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Journal articles on the topic 'H9C2 myoblasts'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Apostolova, Margarita D., Iordanka A. Ivanova, and M. George Cherian. "Signal transduction pathways, and nuclear translocation of zinc and metallothionein during differentiation of myoblasts." Biochemistry and Cell Biology 78, no. 1 (2000): 27–37. http://dx.doi.org/10.1139/o99-070.

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The changes in subcellular localization of metallothionein during differentiation were studied in two myoblast cell lines, L6 and H9C2. Addition of insulin like growth factor-I or lowering foetal bovine serum to 1% can induce differentiation of myoblasts to myotubes. Metallothionein and zinc were localized mainly in the cytoplasm in myoblasts but were translocated into the nucleus of newly formed myotubes during early differentiation. In fully differentiated myotubes, metallothionein content was decreased with a cytoplasmic localization. Addition of an inhibitor of mitogen-activated protein kinase, PD 98059, did not affect differentiation but blocked nuclear translocation of metallothionein. LY 294092, an inhibitor of PI3 kinase, and rapamycin, an inhibitor of p70S6 serine/threonine kinase, abolished insulin-like growth factor-I induced differentiation of myoblasts, retained metallothionein in the cytoplasm, and decreased metallothionein content. These results demonstrate that the cytoplasmic-nuclear translocation of metallothionein occurs during the early stage of differentiation of myoblasts to myotubes and can be blocked by inhibition of certain signal transduction pathways. The transient nuclear localization of metallothionein and zinc may be related to a high requirement for zinc for metabolic activities during the early stage of differentiation.

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2

Khodade, Vinayak S., Sahil C. Aggarwal, Blaze M. Pharoah, Nazareno Paolocci, and John P. Toscano. "Alkylsulfenyl thiocarbonates: precursors to hydropersulfides potently attenuate oxidative stress." Chemical Science 12, no. 23 (2021): 8252–59. http://dx.doi.org/10.1039/d1sc01550h.

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A series of novel alkylsulfenyl thiocarbonates have been developed that efficiently release hydropersulfides (RSSH) over a range of half-lives. RSSH generation by these precursors potently ameliorates oxidative stress in H9c2 cardiac myoblasts.

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3

Kaminska, Iwona, Malgorzata Kotulska, Anna Stecka, et al. "Electroporation-induced changes in normal immature rat myoblasts (H9C2)." General physiology and biophysics 31, no. 01 (2012): 19–25. http://dx.doi.org/10.4149/gpb_2012_003.

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4

Hsu, Ron-Bin, Cheng-Hsin Lin, Wen-Shiann Wu, Wen-Ping Liu, Mao-Tsun Lin, and Ching-Ping Chang. "Attenuating Ischemia-Induced H9c2 Myoblasts Apoptosis by Therapeutic Hypothermia." American Journal of the Medical Sciences 339, no. 3 (2010): 258–65. http://dx.doi.org/10.1097/maj.0b013e3181ce507f.

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5

van der Putten, HH, BJ Joosten, PH Klaren, and ME Everts. "Uptake of tri-iodothyronine and thyroxine in myoblasts and myotubes of the embryonic heart cell line H9c2(2-1)." Journal of Endocrinology 175, no. 3 (2002): 587–96. http://dx.doi.org/10.1677/joe.0.1750587.

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Uptake of tri-iodothyronine (T(3)) was compared with that of thyroxine (T(4)) in the embryonic heart cell line H9c2 (2-1). These cells propagate as myoblasts and form differentiated myotubes upon reduction of the serum concentration, as indicated by a 31-fold increase in creatine kinase activity. Protein and DNA content per well were around 2-fold higher in myotubes than in myoblasts. When expressed per well, T(3) and T(4) uptake were, compared with myoblasts, 1.9- to 2-fold and 3.1- to 4-fold higher in myotubes respectively. On the other hand, the characteristics of T(3) and T(4) uptake were similar in myoblasts and myotubes. At any time-point, T(4) uptake was 2-fold higher than that of T(3), and both uptakes were energy but not Na(+) dependent. T(3) and T(4) uptake exhibited mutual inhibition in myoblasts and myotubes: 10 microM unlabeled T(3) reduced T(4) uptake by 51-60% (P<0.001), while 10 microM T(4) inhibited T(3) uptake by 48-51% (P<0.001). Furthermore, T(3) and T(4) uptake in myoblasts was dose-dependently inhibited by tryptophan (maximum inhibition around 70%; P<0.001). Exposure of the cells to T(3) or T(4) during differentiation significantly increased the fusion index (35 and 40%; P < 0.01). Finally, both myoblasts and myotubes showed a small deiodinase type I activity, while deiodinase type II activity was undetectable. In conclusion, T(3) and T(4) share a common energy-dependent transport system in H9c2(2-1) cells, that may be important for the availability of thyroid hormone during differentiation.

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6

Kulbacka, Julita, Julita Bar, Agnieszka Chwilkowska, et al. "Oxidative modulation of marcaine and lekoptin in H9C2 rat myoblasts." Acta Pharmacologica Sinica 30, no. 2 (2009): 184–92. http://dx.doi.org/10.1038/aps.2008.27.

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7

Loiselle, Julie J., Sarah J. Tessier, and Leslie C. Sutherland. "Post-transcriptional regulation of Rbm5 expression in undifferentiated H9c2 myoblasts." In Vitro Cellular & Developmental Biology - Animal 52, no. 3 (2015): 327–36. http://dx.doi.org/10.1007/s11626-015-9976-x.

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8

Govoni, Marco, Francesca Bonavita, Lisa M. Shantz, Carlo Guarnieri, and Emanuele Giordano. "Overexpression of ornithine decarboxylase increases myogenic potential of H9c2 rat myoblasts." Amino Acids 38, no. 2 (2009): 541–47. http://dx.doi.org/10.1007/s00726-009-0415-8.

