Vasopressin-induced hypertrophy in H9c2 heart-derived myocytes

Brostrom, Margaret A.; Reilly, Barbara; Wilson, Frank J.; Brostrom, Charles O.

doi:10.1016/s1357-2725(00)00037-6

Cited by 33 publications

(52 citation statements)

References 41 publications

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“…In fact, one of the limitations of the present work is the fact that the H9c2 cell line is phenotypically distinct from cardiac myocytes, even though they share several properties (Hescheler et al 1991;Kimes and Brandt 1976). Although this myoblastic cell line shows similar morphological characteristics to immature embryonic cardiomyocytes, it has been shown to retain several electrical and hormonal signaling pathways found in adult cardiomyocytes and is, therefore, a useful model for studying various aspects of cardiomyocyte physiology and pathophysiology (Brostrom et al 2000;Wayman et al 2001). One particular question currently under study in our laboratory is if differences in cell proliferation observed in undifferentiated vs. differentiated H9c2 cells can alter the susceptibility to Dox or if these same morphological changes occur in non-cardiac cells exposed to Dox in culture.…”

Section: Discussionmentioning

confidence: 90%

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

et al. 2008

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Doxorubicin (Dox) is a very potent antineoplastic agent used against several types of cancer, despite a cumulative cardiomyopathy that reduces the therapeutic index for treatment. H9c2 myoblast cells have been used as an in vitro model to study biochemical alterations induced by Dox treatment on cardiomyocyte cells. Despite the extensive work already published, few data are available regarding morphological alterations of H9c2 cells during Dox treatment. The purpose of the present work was to evaluate Doxinduced morphological alterations in H9c2 myoblasts, focusing especially on the nuclei, mitochondria, and structural fibrous proteins. Treatment of H9c2 cell with low concentrations of Dox causes alterations in fibrous structural proteins including the nuclear lamina and sarcomeric cardiac myosin, as well as mitochondrial depolarization and fragmentation, membrane blebbing with cell shape changes, and phosphatidylserine externalization. For higher Dox concentrations, more profound alterations are evident, including nuclear swelling with disruption of nuclear membrane structure, mitochondrial swelling, and extensive cytoplasm vacuolization. The results obtained indicate that Dox causes morphological alterations in mitochondrial, nuclear, and fibrous protein structures in H9c2 cells, which are dependent on the drug concentration. Data obtained with the present study allow for a better characterization of the effects of Dox on H9c2 myoblasts, used as a model to study Dox-induced cardiotoxicity. The results obtained also provide new and previously unknown targets that can contribute to understand the mechanisms involved in the cardiotoxicity of Dox.

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Section: Discussionmentioning

confidence: 90%

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

et al. 2008

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“…H9c2 cells were hypertrophied by exposure to arginine vasopressin (AVP), which is a peptide neurohormone that is significantly and chronically elevated in the plasma of heart failure patients (18,32) and experimental animals (15) and has effects on processes that participate in the pathogenesis of heart failure, including body fluid regulation, vascular tone, and cardiac contractile function and remodeling (32). AVP may contribute to structural remodeling in heart failure (18) as it has been shown to cause hypertrophy of heart muscle cells in culture (8,39) and stimulate protein synthesis in isolated hearts (16). Moreover, Hupf and colleagues (23) have demonstrated that the heart possesses a local AVP system that is activated in response to pressure overload, suggesting that, in pathological settings, the heart may not only respond to circulating AVP but also to locally produced AVP in a paracrine or autocrine fashion.…”

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confidence: 99%

AMP-activated protein kinase influences metabolic remodeling in H9c2 cells hypertrophied by arginine vasopressin

Saeedi

Saran²,

Wu³

et al. 2009

American Journal of Physiology-Heart and Circulatory Physiology

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Substrate use switches from fatty acids toward glucose in pressure overload-induced cardiac hypertrophy with an acceleration of glycolysis being characteristic. The activation of AMP-activated protein kinase (AMPK) observed in hypertrophied hearts provides one potential mechanism for the acceleration of glycolysis. Here, we directly tested the hypothesis that AMPK causes the acceleration of glycolysis in hypertrophied heart muscle cells. The H9c2 cell line, derived from the embryonic rat heart, was treated with arginine vasopressin (AVP; 1 M) to induce a cellular model of hypertrophy. Rates of glycolysis and oxidation of glucose and palmitate were measured in nonhypertrophied and hypertrophied H9c2 cells, and the effects of inhibition of AMPK were determined. AMPK activity was inhibited by 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo-[1,5-a]pyrimidine (compound C) or by adenovirus-mediated transfer of dominant negative AMPK. Compared with nonhypertrophied cells, glycolysis was accelerated and palmitate oxidation was reduced with no significant alteration in glucose oxidation in hypertrophied cells, a metabolic profile similar to that of intact hypertrophied hearts. Inhibition of AMPK resulted in the partial reduction of glycolysis in AVP-treated hypertrophied H9c2 cells. Acute exposure of H9c2 cells to AVP also activated AMPK and accelerated glycolysis. These elevated rates of glycolysis were not altered by AMPK inhibition but were blocked by agents that interfere with Ca 2ϩ signaling, including extracellular EGTA, dantrolene, and 2-aminoethoxydiphenyl borate. We conclude that the acceleration of glycolysis in AVP-treated hypertrophied heart muscle cells is partially dependent on AMPK, whereas the acute glycolytic effects of AVP are AMPK independent and at least partially Ca 2ϩ dependent. cardiac hypertrophy; energy metabolism; glucose utilization

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“…We used the clonal rat muscle cell line H9c2 as a cell model of normal cardiac myocytes. This cell line is derived from embryonic rat heart tissue and has properties of skeletal muscle as well as cardiac muscle [11,12].…”

Section: Discussionmentioning

confidence: 99%

Distribution of beta-enolase in normal and tumor rat cells.

Seweryn

Bednarz−Misa²,

Danielewicz³

et al. 2009

Folia Histochem Cytobiol.

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Enolase -a glycolytic enzyme is also expressed on the surface of eukaryotic cells such as macrophages, neutrophils, endothelial, neuronal, tumor cells. Surface enolase as plasminogen receptor plays an important role in myogenesis, tumorgenesis and angiogenesis. Determination of enolase localization in the cell lines may give rise to the elucidation of its receptor function in tumor cells. The cellular localization of the muscle-specific isoform of the enolase in normal rat cardiomyocytes (H9c2, an embryonic rat heart-derived cell line) and a rat sarcoma (R1) cell line is reported here. Immunocytochemical assays showed that this enolase isoform is freely diffused in the sarcoplasm of rat cells. The evident location of enolase molecules on the perinuclear surface is observed in immunofluorescence assays. Enolase localization on the surface of some intact normal rat cardiomyocytes was also observed. This surface protein maintains enolase catalytic activity.

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Vasopressin-induced hypertrophy in H9c2 heart-derived myocytes

Cited by 33 publications

References 41 publications

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

Morphological alterations induced by doxorubicin on H9c2 myoblasts: nuclear, mitochondrial, and cytoskeletal targets

AMP-activated protein kinase influences metabolic remodeling in H9c2 cells hypertrophied by arginine vasopressin

Distribution of beta-enolase in normal and tumor rat cells.

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