Adult rat cardiomyocytes exhibit capacitative calcium entry

Hunton, Dacia L.; Zou, Luyun; Pang, Yi; Marchase, Richard B.

doi:10.1152/ajpheart.00162.2003

Cited by 86 publications

(97 citation statements)

References 39 publications

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“…However, in 2002 this laboratory (38) and Uehara and colleagues (122) demonstrated that Ca 2ϩ store depletion in neonatal and embryonic cardiomyocytes, respectively, resulted in a robust and persistent influx of extracellular Ca 2ϩ that was blocked by SOC inhibitors but not inhibitors of either L-type Ca 2ϩ channels (LTCC) or Na ϩ /Ca 2ϩ exchangers (NCX). We first reported the presence of SOCE in adult cardiomyocytes in 2004 using the combination of thapsigargin and the IP 3 -generating agonist ANG II (39). Using a differential dye-loading protocol to measure both ER/SR and cytosolic Ca 2ϩ levels, we observed a significant increase in cytosolic Ca 2ϩ concomitant with an immediate drop in store Ca 2ϩ levels, consistent with the activation of SOCE (39).…”

Section: Orai1/trpcmentioning

confidence: 65%

STIM1/Orai1-mediated SOCE: current perspectives and potential roles in cardiac function and pathology

Collins

Zhu-Mauldin

Marchase

et al. 2013

American Journal of Physiology-Heart and Circulatory Physiology

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111

102

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Collins HE, Zhu-Mauldin X, Marchase RB, Chatham JC. STIM1/Orai1-mediated SOCE: current perspectives and potential roles in cardiac function and pathology. Am J Physiol Heart Circ Physiol 305: H446 -H458, 2013. First published June 21, 2013 doi:10.1152/ajpheart.00104.2013.-Store-operated Ca 2ϩ entry (SOCE) is critical for Ca 2ϩ signaling in nonexcitable cells; however, its role in the regulation of cardiomyocyte Ca 2ϩ homeostasis has only recently been investigated. The increased understanding of the role of stromal interaction molecule 1 (STIM1) in regulating SOCE combined with recent studies demonstrating the presence of STIM1 in cardiomyocytes provides support that this pathway co-exists in the heart with the more widely recognized Ca 2ϩ handling pathways associated with excitation-contraction coupling. There is now substantial evidence that STIM1-mediated SOCE plays a key role in mediating cardiomyocyte hypertrophy, both in vitro and in vivo, and there is growing support for the contribution of SOCE to Ca 2ϩ overload associated with ischemia/reperfusion injury. Here, we provide an overview of our current understanding of the molecular regulation of SOCE and discuss the evidence supporting the role of STIM1/Orai1-mediated SOCE in regulating cardiomyocyte function.store-operated Ca 2ϩ entry; stromal interaction molecule 1; orai1; cardiomyocytes STORE-OPERATED CA 2ϩ ENTRY (SOCE), also known as capacitative calcium entry (CCE), is the major mechanism of Ca 2ϩ entry in nearly all nonexcitable cells (97, 99). In addition, it is increasingly recognized to co-exist with voltage-gated Ca 2ϩ channels in excitable cells, including neurons, skeletal muscle cells, and cardiomyocytes (1,38,45,83,121). In response to inositol 1,4,5-triphosphate (IP 3 )-(43) or ryanodine receptor (RyR)-mediated (3) Ca 2ϩ release from ER/SR stores, SOCE facilitates the influx of Ca 2ϩ from the extracellular space, resulting in a sustained increase in cytosolic Ca 2ϩ levels. Thus, although one of the roles of SOCE is to rapidly refill the depleted ER/SR stores, the subsequent sustained increase in cytosolic Ca 2ϩ also regulates numerous gene transcription pathways (33,50,151). Indeed, aberrant SOCE has been observed in a growing number of diseases including severe combined immunodeficiency, acute pancreatitis, and Alzheimer's disease (86).The integration of SOCE into well-established models of Ca 2ϩ homeostasis was hampered for many years by the lack of specific molecular mediators; even as recently as 2004 there was considerable controversy as to the specific mechanisms regulating SOCE (90, 113). However, in 2005, stromal interaction molecule 1 (STIM1) was found to localize to the ER/SR membrane and shown to function as a primary mediator of SOCE (54, 102). The putative physiological and pathophysiological roles of SOCE and STIM1 that have been identified to date are summarized in Table 1. A number of studies have recently reported the presence of STIM1 in adult cardiomyocytes (37,59,153), and consistent with earlier evidence supporting a rol...