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9

Adams, J. C., and J. Lawler. "Cell-type specific adhesive interactions of skeletal myoblasts with thrombospondin-1." Molecular Biology of the Cell 5, no. 4 (1994): 423–37. http://dx.doi.org/10.1091/mbc.5.4.423.

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Thrombospondin-1 (TSP-1) is an extracellular matrix glycoprotein that may play important roles in the morphogenesis and repair of skeletal muscle. To begin to explore the role of thrombospondin-1 in this tissue, we have examined the interactions of three rodent skeletal muscle cell lines, C2C12, G8, and H9c2, with platelet TSP-1. The cells secrete thrombospondin and incorporate it into the cell layer in a distribution distinct from that of fibronectin. Myoblasts attach and spread on fibronectin- or thrombospondin-coated substrates with similar time and concentration dependencies. Whereas cells adherent on fibronectin organize actin stress fibers, cells adherent on TSP-1 display prominent membrane ruffles and lamellae that contain radial actin microspikes. Attachment to thrombospondin-1 or the 140-kDa tryptic fragment is mediated by interactions with the type 1 repeats and the carboxy-terminal globular domain. Attachment is not inhibited by heparin, GRGDSP peptide, or VTCG peptide but is inhibited by chondroitin sulphate A. Integrins of the beta 1 or alpha V subgroups do not appear to be involved in myoblast attachment to TSP-1; instead, this process depends in part on cell surface chondroitin sulphate proteoglycans. Whereas the central 70-kDa chymotryptic fragment of TSP-1 does not support myoblast attachment, the carboxy-terminal domain of TSP-1 expressed as a fusion protein in the bacterial expression vector, pGEX, supported myoblast attachment to 30% the level of intact TSP-1. Thrombospondin-4 (TSP-4) is also present in skeletal muscle and a fusion protein containing the carboxy-terminal domain of TSP-4 also supported myoblast adhesion, although this protein was less active on a molar basis than the TSP-1 fusion protein. Thus, the carboxyterminal domain of TSP-1 appears to contain a primary attachment site for myoblasts, and this activity is present in a second member of the thrombospondin family.

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10

Wang, Wei, Makino Watanabe, Takeshi Nakamura, Yoshihisa Kudo, and Rikuo Ochi. "Properties and expression of Ca2+-activated K+ channels in H9c2 cells derived from rat ventricle." American Journal of Physiology-Heart and Circulatory Physiology 276, no. 5 (1999): H1559—H1566. http://dx.doi.org/10.1152/ajpheart.1999.276.5.h1559.

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H9c2 is a clonal myogenic cell line derived from embryonic rat ventricle that can serve as a surrogate for cardiac or skeletal muscle in vitro. Using whole cell clamp with H9c2 myotubes, we observed that depolarizing pulses activated slow outward K+ currents and then slow tail currents. The K+ currents were abolished in a Ca2+-free external solution, indicating that they were Ca2+-activated K+ currents. They were blocked by apamin, a small-conductance Ca2+-activated K+ (SK) channel antagonist (IC50 = 6.2 nM), and by d-tubocurarine (IC50 = 49.4 μM). Activation of SK channels exhibited a bell-shaped voltage dependence that paralleled the current-voltage relation for L-type Ca2+ currents ( I Ca,L). I Ca,L exhibited a slow time course similar to skeletal I Ca,L, were unaffected by apamin, and were only slightly depressed by d-tubocurarine. RT-PCR analysis of the mRNAs revealed that rSK3, but not rSK1 or rSK2, was expressed in H9c2 myotubes but not in myoblasts. These results suggest that rSK3 channels are expressed in H9c2 myotubes and are primarily activated by I Ca,L directly or indirectly via Ca2+-induced Ca2+ release from sarcoplasmic reticulum.

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11

van den Eijnde, Stefan M., Maurice J. B. van den Hoff, Chris P. M. Reutelingsperger, et al. "Transient expression of phosphatidylserine at cell-cell contact areas is required for myotube formation." Journal of Cell Science 114, no. 20 (2001): 3631–42. http://dx.doi.org/10.1242/jcs.114.20.3631.

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Cell surface exposure of phosphatidylserine (PS) is shown to be part of normal physiology of skeletal muscle development and to mediate myotube formation. A transient exposure of PS was observed on mouse embryonic myotubes at E13, at a stage of development when primary myotubes are formed. The study of this process in cell cultures of differentiating C2C12 and H9C2 myoblasts also reveals a transient expression of PS at the cell surface. This exposure of PS locates mainly at cell-cell contact areas and takes place at a stage when the structural organization of the sarcomeric protein titin is initiated, prior to actual fusion of individual myoblast into multinucleated myotubes. Myotube formation in vitro can be inhibited by the PS binding protein annexin V, in contrast to its mutant M1234, which lacks the ability to bind to PS. Although apoptotic myoblasts also expose PS, differentiating muscle cells show neither loss of mitochondrial membrane potential nor detectable levels of active caspase-3 protein. Moreover, myotube formation and exposure of PS cannot be blocked by the caspase inhibitor zVAD(OMe)-fmk. Our findings indicate that different mechanisms regulate PS exposure during apoptosis and muscle cell differentiation, and that surface exposed PS plays a crucial role in the process of myotube formation.

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12

Hatch, Grant M., and Grant McClarty. "Regulation of Cardiolipin Biosynthesis in H9c2 Cardiac Myoblasts by Cytidine 5′-Triphosphate." Journal of Biological Chemistry 271, no. 42 (1996): 25810–16. http://dx.doi.org/10.1074/jbc.271.42.25810.

