Ca2 Mobilization in Adult Rat Cardiomyocytes by Angiotensin Type 1 and 2 Receptors

Shao, Qiming; Saward, Laura; Zahradka, Peter; Dhalla, Naranjan S.

doi:10.1016/s0006-2952(97)00653-9

Cited by 24 publications

(18 citation statements)

References 27 publications

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“…The increase in baseline [Ca 2ϩ ] i observed with the addition of ANG II was not observed in the absence of extracellular Ca 2ϩ (data not shown). These effects of ANG II on NRVMs are consistent with the findings of earlier studies in which investigators examined the effect of ANG II on cardiomyocyte function (19,20,43,46).…”

Section: Ang Ii-induced [Ca 2ϩ ] I Elevation In Nrvms Is Inhibited Bysupporting

confidence: 90%

“…The major target of DAG is PKC, whereas IP 3 triggers an increase in cytosolic Ca 2ϩ concentration ([Ca 2ϩ ] i ) through IP 3 receptors located in the sarcoplasmic reticulum (SR). A number of studies have demonstrated that ANG II treatment leads to an increase in basal (i.e., diastolic) [Ca 2ϩ ] i in both adult and neonatal cardiomyocytes (19,43,46). In addition to participating in excitation-contraction coupling (5), changes in [Ca 2ϩ ] i also influence acute inotropic responses (29, 48a) as well as modulate a number of different signaling pathways regulating myocyte hypertrophy and apoptosis (1,3,15,38).…”

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confidence: 99%

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Glucosamine inhibits angiotensin II-induced cytoplasmic Ca²⁺ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine

Nagy

Champattanachai

Marchase

et al. 2006

American Journal of Physiology-Cell Physiology

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We previously reported that glucosamine and hyperglycemia attenuate the response of cardiomyocytes to inositol 1,4,5-trisphosphate-generating agonists such as ANG II. This appears to be related to an increase in flux through the hexosamine biosynthesis pathway (HBP) and decreased Ca2+ entry into the cells; however, a direct link between HBP and intracellular Ca2+ homeostasis has not been established. Therefore, using neonatal rat ventricular myocytes, we investigated the relationship between glucosamine treatment; the concentration of UDP-N-acetylglucosamine (UDP-GlcNAc), an end product of the HBP; and the level of protein O-linked N-acetylglucosamine (O-GlcNAc) on ANG II-mediated changes in intracellular free Ca2+ concentration ([Ca2+]i). We found that glucosamine blocked ANG II-induced [Ca2+]i increase and that this phenomenon was associated with a significant increase in UDP-GlcNAc and O-GlcNAc levels. O-(2-acetamido-2-deoxy-D-glucopyranosylidene)-amino-N-phenylcarbamate, an inhibitor of O-GlcNAcase that increased O-GlcNAc levels without changing UDP-GlcNAc concentrations, mimicked the effect of glucosamine on the ANG II-induced increase in [Ca2+]i. An inhibitor of O-GlcNAc-transferase, alloxan, prevented the glucosamine-induced increase in O-GlcNAc but not the increase in UDP-GlcNAc; however, alloxan abrogated the inhibition of the ANG II-induced increase in [Ca2+]i. These data support the notion that changes in O-GlcNAc levels mediated via increased HBP flux may be involved in the regulation of [Ca2+]i homeostasis in the heart.

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Section: Ang Ii-induced [Ca 2ϩ ] I Elevation In Nrvms Is Inhibited Bysupporting

confidence: 90%

mentioning

confidence: 99%

Glucosamine inhibits angiotensin II-induced cytoplasmic Ca²⁺ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine

Nagy

Champattanachai

Marchase

et al. 2006

American Journal of Physiology-Cell Physiology

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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

117

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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“…[Ca 2+ ] c was determined using the calcium-sensitive fluorescent indicator Fura-2 as reported previously [14] . Neonatal rat cardiomyocytes (5×10 5 cells/mL) cultured for 2-3 h were loaded with 5 µmol/L Fura-2/AM for 30 min in the dark, and the cells were then washed with Hanks' solution three times to remove the extracellular Fura-2/AM.…”

Section: Measurement Of [Ca 2+ ] Cmentioning

confidence: 99%

Glycine inhibits the LPS-induced increase in cytosolic Ca2+ concentration and TNFα production in cardiomyocytes by activating a glycine receptor

Wang

et al. 2009

Acta Pharmacol Sin

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Aim: Previous studies have demonstrated that glycine (GLY) markedly reduces lipopolysaccharide (LPS)-induced myocardial injury. However, the mechanism of this effect is still unclear. The present study investigated the effect of GLY on cytosolic calcium concentration ([Ca 2+ ] c ) and tumor necrosis factor-α (TNFα) production in cardiomyocytes exposed to LPS, as well as whether the glycine-gated chloride channel is involved in this process. Methods: Neonatal rat cardiomyocytes were isolated, and the [Ca 2+ ] c and TNFα levels were determined by using Fura-2 and a Quantikine enzyme-linked immunosorbent assay, respectively. The distribution of the GLY receptor and GLY-induced currents in cardiomyocytes were also investigated using immunocytochemistry and the whole-cell patch-clamp technique, respectively. Results: LPS at concentrations ranging from 10 ng/mL to 100 µg/mL significantly stimulated TNFα production. GLY did not inhibit TNFα production induced by LPS at concentrations below 10 ng/mL but did significantly decrease TNFα release stimulated by 100 µg/mL LPS and prevented an LPS-induced increase in [Ca 2+ ] c , which was reversed by strychnine, a glycine receptor antagonist. GLY did not block the isoproterenol-induced increase in [Ca 2+ ] c , but did prevent the potassium chloride-induced increase in [Ca 2+ ] c in cardiomyocytes. Strychnine reversed the inhibition of the KCl-stimulated elevation in [Ca 2+ ] c by GLY. In chloride-free buffer, GLY had no effect on the dipotassium hydrogen phosphate-induced increase in [Ca 2+ ] c . Furthermore, GLY receptor α 1 and β subunit-immunoreactive spots were observed in cardiomyocytes, and GLY-evoked currents were blocked by strychnine. Conclusion: Cardiomyocytes possess the glycine-gated chloride channel, through which GLY prevents the increase in [Ca 2+ ] c and inhibits the TNFα production induced by LPS at high doses in neonatal rat cardiomyocytes.

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Ca2 Mobilization in Adult Rat Cardiomyocytes by Angiotensin Type 1 and 2 Receptors

Cited by 24 publications

References 27 publications

Glucosamine inhibits angiotensin II-induced cytoplasmic Ca²⁺ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine

Glucosamine inhibits angiotensin II-induced cytoplasmic Ca²⁺ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine

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

Glycine inhibits the LPS-induced increase in cytosolic Ca2+ concentration and TNFα production in cardiomyocytes by activating a glycine receptor

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Ca2 Mobilization in Adult Rat Cardiomyocytes by Angiotensin Type 1 and 2 Receptors

Cited by 24 publications

References 27 publications

Glucosamine inhibits angiotensin II-induced cytoplasmic Ca2+ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine

Glucosamine inhibits angiotensin II-induced cytoplasmic Ca2+ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine

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

Glycine inhibits the LPS-induced increase in cytosolic Ca2+ concentration and TNFα production in cardiomyocytes by activating a glycine receptor

Contact Info

Product

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About

Glucosamine inhibits angiotensin II-induced cytoplasmic Ca²⁺ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine

Glucosamine inhibits angiotensin II-induced cytoplasmic Ca²⁺ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine