca 2ϩ -free perfusion and 30-min reperfusion with normal medium) was observed to produce dramatic changes in SR gene expression, and the heart failed to contract; these alterations were attenuated by IP. Our results show that 1) both I/R and CP depress SR gene expression in the normal heart, 2) IP attenuates I/R-and CP-induced depression in cardiac function and SR gene expression, and 3) intracellular Ca 2ϩ overload may play a role in depressing SR gene expression in both I/R and CP hearts. ischemic preconditioning; ischemia-reperfusion; cardiac mRNA levels; Ca 2ϩ paradoxic heart ISCHEMIC PRECONDITIONING (IP) was first defined by Murry et al. (14) as repetitive cycles of brief ischemia and reperfusion that protected the heart against a subsequent period of prolonged ischemic injury. IP has been shown to enhance the recovery of cardiac function (4, 16), decrease the incidence of arrhythmias (8,19), and reduce infarct size (8) in hearts subjected to ischemia-reperfusion (I/R) injury. Several endogenous mediators such as adenosine, norepinephrine, protein kinase C, and free radicals have been proposed to mediate the beneficial effects of IP (11). Earlier, we (9) reported that IP improved cardiac performance not only in hearts exposed to I/R (16) but also in hearts subjected to Ca 2ϩ paradox (CP). CP is known to occur as a consequence of a brief period of Ca 2ϩ depletion followed by Ca 2ϩ repletion (28) and is considered to be an appropriate model for studying the effect of intracellular Ca 2ϩ overload as a contributing factor in the pathogenesis of cardiac dysfunction (1, 2).By virtue of its ability to regulate the intracellular concentration of free Ca 2ϩ , the sarcoplasmic reticulum (SR) plays a central role in the cardiac contracti...

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Section: Methodsmentioning

confidence: 83%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Preconditioning prevents alterations in cardiac SR gene expression due to ischemia-reperfusion

Temsah

Kawabata

Chapman

et al. 2002

American Journal of Physiology-Heart and Circulatory Physiology

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“…These studies employ a variety of approaches (in particular immunoprecipitation and heterologous expression of SERCA mutants) to establish the identity of the phosphoprotein critically (24 -26, 30). In other cases the description of SERCA phosphorylation is made on the basis of coincident migration of SERCA and the phosphoprotein in a one-dimensional SDS-PAGE gel (27)(28)(29). This criterion is not sufficiently critical to enable identification of the phosphoprotein, and does not establish whether SERCA is a phosphoprotein.…”

Section: Discussionmentioning

confidence: 99%

Critical Evaluation of Cardiac Ca2+-ATPase Phosphorylation on Serine 38 Using a Phosphorylation Site-specific Antibody

Rodríguez¹,

Jackson²,

Colyer

2004

Journal of Biological Chemistry

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The phosphorylation of the cardiac muscle isoform of the sarcoplasmic reticulum (SR) Ca 2؉ -ATPase (SERCA2a) on serine 38 has been described as a regulatory event capable of very significant enhancement of enzyme activity (Hawkins, C., Xu, A., and Narayanan, N. (1994) J. Biol. Chem. 269, 31198 -31206). Independent confirmation of these observations has not been forthcoming. This study has utilized a polyclonal antibody specific for the phosphorylated serine 38 epitope on the Ca 2؉ -ATPase to evaluate the phosphorylation of SERCA2a in isolated sarcoplasmic reticulum vesicles and isolated rat ventricular myocytes. A quantitative Western blot approach failed to detect serine 38-phosphorylated Ca 2؉ -ATPase in either kinase-treated sarcoplasmic reticulum vesicles or suitably stimulated cardiac myocytes. Calibration standards confirmed that the detection sensitivity of assays was adequate to detect Ser-38 phosphorylation if it occurred on at least 1% of Ca 2؉ -ATPase molecules in SR vesicle experiments or on at least 0.1% of Ca 2؉ -ATPase molecules in cardiac myocytes. The failure to detect a phosphorylated form of the Ca 2؉ -ATPase in either preparation (isolated myocyte, purified sarcoplasmic reticulum vesicles) suggests that Ser-38 phosphorylation of the Ca 2؉ -ATPase is not a significant regulatory feature of cardiac Ca 2؉ homeostasis.Regulation of Ca 2ϩ sequestration by cardiac sarcoplasmic reticulum has been identified as a key control point in cardiac muscle contraction (1, 2). Stimulation of the rate of Ca 2ϩ uptake occurs during exercise, or following ␤-adrenergic stimulation (3) and is associated with an enhanced force of contraction and an increased rate of relaxation. This accounts for much of the positive inotropic and positive lusitropic effects of these interventions. In contrast, Ca 2ϩ sequestration by cardiac SR 1 is abnormally slow in the muscle of individuals with heart failure (4 -6). In animal studies, normalization of the rate of Ca 2ϩ sequestration has been shown to prevent progression of heart failure (7) and thus the molecular mechanism of control of Ca 2ϩ transport into the sarcoplasmic reticulum has become a focus for research into purposeful therapies to combat human heart failure (7,8).Ca 2ϩ transport into cardiac SR is an enzymatic process performed by the (Ca 2ϩ -Mg 2ϩ )-ATPase (9) (or SERCA2a, Ref. 10), a member of the P-type ATPase family (11). The transport process involves the movement of two Ca 2ϩ from the cytoplasm into the lumen of the SR following the hydrolysis of a single molecule of ATP (12), although significantly lower coupling efficiencies have been measured empirically (13). The reaction cycle is relatively slow and thus a large number of SERCA2 molecules are expressed in cardiac muscle (up to 45% of total SR protein content, 14) to achieve the rates of Ca 2ϩ sequestration required by the kinetics of contraction and relaxation.Regulation of Ca 2ϩ transport into the SR occurs on an acute time scale (seconds to minutes) through the transient modification of the proteins inv...

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Modification of Ischemia‐Reperfusion‐Induced Injury by Cardioprotective Interventions

Zhang¹,

Sallam²,

Xu³

et al. 2003

Myocardial Protection

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Modification of ischemia-reperfusion-induced changes in cardiac sarcoplasmic reticulum by preconditioning

Cited by 76 publications

References 24 publications

Preconditioning prevents alterations in cardiac SR gene expression due to ischemia-reperfusion

Preconditioning prevents alterations in cardiac SR gene expression due to ischemia-reperfusion

Critical Evaluation of Cardiac Ca2+-ATPase Phosphorylation on Serine 38 Using a Phosphorylation Site-specific Antibody

Modification of Ischemia‐Reperfusion‐Induced Injury by Cardioprotective Interventions

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