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13

Pollard, Celina, Victoria Desimine, Shelby Wertz та ін. "Deletion of Osteopontin Enhances β2-Adrenergic Receptor-Dependent Anti-Fibrotic Signaling in Cardiomyocytes". International Journal of Molecular Sciences 20, № 6 (2019): 1396. http://dx.doi.org/10.3390/ijms20061396.

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Cardiac β2-adrenergic receptors (ARs) are known to inhibit collagen production and fibrosis in cardiac fibroblasts and myocytes. The β2AR is a Gs protein-coupled receptor (GPCR) and, upon its activation, stimulates the generation of cyclic 3′,5′-adenosine monophosphate (cAMP). cAMP has two effectors: protein kinase A (PKA) and the exchange protein directly activated by cAMP (Epac). Epac1 has been shown to inhibit cardiac fibroblast activation and fibrosis. Osteopontin (OPN) is a ubiquitous pro-inflammatory cytokine, which also mediates fibrosis in several tissues, including the heart. OPN underlies several cardiovascular pathologies, including atherosclerosis and cardiac adverse remodeling. We found that the cardiotoxic hormone aldosterone transcriptionally upregulates OPN in H9c2 rat cardiac myoblasts—an effect prevented by endogenous β2AR activation. Additionally, CRISPR-mediated OPN deletion enhanced cAMP generation in response to both β1AR and β2AR activation in H9c2 cardiomyocytes, leading to the upregulation of Epac1 protein levels. These effects rendered β2AR stimulation capable of completely abrogating transforming growth factor (TGF)-β-dependent fibrosis in OPN-lacking H9c2 cardiomyocytes. Finally, OPN interacted constitutively with Gαs subunits in H9c2 cardiac cells. Thus, we uncovered a direct inhibitory role of OPN in cardiac β2AR anti-fibrotic signaling via cAMP/Epac1. OPN blockade could be of value in the treatment and/or prevention of cardiac fibrosis.

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14

Anju, Vijayalekshmi, Sulochana Priya, Sabulal Baby, and Koranappallil Bahuleyan Rameshkumar. "Chemical Constituents and Cytotoxicity of Euphorbia vajravelui." Letters in Organic Chemistry 16, no. 8 (2019): 643–46. http://dx.doi.org/10.2174/1570178616666181129130127.

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Euphorbia species are important in traditional medicines as well as in horticulture. Though 82 Euphorbia species are reported from India, most of the species are yet to be explored for the phytochemicals or bioactivities. The present study reports the phytochemical and cytotoxicity studies of the Western Ghats endemic plant Euphorbia vajravelui. Compounds were isolated from the extracts of E. vajravelui using column chromatography and were characterized through various spectroscopic techniques. The structures were further confirmed through single crystal XRD. The major pentacyclic triterpene 3β-friedelinol was estimated using a validated HPTLC method. Cytotoxicity of the extracts was tested against human cervical cancer cell line HeLa and normal cardiac myoblasts cell line H9C2 using MTT assay. The pentacyclic triterpenoids taraxeryl acetate, epi-friedelinyl acetate, 3β-friedelinol, taraxerol, 3α-friedelinol and friedelane-2β,3α-diyl diacetate and the phenolic compound 3,4,3'-tri-Omethyl ellagic acid 4'-rutinoside were isolated and characterized from E. vajravelui. Single crystal XRD data of epi-friedelinyl acetate, taraxerol and 3α-friedelinol were also reported. The major compound 3β-friedelinol was found to contain 0.33 ± 0.03%, estimated through a validated HPTLC method. The extracts were non-toxic towards normal cell line H9C2 (cardiac myoblasts) and showed negligible cytotoxic effects towards cervical cancer cell line HeLa upto100 µg/mL concentration. The major compounds isolated from E. vajravelui were triterpenoids and single crystal XRD data unambiguously confirmed the structures. The latex extract was non toxic towards normal cell line H9C2 and cancer cell line HeLa and the result was relevant especially in the context of the eco-toxicological concerns around Euphorbia species. This is the first report of the phytochemical and cytotoxicity studies of the Western Ghats endemic species E. vajravelui.

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15

Wang, Wei, Naoki Hino, Hiroshi Yamasaki, Takashi Aoki, and Rikuo Ochi. "KV2.1 K+ Channels Underlie Major Voltage-Gated K+ Outward Current in H9c2 Myoblasts." Japanese Journal of Physiology 52, no. 6 (2002): 507–14. http://dx.doi.org/10.2170/jjphysiol.52.507.

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16

Son, Euncheol, Dongju Lee, Chul-Woong Woo, and Young-Hoon Kim. "The optimal model of reperfusion injury in vitro using H9c2 transformed cardiac myoblasts." Korean Journal of Physiology & Pharmacology 24, no. 2 (2020): 173. http://dx.doi.org/10.4196/kjpp.2020.24.2.173.

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17

Reyes, Leila, Clare L. Hawkins, and Benjamin S. Rayner. "Characterization of the cellular effects of myeloperoxidase-derived oxidants on H9c2 cardiac myoblasts." Archives of Biochemistry and Biophysics 665 (April 2019): 132–42. http://dx.doi.org/10.1016/j.abb.2019.03.004.

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18

Sardão, Vilma A., Paulo J. Oliveira, Jon Holy, Catarina R. Oliveira, and Kendall B. Wallace. "Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets." Cell Biology and Toxicology 25, no. 3 (2008): 227–43. http://dx.doi.org/10.1007/s10565-008-9070-1.

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19

Stathopoulou, Konstantina, Isidoros Beis, and Catherine Gaitanaki. "MAPK signaling pathways are needed for survival of H9c2 cardiac myoblasts under extracellular alkalosis." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 3 (2008): H1319—H1329. http://dx.doi.org/10.1152/ajpheart.01362.2007.

