Tubulin ligands suggest a microtubule–NADPH oxidase relationship in postischemic cardiomyocytes

Devillard, L.; Vandroux, David; Tissier, Cindy; Brochot, Amandine; Voisin, Sophie; Rochette, Luc; Athias, Pierre

doi:10.1016/j.ejphar.2006.08.004

Cited by 16 publications

(8 citation statements)

References 36 publications

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“…Several lines of evidence support this theory: 1) Rac is a required subunit for Nox2 activation and inhibition of Rac1 blocks X-ROS signaling [1]; 2) Rac1 binds microtubules [37] and translocates to gp91 phox separately from other regulatory subunits [36]; 3) Microtubules have been suggested to facilitate the recruitment of activating subunits to gp91 phox in the membrane [38]; 4) destabilization of the microtubule network inhibits Nox2 activity [38] and blocks X-ROS signaling [1, 6]. Still, a clear demonstration of stretch-dependent Rac1 recruitment to gp91 phox in a microtubule-dependent fashion is needed to validate this model.…”

Section: Resultsmentioning

confidence: 99%

X-ROS signaling in the heart and skeletal muscle: Stretch-dependent local ROS regulates [Ca2+]i

Prosser

Khairallah

Ziman

et al. 2013

Journal of Molecular and Cellular Cardiology

107

112

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X-ROS signaling is a novel redox signaling pathway that links mechanical stress to changes in [Ca2+]i. This pathway is activated rapidly and locally within a muscle cell under physiological conditions, but can also contribute to Ca2+-dependent arrhythmia in heart and to the dystrophic phenotype in heart and skeletal muscle. Upon physiologic cellular stretch, microtubules serve as mechanotransducers to activate NADPH oxidase 2 in the transverse tubules and sarcolemmal membranes to produce reactive oxygen species (ROS). In heart, the ROS acts locally to activate ryanodine receptor Ca2+ release channels in the junctional sarcoplasmic reticulum, increasing the Ca2+ spark rate and “tuning” excitation-contraction coupling. In skeletal muscle, where Ca2+ sparks are not normally observed, the X-ROS signaling process is muted. However in muscular dystrophies, such as Duchenne Muscular Dystrophy and dysferlinopathy, X-ROS signaling operates at a high level and contributes to myopathy. Importantly, Ca2+ permeable stretch-activated channels are activated by X-ROS and contribute to skeletal muscle pathology. Here we review X-ROS signaling and mechanotransduction in striated muscle, and highlight important questions to drive future work on stretch-dependent signaling. We conclude that X-ROS provides an exciting mechanism for the mechanical control of redox and Ca2+ signaling, but much work is needed to establish its contribution to physiologic and pathophysiologic processes in diverse cell systems.

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Section: Resultsmentioning

confidence: 99%

X-ROS signaling in the heart and skeletal muscle: Stretch-dependent local ROS regulates [Ca2+]i

Prosser

Khairallah

Ziman

et al. 2013

Journal of Molecular and Cellular Cardiology

107

112

View full text Add to dashboard Cite

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“…The role of coronin-6 in cardiac muscle is yet to be described but changes in the expression of coronin 1 are associated with the transition to maladaptive cardiac hypertrophy induced by transgenic overexpression of myotrophin[33]. Changes in microtubule proteins are consistent with elevated oxidative stress [34] and proteasomal dysfunction [35], which may contribute to the development of cardiomyopathy [36]. Accordingly, LCR exhibited greater expression of proteasome activator complex subunit 1 (PA28α).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis reveals perturbed energy metabolism and elevated oxidative stress in hearts of rats with inborn low aerobic capacity

et al. 2011

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Selection on running capacity has created rat phenotypes of high capacity runners (HCR) that have enhanced cardiac function and low capacity runners (LCR) that exhibit risk factors of metabolic syndrome. We analysed hearts of HCR and LCR from generation 22 of selection using DIGE and identified proteins from MS database searches. The running capacity of HCR was 6-fold greater than LCR. DIGE resolved 957 spots and proteins were unambiguously identified in 369 spots. Protein expression profiling detected 67 statistically significant (P<0.05; false discovery rate <10 %, calculated using q-values) differences between HCR and LCR. Hearts of HCR rats exhibited robust increases in the abundance of each enzyme of the beta-oxidation pathway. In contrast, LCR hearts were characterised by the modulation of enzymes associated with ketone body or amino acid metabolism. LCR also exhibited enhanced expression of antioxidant enzymes such as catalase and greater phosphorylation of alpha B-crystallin at serine 59, which is a common point of convergence in cardiac stress signalling. Thus proteomic analysis revealed selection on low running capacity is associated with perturbations in cardiac energy metabolism and provided the first evidence that the LCR cardiac proteome is exposed to greater oxidative stress.

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“…Cytoskeleton disorganization, and more particularly that of the microtubules, seems to play a significant role in the pathogenesis of the myocardial injury induced by ischemiareperfusion [196,197] and that a possible interplay between microtubule plasticity and NADPH oxidase exists in cardiomyocytes [198].…”

Section: Cytoskeletonmentioning

confidence: 99%

Molecular and Biochemical Changes of the Cardiovascular System due to Smoking Exposure

Armani¹,

Landini²,

Leone³

2009

CPD

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Cigarette smoking (CS) is a major health hazard particularly for the cardiovascular system and cancer. The mechanisms involved in CS-related cardiovascular dysfunction have been largely debated. CS increases inflammation, thrombosis, and oxidation of low-density lipoproteins. Recent experimental and clinical data support the hypothesis that cigarette smoke exposure increases oxidative stress as a potential mechanism for initiating cardiovascular dysfunction. Cardiac myocytes, as well as and other long-lived postmitotic cells show dramatic smoke-related alterations that mainly affect the mitochondria and lysosomal compartment. Mitochondria are primary sites of reactive oxygen species formation that cause progressive damage to mitochondrial DNA and proteins in parallel to intralysosomal lipofuscin accumulation. There is amassing evidence that various mechanisms may contribute to accumulation of damaged mitochondria following initial oxidative injury. Such mechanisms may include clonal expansion of defective mitochondria, decreased propensity of altered mitochondria to become autophagocytosed, suppressed autophagy because of heavy lipofuscin loading of lysosomes and decreased efficiency of specific proteases involved into mitochondrial degradation. A possible interplay between microtubule plasticity and oxidative stress also exists in cardiomyocytes, so this could represent another potential mechanism by which smoking induces/accelerates atherosclerosis.

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Tubulin ligands suggest a microtubule–NADPH oxidase relationship in postischemic cardiomyocytes

Cited by 16 publications

References 36 publications

X-ROS signaling in the heart and skeletal muscle: Stretch-dependent local ROS regulates [Ca2+]i

X-ROS signaling in the heart and skeletal muscle: Stretch-dependent local ROS regulates [Ca2+]i

Proteomic analysis reveals perturbed energy metabolism and elevated oxidative stress in hearts of rats with inborn low aerobic capacity

Molecular and Biochemical Changes of the Cardiovascular System due to Smoking Exposure

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