Proteomic analysis of mitochondrial proteins in cardiomyocytes from chronic stressed rat

Liu, Xiaohua; Lei, Qian; Gong, Jicheng; Shen, Jing; Zhang, Xuemin; Qian, Xiaohong

doi:10.1002/pmic.200300845

Cited by 55 publications

(34 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In our previous study, we found that the PHB content in mitochondria increased in apoptotic cardiomyocytes induced by restraint stress (Liu et al 2004). To determine whether PHB played a role in regulating the cardiomyocyte apoptosis induced by H 2 O 2 intervention, the apoptotic rate of cardiomyocytes treated with 200 μM H 2 O 2 for 12 h was examined by flow cytometry.…”

Section: Overexpression Of Prohibitin Inhibits Oxidative Stress-inducmentioning

confidence: 96%

“…Recently, Vessal and colleagues have found that PHB existing in extracellular fluid of cultured adipocytes can be translocated to mitochondria and modulates mitochondrial fuel metabolism by inhibition of pyruvate carboxylase (Vessal et al 2006). Previous studies in our laboratory (Liu et al 2004) using proteomics technology have found PHB expression in mitochondria increased dramatically when cardiac structures and functions were injured by chronic restraint stress. However, the function of PHB in cardiomyocytes is still far from clear.…”

Section: Introductionmentioning

confidence: 94%

See 1 more Smart Citation

Prohibitin protects against oxidative stress-induced cell injury in cultured neonatal cardiomyocyte

Liu¹,

Ren²,

Zhan³

et al. 2009

Cell Stress and Chaperones

View full text Add to dashboard Cite

Oxidative stress is one of the main causes of myocardial injury, which is associated with cardiomyocyte death. Mitochondria play a key role in triggering the necrosis and apoptosis pathway of cardiomyocytes under oxidative stress. Although prohibitin (PHB) has been acknowledged as a mitochondrial chaperone, its functions in cardiomyocytes are poorly characterized. The present research was designed to investigate the cardioprotective role of PHB in mitochondria. Oxidative stress can increase the PHB content in mitochondria in a time-dependent manner. Overexpression of PHB in cultured cardiomyocytes by transfection of recombinant adenovirus vector containing PHB sense cDNA resulted in an increase of PHB in mitochondria. Compared with the non-transfection cardiomyocytes, PHB overexpression could protect the mitochondria from oxidative stress-induced injury. The mitochondria-mediated apoptosis pathway was consistently suppressed in PHB-overexpressed cardiomyocytes after hydrogen peroxide (H(2)O(2)) treatment, including a reduced change in mitochondrial membrane permeability transition and an inhibited release of cytochrome c from mitochondria to cytoplasma. As a result, the oxidative stress-induced cardiomyocyte apoptosis was suppressed. These data indicated that PHB protected the cardiomyocytes from oxidative stress-induced damage, and that increasing PHB content in mitochondria constituted a new therapeutic target for myocardium injury.

show abstract

Section: Overexpression Of Prohibitin Inhibits Oxidative Stress-inducmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 94%

Prohibitin protects against oxidative stress-induced cell injury in cultured neonatal cardiomyocyte

Liu¹,

Ren²,

Zhan³

et al. 2009

Cell Stress and Chaperones

View full text Add to dashboard Cite

show abstract

“…Whereas there is no literature concerning phosphorylation of CPT2, it is known that phosphorylation of CPT1 occurs and that phosphorylation increases CPT1 activity (66). CPT2 activity decreased in rat heart after chronic stress (78), but its association with responses to severe hemorrhage has not been documented.…”

Section: Discussionmentioning

confidence: 99%

Cardiac mitochondrial proteomic expression in inbred rat strains divergent in survival time after hemorrhage