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pH is one of the most important physiological parameters, with its changes affecting the function of vital organs like the heart. However, the effects of alkalosis on the regulation of cardiac myocyte function have not been extensively investigated. Therefore, we decided to study whether the mitogen-activated protein kinase (MAPK) signaling pathways [c-Jun NH2-terminal kinases (JNKs), extracellular signal-regulated kinases (ERKs), and p38 MAPK] are activated by alkalosis induced with Tris-Tyrode buffer at two pH values, 8.5 and 9.5, in H9c2 rat cardiac myoblasts. These buffers also induced intracellular alkalinization comparable to that induced by 1 mM NH4Cl. The three MAPKs examined presented differential phosphorylation patterns that depended on the severity and the duration of the stimulus. Inhibition of Na+/H+ exchanger (NHE)1 by its inhibitor HOE-642 prevented alkalinization and partially attenuated the alkalosis (pH 8.5)-induced activation of these kinases. The same stimulus also promoted c-Jun phosphorylation and enhanced the binding at oligonucleotides bearing the activator protein-1 (AP-1) consensus sequence, all in a JNK-dependent manner. Additionally, mitogen- and stress-activated kinase 1 (MSK1) was transiently phosphorylated by alkalosis (pH 8.5), and this was abolished by the selective inhibitors of either p38 MAPK or ERK pathways. JNKs also mediated Bcl-2 phosphorylation in response to incubation with the alkaline medium (pH 8.5), while selective inhibitors of the three MAPKs diminished cell viability under these conditions. All these data suggest that alkalosis activates MAPKs in H9c2 cells and these kinases, in turn, modify proteins that regulate gene transcription and cell survival.

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20

Choi, Hyun Ju, Mi Ra Seon, Soon Sung Lim, Jong-Sang Kim, Hyang Sook Chun, and Jung Han Yoon Park. "Hexane/Ethanol Extract ofGlycyrrhiza uralensisLicorice Suppresses Doxorubicin-Induced Apoptosis in H9c2 Rat Cardiac Myoblasts." Experimental Biology and Medicine 233, no. 12 (2008): 1554–60. http://dx.doi.org/10.3181/0807-rm-221.

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21

Mei, Chieh, Chih‐Wei Chao, Che‐Wei Lin, et al. "Three‐dimensional spherical gelatin bubble‐based scaffold improves the myotube formation of H9c2 myoblasts." Biotechnology and Bioengineering 116, no. 5 (2019): 1190–200. http://dx.doi.org/10.1002/bit.26917.

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22

Girard, Béatrice, L'Houcine Ouafik та Françoise Boudouresque. "Characterization and regulation of peptidylglycine α-amidating monooxygenase (PAM) expression in H9c2 cardiac myoblasts". Cell and Tissue Research 298, № 3 (1999): 489–97. http://dx.doi.org/10.1007/s004410050071.

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23

Girard, Béatrice, L'Houcine Ouafik та Françoise Boudouresque. "Characterization and regulation of peptidylglycine α-amidating monooxygenase (PAM) expression in H9c2 cardiac myoblasts". Cell and Tissue Research 298, № 3 (1999): 489–97. http://dx.doi.org/10.1007/s004419900111.

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24

O-Uchi, Jin, Bong Sook Jhun, Stephen Hurst, et al. "Overexpression of ryanodine receptor type 1 enhances mitochondrial fragmentation and Ca2+-induced ATP production in cardiac H9c2 myoblasts." American Journal of Physiology-Heart and Circulatory Physiology 305, no. 12 (2013): H1736—H1751. http://dx.doi.org/10.1152/ajpheart.00094.2013.

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Ca+ influx to mitochondria is an important trigger for both mitochondrial dynamics and ATP generation in various cell types, including cardiac cells. Mitochondrial Ca2+ influx is mainly mediated by the mitochondrial Ca2+ uniporter (MCU). Growing evidence also indicates that mitochondrial Ca2+ influx mechanisms are regulated not solely by MCU but also by multiple channels/transporters. We have previously reported that skeletal muscle-type ryanodine receptor (RyR) type 1 (RyR1), which expressed at the mitochondrial inner membrane, serves as an additional Ca2+ uptake pathway in cardiomyocytes. However, it is still unclear which mitochondrial Ca2+ influx mechanism is the dominant regulator of mitochondrial morphology/dynamics and energetics in cardiomyocytes. To investigate the role of mitochondrial RyR1 in the regulation of mitochondrial morphology/function in cardiac cells, RyR1 was transiently or stably overexpressed in cardiac H9c2 myoblasts. We found that overexpressed RyR1 was partially localized in mitochondria as observed using both immunoblots of mitochondrial fractionation and confocal microscopy, whereas RyR2, the main RyR isoform in the cardiac sarcoplasmic reticulum, did not show any expression at mitochondria. Interestingly, overexpression of RyR1 but not MCU or RyR2 resulted in mitochondrial fragmentation. These fragmented mitochondria showed bigger and sustained mitochondrial Ca2+ transients compared with basal tubular mitochondria. In addition, RyR1-overexpressing cells had a higher mitochondrial ATP concentration under basal conditions and showed more ATP production in response to cytosolic Ca2+ elevation compared with nontransfected cells as observed by a matrix-targeted ATP biosensor. These results indicate that RyR1 possesses a mitochondrial targeting/retention signal and modulates mitochondrial morphology and Ca2+-induced ATP production in cardiac H9c2 myoblasts.

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Chua, Chu Chang, Xuwan Liu, Jinping Gao, Ronald C. Hamdy та Balvin H. L. Chua. "Multiple actions of pifithrin-α on doxorubicin-induced apoptosis in rat myoblastic H9c2 cells". American Journal of Physiology-Heart and Circulatory Physiology 290, № 6 (2006): H2606—H2613. http://dx.doi.org/10.1152/ajpheart.01138.2005.