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Section: Orai1/trpcmentioning

confidence: 65%

STIM1/Orai1-mediated SOCE: current perspectives and potential roles in cardiac function and pathology

Collins

Zhu-Mauldin

Marchase

et al. 2013

American Journal of Physiology-Heart and Circulatory Physiology

Self Cite

111

102

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“…First described in nonexcitable cells, CCE has now been shown to coexist with L-type channels in smooth and skeletal muscle cells (17,35) and in both neonatal and adult cardiomyocytes (12,13,31). The TRPC protein family has been a prime candidate for CCE channel proteins (14) and TRPC1, -3, -4, -5, and -6 have all been identified in rat and mouse hearts (14,28,30).…”

Section: Discussionmentioning

confidence: 99%

“…CCE or store-operated calcium, which was first described in nonexcitable cells (34), refers to the influx of Ca 2ϩ through plasma membrane calcium channels, activated in response to depletion of calcium in the endo/sarcoplasmic reticulum. We have demonstrated that in cardiomyocytes, Ca 2ϩ entry via the CCE-mediated pathway is clearly distinct from both L-type voltage-gated channels and the reverse mode of Na ϩ /Ca 2ϩ exchanger (12,13).…”

mentioning

confidence: 91%

“…Although a number of Ca 2ϩ entry pathways, including the Na ϩ /Ca 2ϩ exchanger and the L-type Ca 2ϩ channel, have been implicated in mediating cardiomyocyte Ca 2ϩ overload (4,6,32), there is little consensus as to which pathways are critical in mediating this process. We have identified a capacitative calcium entry (CCE) or store-operated calcium entry pathway in neonatal and adult rat cardiomyocytes (12,13) that not only influences the response to hypertrophic stimuli but may also play a role in mediating Ca 2ϩ overload in the heart (20). CCE or store-operated calcium, which was first described in nonexcitable cells (34), refers to the influx of Ca 2ϩ through plasma membrane calcium channels, activated in response to depletion of calcium in the endo/sarcoplasmic reticulum.…”

mentioning

confidence: 99%

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Overexpression of TRPC3 increases apoptosis but not necrosis in response to ischemia-reperfusion in adult mouse cardiomyocytes

Shan

Marchase²,

Chatham

2008

American Journal of Physiology-Cell Physiology

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Shan D, Marchase RB, Chatham JC. Overexpression of TRPC3 increases apoptosis but not necrosis in response to ischemia-reperfusion in adult mouse cardiomyocytes. Am J Physiol Cell Physiol 294: C833-C841, 2008. First published January 9, 2008 doi:10.1152/ajpcell.00313.2007.-An increase in cytosolic Ca 2ϩ via a capacitative calcium entry (CCE)-mediated pathway, attributed to members of the transient receptor potential (TRP) superfamily, TRPC1 and TRPC3, has been reported to play an important role in regulating cardiomyocyte hypertrophy. Increased cytosolic Ca 2ϩ also plays a critical role in mediating cell death in response to ischemiareperfusion (I/R). Therefore, we tested the hypothesis that overexpression of TRPC3 in cardiomyocytes will increase sensitivity to I/R injury. Adult cardiomyocytes isolated from wild-type (WT) mice and from mice overexpressing TRPC3 in the heart were subjected to 90 min of ischemia and 3 h of reperfusion. After I/R, viability was 51 Ϯ 1% in WT mice and 42 Ϯ 5% in transgenic mice (P Ͻ 0.05). Apoptosis assessed by annexin V was significantly increased in the TRPC3 group compared with WT (32 Ϯ 1% vs. 21 Ϯ 3%; P Ͻ 0.05); however, there was no significant difference in necrosis between groups. Treatment of TRPC3 cells with the CCE inhibitor SKF-96365 (0.5 M) significantly improved cellular viability (54 Ϯ 4%) and decreased apoptosis (15 Ϯ 4%); in contrast, the L-type Ca 2ϩ channel inhibitor verapamil (10 M) had no effect. Calpain-mediated cleavage of ␣-fodrin was increased approximately threefold in the transgenic group following I/R compared with WT (P Ͻ 0.05); this was significantly attenuated by SKF-96365. The calpain inhibitor PD-150606 (25 M) attenuated the increase in both ␣-fodrin cleavage and apoptosis in the TPRC3 group. Increased TRPC3 expression also increased sensitivity to Ca 2ϩ overload stress, but it did not affect the response to TNF-␣-induced apoptosis. These results suggest that CCE mediated via TRPC may play a role in cardiomyocyte apoptosis following I/R due, at least in part, to increased calpain activation.