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Doxorubicin (Dox) is a chemotherapeutic agent that causes significant cardiotoxicity. We showed previously that Dox activates p53 and induces apoptosis in mouse hearts. This study was designed to elucidate the molecular events that lead to p53 stabilization, to examine the pathways involved in Dox-induced apoptosis, and to evaluate the effectiveness of pifithrin-α (PFT-α), a p53 inhibitor, in blocking apoptosis of rat H9c2 myoblasts. H9c2 cells that were exposed to 5 μM Dox had elevated levels of p53 and phosphorylated p53 at Ser15. Dox also triggered a transient activation of p38, p42/p44ERK, and p46/p54JNK MAP kinases. Caspase activity assays and Western blot analysis showed that H9c2 cells treated with Dox for 16 h had marked increase in the levels of caspases-2, -3, -8, -9, -12, Fas, and cleaved poly(ADP ribose) polymerase (PARP). There was a concomitant increase in p53 binding activity, cytochrome c release, and apoptosis. These results suggest that Dox can trigger intrinsic, extrinsic, and endoplasmic reticulum-associated apoptotic pathways. Pretreatment of cells with PFT-α followed by Dox administration attenuated Dox-induced increases in p53 levels and p53 binding activity and partially blocked the activation of p46/p54JNK and p42/p44ERK. PFT-α also led to decreased levels of caspases-2, -3, -8, -9, -12, Fas, PARP, cytochrome c release, and apoptosis. Our results suggest that p53 stabilization is a focal point of Dox-induced apoptosis and that PFT-α interferes with multiple steps of Dox-induced apoptosis.

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Liu, Ling, Ping Wang, Xinwei Liu, Dongwei He, Canxin Liang, and Ying Yu. "Exogenous NAD+supplementation protects H9c2 cardiac myoblasts against hypoxia/reoxygenation injury via Sirt1-p53 pathway." Fundamental & Clinical Pharmacology 28, no. 2 (2013): 180–89. http://dx.doi.org/10.1111/fcp.12016.

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27

Soler, Fernando, Antonio Lax, M. Carmen Asensio, Domingo Pascual-Figal, and Francisco Fernández-Belda. "Passive Ca2+ overload in H9c2 cardiac myoblasts: Assessment of cellular damage and cytosolic Ca2+ transients." Archives of Biochemistry and Biophysics 512, no. 2 (2011): 175–82. http://dx.doi.org/10.1016/j.abb.2011.05.019.

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28

Huo, Shengqi, Wei Shi, Haiyan Ma, et al. "Alleviation of Inflammation and Oxidative Stress in Pressure Overload-Induced Cardiac Remodeling and Heart Failure via IL-6/STAT3 Inhibition by Raloxifene." Oxidative Medicine and Cellular Longevity 2021 (March 20, 2021): 1–15. http://dx.doi.org/10.1155/2021/6699054.

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Background. Inflammation and oxidative stress are involved in the initiation and progress of heart failure (HF). However, the role of the IL6/STAT3 pathway in the pressure overload-induced HF remains controversial. Methods and Results. Transverse aortic constriction (TAC) was used to induce pressure overload-HF in C57BL/6J mice. 18 mice were randomized into three groups (Sham, TAC, and TAC+raloxifene, n = 6 , respectively). Echocardiographic and histological results showed that cardiac hypertrophy, fibrosis, and left ventricular dysfunction were manifested in mice after TAC treatment of eight weeks, with aggravation of macrophage infiltration and interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-α) expression in the myocardium. TAC (four and eight weeks) elevated the phosphorylation of signal transducer and activator of transcription 3 (p-STAT3) and prohibitin2 (PHB2) protein expression. Importantly, IL-6/gp130/STAT3 inhibition by raloxifene alleviated TAC-induced myocardial inflammation, cardiac remodeling, and dysfunction. In vitro, we demonstrated cellular hypertrophy with STAT3 activation and oxidative stress exacerbation could be elicited by IL-6 (25 ng/mL, 48 h) in H9c2 myoblasts. Sustained IL-6 stimulation increased intracellular reactive oxygen species, repressed mitochondrial membrane potential (MMP), decreased intracellular content of ATP, and led to decreased SOD activity, an increase in iNOS protein expression, and increased protein expression of Pink1, Parkin, and Bnip3 involving in mitophagy, all of which were reversed by raloxifene. Conclusion. Inflammation and IL-6/STAT3 signaling were activated in TAC-induced HF in mice, while sustained IL-6 incubation elicited oxidative stress and mitophagy-related protein increase in H9c2 myoblasts, all of which were inhibited by raloxifene. These indicated IL-6/STAT3 signaling might be involved in the pathogenesis of myocardial hypertrophy and HF.

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29

Fong, Chi Chun, Fan Wei, Yao Chen, et al. "Danshen–Gegen decoction exerts proliferative effect on rat cardiac myoblasts H9c2 via MAPK and insulin pathways." Journal of Ethnopharmacology 138, no. 1 (2011): 60–66. http://dx.doi.org/10.1016/j.jep.2011.08.027.

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30

Vineetha, V. P., A. Prathapan, R. S. Soumya, and K. G. Raghu. "Arsenic Trioxide Toxicity in H9c2 Myoblasts—Damage to Cell Organelles and Possible Amelioration with Boerhavia diffusa." Cardiovascular Toxicology 13, no. 2 (2012): 123–37. http://dx.doi.org/10.1007/s12012-012-9191-x.

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31

Bryantsev, Anton L., Svetlana A. Loktionova, Olga P. Ilyinskaya, Eduard M. Tararak, Harm H. Kampinga, and Alexander E. Kabakov. "Distribution, phosphorylation, and activities of Hsp25 in heat-stressed H9c2 myoblasts: a functional link to cytoprotection." Cell Stress & Chaperones 7, no. 2 (2002): 146. http://dx.doi.org/10.1379/1466-1268(2002)007<0146:dpaaoh>2.0.co;2.

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32

Kim, S. S., J. Kim, S. Kwon, et al. "PI3-kinase activates p38 MAPK independently of PKB/Akt during myogenic differentiation of H9c2 cardiac myoblasts." Biochemical Society Transactions 28, no. 5 (2000): A292. http://dx.doi.org/10.1042/bst028a292b.

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Su, Ching-Yuan, Kowit-Yu Chong, JianXiong Chen, Stefan Ryter, Romesh Khardori, and Chen-Ching Lai. "A Physiologically Relevant Hyperthermia Selectively Activates Constitutive hsp70 in H9c2 Cardiac Myoblasts and Confers Oxidative Protection." Journal of Molecular and Cellular Cardiology 31, no. 4 (1999): 845–55. http://dx.doi.org/10.1006/jmcc.1998.0923.

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Hu, Yue-huai, Jie Liu, Jing Lu, et al. "sFRP1 protects H9c2 cardiac myoblasts from doxorubicin-induced apoptosis by inhibiting the Wnt/PCP-JNK pathway." Acta Pharmacologica Sinica 41, no. 9 (2020): 1150–57. http://dx.doi.org/10.1038/s41401-020-0364-z.

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Alam, Md Jahangir, Richa Gupta, Nitish R. Mahapatra, and Shyamal K. Goswami. "Catestatin reverses the hypertrophic effects of norepinephrine in H9c2 cardiac myoblasts by modulating the adrenergic signaling." Molecular and Cellular Biochemistry 464, no. 1-2 (2019): 205–19. http://dx.doi.org/10.1007/s11010-019-03661-1.

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Botha, Christo J., Y. Zethu Mathe, Gezina C. H. Ferreira, and E. Annette Venter. "Cytotoxicity of the Sesquiterpene Lactones, Ivalin and Parthenolide in Murine Muscle Cell Lines and Their Effect on Desmin, a Cytoskeletal Intermediate Filament." Toxins 12, no. 7 (2020): 459. http://dx.doi.org/10.3390/toxins12070459.

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Vermeersiekte or “vomiting disease” is an economically important disease of ruminants following ingestion of Geigeria (G.) species in South Africa. Sheep are more susceptible, and poisoning is characterized by stiffness, regurgitation, bloat, paresis, and paralysis. Various sesquiterpene lactones have been implicated as the cause of poisoning. The in vitro cytotoxicity of two sesquiterpene lactones, namely, ivalin (purified from Geigeria aspera) and parthenolide (a commercially available sesquiterpene lactone), were compared using mouse skeletal myoblast (C2C12) and rat embryonic cardiac myocyte (H9c2) cell lines, representing the oesophageal, skeletal and cardiac muscles, which are affected in sheep. For 24, 48, and 72 h, both cell lines were exposed. A colorimetric viability assay, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT), was used to assess cytotoxicity. A concentration-dependent cytotoxic response was observed in both cell lines, however, the C2C12 cells were more sensitive, with the half-maximal effective concentrations (EC50s) ranging between 2.7 and 3.3 µM. In addition, the effect that ivalin and parthenolide has on desmin, an important cytoskeletal intermediate filament in myocytes, was evaluated using the C2C12 myoblasts. Disorganization and aggregation of desmin were caused by both sesquiterpene lactones, which could clarify some of the ultrastructural lesions described in vermeersiekte.

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Lee, Insu, Jin Woo, Min Lee, Tae-Joon Jeon, and Sun Kim. "Hypoxic Physiological Environments in a Gas-Regulated Microfluidic Device." Micromachines 10, no. 1 (2018): 16. http://dx.doi.org/10.3390/mi10010016.

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Hypoxic environment is known as one of the critical factors in various physiological/pathological processes. It is imperative to recapitulate oxygen level in microscale for human physiology/pathology induced by hypoxia. Herein, we propose an oxygen-regulating system that can be applied to in vitro tissue models. We fabricated a microdevice with a gas-permeable membrane, allowing oxygen diffusion without direct contact to cells. We verified the formation of oxygen level less than 2% O2 concentration inside the device through computational simulation and experiments. H9c2 heart myoblasts were exposed to hypoxic condition in the device, and their cell viability were investigated. We anticipate that our system will be integrated with a platform to study hypoxia-induced human physiology and pathology as an efficient oxygen-regulating system.

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Sugarman, Eliot, Ada Koo, Eigo Suyama, et al. "Identification of Inhibitors of Triacylglyceride Accumulation in Muscle Cells." Journal of Biomolecular Screening 19, no. 1 (2013): 77–87. http://dx.doi.org/10.1177/1087057113501198.

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Excess caloric consumption leads to triacylglyceride (TAG) accumulation in tissues that do not typically store fat, such as skeletal muscle. This ectopic accumulation alters cells, contributing to the pathogenesis of metabolic syndrome, a major health problem worldwide. We developed a 1536-well assay to measure intracellular TAG accumulation in differentiating H9c2 myoblasts. For this assay, cells were incubated with oleic acid to stimulate TAG accumulation prior to adding compounds. We used Nile red as a fluorescent dye to quantify TAG content with a microplate reader. The cell nuclei were counterstained with DAPI nuclear stain to assess cell count and filter cytotoxic compounds. In parallel, we developed an image-based assay in H9c2 cells to measure lipid accumulation levels via high-content analysis, exploiting the dual-emission spectra characteristic of Nile red staining of neutral and phospholipids. Using both approaches, we successfully screened ~227,000 compounds from the National Institutes of Health library. The screening data from the plate reader and IC50 values correlated with that from the Opera QEHS cell imager. The 1536-well plate reader assay is a powerful high-throughout screening platform to identify potent inhibitors of TAG accumulation to better understand the molecular pathways involved in lipid metabolism that lead to lipotoxicity.