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“…Angiotensin II, an IP 3 -generating agonist, is a potent stimulator of cardiomyocyte hypertrophy that can elevate cytoplasmic Ca 2+ during vasoconstriction, increased blood pressure, and hemodynamic stress. A number of studies have demonstrated that angiotensin II treatment leads to an increase in basal Ca 2+ levels in adult and neonatal cardiomyocytes (Kem et al 1991;Shao et al 1998;Hunton et al 2004), with sustained exposure affecting numerous cellular pathways (Meldrum et al 1996;Liu et al 2004b;Zhang et al 2004) and eventually resulting in cell death (Goldenberg et al 2001;Kajstura et al 1997). Elevating UDP-GlcNAc and O-GlcNAc levels through treatment with glucosamine or the O-GlcNAcase inhibitor PUGNAc attenuates angiotensin IIinduced CCE during I/R injury (Nagy et al 2006).…”

Section: Calcium Homeostasismentioning

confidence: 99%

Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

Groves

Lee

Yildirir

et al. 2013

Cell Stress and Chaperones

120

112

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O-linked N-acetyl-β-D-glucosamine (O-GlcNAc) is a ubiquitous and dynamic post-translational modification known to modify over 3,000 nuclear, cytoplasmic, and mitochondrial eukaryotic proteins. Addition of O-GlcNAc to proteins is catalyzed by the O-GlcNAc transferase and is removed by a neutral-N-acetyl-β-glucosaminidase (OGlcNAcase). O-GlcNAc is thought to regulate proteins in a manner analogous to protein phosphorylation, and the cycling of this carbohydrate modification regulates many cellular functions such as the cellular stress response. Diverse forms of cellular stress and tissue injury result in enhanced O-GlcNAc modification, or O-GlcNAcylation, of numerous intracellular proteins. Stress-induced OGlcNAcylation appears to promote cell/tissue survival by regulating a multitude of biological processes including: the phosphoinositide 3-kinase/Akt pathway, heat shock protein expression, calcium homeostasis, levels of reactive oxygen species, ER stress, protein stability, mitochondrial dynamics, and inflammation. Here, we will discuss the regulation of these processes by O-GlcNAc and the impact of such regulation on survival in models of ischemia reperfusion injury and trauma hemorrhage. We will also discuss the misregulation of O-GlcNAc in diseases commonly associated with the stress response, namely Alzheimer's and Parkinson's diseases. Finally, we will highlight recent advancements in the tools and technologies used to study the O-GlcNAc modification.

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Adult rat cardiomyocytes exhibit capacitative calcium entry

Abstract: review. J. Bioenerg. Biomembr. 35:533-575. 15. Freichel, M., et al. 1999. Store-operated cation channels in the heart and cells of the cardiovascu-lar system.

Cited by 86 publications

References 39 publications

STIM1/Orai1-mediated SOCE: current perspectives and potential roles in cardiac function and pathology

STIM1/Orai1-mediated SOCE: current perspectives and potential roles in cardiac function and pathology

Overexpression of TRPC3 increases apoptosis but not necrosis in response to ischemia-reperfusion in adult mouse cardiomyocytes

Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

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