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Lee, Christopher T., John R. Ussher, Askar Mohammad, Anna Lam, and Gary D. Lopaschuk. "5′-AMP-activated protein kinase increases glucose uptake independent of GLUT4 translocation in cardiac myocytes." Canadian Journal of Physiology and Pharmacology 92, no. 4 (2014): 307–14. http://dx.doi.org/10.1139/cjpp-2013-0107.

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Glucose uptake and glycolysis are increased in the heart during ischemia, and this metabolic alteration constitutes an important contributing factor towards ischemic injury. Therefore, it is important to understand glucose uptake regulation in the ischemic heart. There are primarily 2 glucose transporters controlling glucose uptake into cardiac myocytes: GLUT1 and GLUT4. In the non-ischemic heart, insulin stimulates GLUT4 translocation to the sarcolemmal membrane, while both GLUT1 and GLUT4 translocation can occur following AMPK stimulation. Using a newly developed technique involving [3H]2-deoxyglucose, we measured glucose uptake in H9c2 ventricular myoblasts, and demonstrated that while insulin has no detectable effect on glucose uptake, phenformin-induced AMPK activation increases glucose uptake 2.5-fold. Furthermore, insulin treatment produced no discernible effect on either Akt serine 473 phosphorylation or AMPKα threonine 172 phosphorylation, while treatment with phenformin results in an increase in AMPKα threonine 172 phosphorylation, and a decrease in Akt serine 473 phosphorylation. Visualization of a dsRed-GLUT4 fusion construct in H9c2 cells by laser confocal microscopy showed that unlike insulin, AMPK activation did not redistribute GLUT4 to the sarcolemmal membrane, suggesting that AMPK may regulate glucose uptake via another glucose transporter. These studies suggest that AMPK is a major regulator of glucose uptake in cardiac myocytes.

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Gopal, Keshav, Bruno Saleme, Rami Al Batran, et al. "FoxO1 regulates myocardial glucose oxidation rates via transcriptional control of pyruvate dehydrogenase kinase 4 expression." American Journal of Physiology-Heart and Circulatory Physiology 313, no. 3 (2017): H479—H490. http://dx.doi.org/10.1152/ajpheart.00191.2017.

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Pyruvate dehydrogenase (PDH) is the rate-limiting enzyme for glucose oxidation and a critical regulator of metabolic flexibility during the fasting to feeding transition. PDH is regulated via both PDH kinases (PDHK) and PDH phosphatases, which phosphorylate/inactivate and dephosphorylate/activate PDH, respectively. Our goal was to determine whether the transcription factor forkhead box O1 (FoxO1) regulates PDH activity and glucose oxidation in the heart via increasing the expression of Pdk4, the gene encoding PDHK4. To address this question, we differentiated H9c2 myoblasts into cardiac myocytes and modulated FoxO1 activity, after which Pdk4/PDHK4 expression and PDH phosphorylation/activity were assessed. We assessed binding of FoxO1 to the Pdk4 promoter in cardiac myocytes in conjunction with measuring the role of FoxO1 on glucose oxidation in the isolated working heart. Both pharmacological (1 µM AS1842856) and genetic (siRNA mediated) inhibition of FoxO1 decreased Pdk4/PDHK4 expression and subsequent PDH phosphorylation in H9c2 cardiac myocytes, whereas 10 µM dexamethasone-induced Pdk4/PDHK4 expression was abolished via pretreatment with 1 µM AS1842856. Furthermore, transfection of H9c2 cardiac myocytes with a vector expressing FoxO1 increased luciferase activity driven by a Pdk4 promoter construct containing the FoxO1 DNA-binding element region, but not in a Pdk4 promoter construct lacking this region. Finally, AS1842856 treatment in fasted mice enhanced glucose oxidation rates during aerobic isolated working heart perfusions. Taken together, FoxO1 directly regulates Pdk4 transcription in the heart, thereby controlling PDH activity and subsequent glucose oxidation rates. NEW & NOTEWORTHY Although studies have shown an association between FoxO1 activity and pyruvate dehydrogenase kinase 4 expression, our study demonstrated that pyruvate dehydrogenase kinase 4 is a direct transcriptional target of FoxO1 (but not FoxO3/FoxO4) in the heart. Furthermore, we report here, for the first time, that FoxO1 inhibition increases glucose oxidation in the isolated working mouse heart.

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Agnetti, Giulio, Tullia Maraldi, Diana Fiorentini, et al. "Activation of glucose transport during simulated ischemia in H9c2 cardiac myoblasts is mediated by protein kinase C isoforms." Life Sciences 78, no. 3 (2005): 264–70. http://dx.doi.org/10.1016/j.lfs.2005.04.039.

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Hong, Feng, Keun-ai Moon, Sam Soo Kim та ін. "Role of Phospholipase C-γ1 in Insulin-like Growth Factor I-Induced Muscle Differentiation of H9c2 Cardiac Myoblasts". Biochemical and Biophysical Research Communications 282, № 3 (2001): 816–22. http://dx.doi.org/10.1006/bbrc.2001.4644.

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Zikaki, Kyriaki, Ioanna-Katerina Aggeli, Catherine Gaitanaki, and Isidoros Beis. "Curcumin induces the apoptotic intrinsic pathway via upregulation of reactive oxygen species and JNKs in H9c2 cardiac myoblasts." Apoptosis 19, no. 6 (2014): 958–74. http://dx.doi.org/10.1007/s10495-014-0979-y.

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Bonavita, Francesca, Claudio Stefanelli, Emanuele Giordano, et al. "H9c2 cardiac myoblasts undergo apoptosis in a model of ischemia consisting of serum deprivation and hypoxia: inhibition by PMA." FEBS Letters 536, no. 1-3 (2003): 85–91. http://dx.doi.org/10.1016/s0014-5793(03)00029-2.

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Saleem, Nikhat, and Shyamal K. Goswami. "Activation of adrenergic receptor in H9c2 cardiac myoblasts co-stimulates Nox2 and the derived ROS mediate the downstream responses." Molecular and Cellular Biochemistry 436, no. 1-2 (2017): 167–78. http://dx.doi.org/10.1007/s11010-017-3088-8.

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Marathe, P., M. Thao, and I. Benjamin. "ID: 11: REDOX PROFILING OF CARVEDILOL AND PROPRANOLOL IN A HEART MODEL." Journal of Investigative Medicine 64, no. 4 (2016): 923.1–923. http://dx.doi.org/10.1136/jim-2016-000120.25.

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IntroductionClinical trials have shown that carvedilol is highly effective against heart failure (HF). Carvedilol, unlike propranolol, has direct antioxidant effects and is capable of mitigating oxidative stress in HF patients. Moreover, it has been suggested that carvedilol has an indirect antioxidant mechanism that could involve the initial production of non-lethal levels of oxidative stress leading to the regulation of an uncharacterized antioxidant response that later counters oxidative stress.HypothesisWe hypothesized that carvedilol's indirect antioxidant mechanism may involve the nuclear factor erythroid 2-related factor 2 (Nrf2)/Kelch ECH associating protein 1 (Keap1) pathway, which is a major antioxidant pathway involved in cardiovascular, pulmonary, and neoplastic diseases.MethodsUsing H9C2 rat myoblasts, we confirmed the activation of the Nrf2/Keap1 pathway by detecting levels of downstream protein targets hemeoxygenase-1 (HO-1) and NAD(P)H: quinone oxidoreductase-1 (NQO-1). We transfected H9C2 cells with reductive-oxidative green fluorescent protein (roGFP) fused with human glutaredoxin 1 that targeted mitochondria or cytosol. Redox state changes were quantified by normalized roGFP intensity ratios measured using live-cell imaging.ResultsIn the short term, carvedilol oxidized both cellular compartments while propranolol did not. In the long term, carvedilol upregulated the production of HO-1 and NQO-1 while propranolol downregulated these antioxidant proteins. These results demonstrate that carvedilol's indirect antioxidant effect involves the Nrf2/Keap 1 pathway. This has strong implications as carvedilol is a commonly used, highly effective beta-blocker and elucidating its antioxidant mechanisms can potentially expand the use of carvedilol for the treatment of other diseases, inform the development of new therapeutics, and optimize HF treatment.

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Gupta, M. K., V. Neelakantan, S. Mishra, et al. "A6. An assessment of the role of reactive oxygen species in norepinephrine-induced apoptosis and hypertrophy of H9c2 cardiac myoblasts." Journal of Molecular and Cellular Cardiology 40, no. 6 (2006): 875. http://dx.doi.org/10.1016/j.yjmcc.2006.03.316.

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Yancy, S. L. "Sodium Arsenite Exposure Alters Cell Migration, Focal Adhesion Localization and Decreases Tyrosine Phosphorylation of Focal Adhesion Kinase in H9C2 Myoblasts." Toxicological Sciences 84, no. 2 (2005): 278–86. http://dx.doi.org/10.1093/toxsci/kfi032.

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Thakur, Anita, Md Jahangir Alam, MR Ajayakumar, Saroj Ghaskadbi, Manish Sharma, and Shyamal K. Goswami. "Norepinephrine-induced apoptotic and hypertrophic responses in H9c2 cardiac myoblasts are characterized by different repertoire of reactive oxygen species generation." Redox Biology 5 (August 2015): 243–52. http://dx.doi.org/10.1016/j.redox.2015.05.005.

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Shete, Varsha, Ning Liu, Yuzhi Jia, Navin Viswakarma, Janardan Reddy та Bayar Thimmapaya. "Mouse Cardiac Pde1C Is a Direct Transcriptional Target of Pparα". International Journal of Molecular Sciences 19, № 12 (2018): 3704. http://dx.doi.org/10.3390/ijms19123704.

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Phosphodiesterase 1C (PDE1C) is expressed in mammalian heart and regulates cardiac functions by controlling levels of second messenger cyclic AMP and cyclic GMP (cAMP and cGMP, respectively). However, molecular mechanisms of cardiac Pde1c regulation are currently unknown. In this study, we demonstrate that treatment of wild type mice and H9c2 myoblasts with Wy-14,643, a potent ligand of nuclear receptor peroxisome-proliferator activated receptor alpha (PPARα), leads to elevated cardiac Pde1C mRNA and cardiac PDE1C protein, which correlate with reduced levels of cAMP. Furthermore, using mice lacking either Pparα or cardiomyocyte-specific Med1, the major subunit of Mediator complex, we show that Wy-14,643-mediated Pde1C induction fails to occur in the absence of Pparα and Med1 in the heart. Finally, using chromatin immunoprecipitation assays we demonstrate that PPARα binds to the upstream Pde1C promoter sequence on two sites, one of which is a palindrome sequence (agcTAGGttatcttaacctagc) that shows a robust binding. Based on these observations, we conclude that cardiac Pde1C is a direct transcriptional target of PPARα and that Med1 may be required for the PPARα mediated transcriptional activation of cardiac Pde1C.

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