Klemcke

DeKroon

Mocanu

et al. 2013

Physiological Genomics

View full text Add to dashboard Cite

Klemcke HG, DeKroon RM, Mocanu M, Robinette JB, Alzate O. Cardiac mitochondrial proteomic expression in inbred rat strains divergent in survival time after hemorrhage. Physiol Genomics 45: 243-255, 2013. First published February 5, 2013 doi:10.1152/physiolgenomics.00118.2012.-We have previously identified inbred rat strains differing in survival time to a severe controlled hemorrhage (StaH). In efforts to identify cellular mechanisms and ultimately genes that are important contributors to enhanced STaH, we conducted a study to characterize potential differences in cardiac mitochondrial proteins in these rats. Inbred rats from three strains [Brown Norway/Medical College of Wisconsin (BN); Dark Agouti (DA), and Fawn Hooded Hypertensive (FHH)] with different StaH (DA ϭ FHH Ͼ BN) were assigned to one of three treatment groups (n ϭ 4/strain): nonoperated controls, surgically catheterized rats, or rats surgically catheterized and hemorrhaged 24 h postsurgery. Rats were euthanized 30 min after handling or 30 min after initiation of a 26 min hemorrhage. After euthanasia, hearts were removed and mitochondria isolated. Differential protein expression was determined using 2D DIGE-based Quantitative Intact Proteomics and proteins identified by MALDI/TOF mass spectrometry. Hundreds of proteins (791) differed among inbred rat strains (P Յ 0.038), and of these 81 were identified. Thirty-eight were unique proteins and 43 were apparent isoforms. For DA rats (longest STaH), 36 proteins increased and 30 decreased compared with BN (shortest STaH). These 81 proteins were associated with lipid (e.g., acyl CoA dehydrogenase) and carbohydrate (e.g., fumarase) metabolism, oxidative phosphorylation (e.g., ubiquinol-cytochrome C reductase), ATP synthesis (F1 ATPase), and H2S synthesis (3-mercaptopyruvate sulfurtransferase). Although we cannot make associations between these identified mitochondrial proteins and StaH, our data do provide evidence for future candidate proteins with which to consider such associations. inbred rats; hemorrhage; proteomics; respiration; cellular pathways; mitochondrial proteomics; 2D DIGE; quantitative intact proteomics PREVIOUS INVESTIGATIONS IN humans (114), dogs (32), and rats (125) have indicated considerable variability in their ability to survive severe hemorrhage and attendant shock. In attempts to understand the nature of this variability, we have recently initiated studies to identify genetic determinants of survival time after controlled hemorrhage (StaH) (68 -69). Our initial investigations have identified several inbred rat strains sufficiently divergent in survival time to warrant their continued use for further genetic-and cellular-level investigations (68, 69). To supplement our search for genetic determinants, in the current study we have investigated mitochondrial characteristics of inbred rat strains divergent in After acute hemorrhage a complex of interacting systemslevel responses occur as the body attempts to maintain homeostasis (101). As the biological pump that provides oxygen and nutr...

show abstract

“…In a previous study, we observed cardiovascular function disruption and pathological alterations in the electrocardiograms of chronically restraint-stressed rats (Wang et al 2009). Cardiomyocyte damage is considered to be an important cellular basis for stress-induced cardiovascular injury and disease (Liu et al 2004). However, the mechanism of stress-induced cardiomyocyte injury remains unclear.…”

Section: Discussionmentioning

confidence: 99%

HSP70 inhibits stress-induced cardiomyocyte apoptosis by competitively binding to FAF1

Gao¹,

Liu²,

Huang³

et al. 2015

Cell Stress and Chaperones

View full text Add to dashboard Cite

Stress-induced cardiomyocyte apoptosis plays an important role in the pathogenesis of a variety of cardiovascular diseases. Our early studies showed that HSP70 effectively inhibited apoptosis, but the underlying mechanism remained unclear. Fas-associated factor 1 (FAF1) is a member of the Fas death-inducing signaling complex (Fas-DISC) that acts upstream of caspase-8. We investigated the interactions among FAF1, HSP70, and FAS in stressed cardiomyocytes to elucidate the protective mechanism of HSP70. FAS and caspase-3/8 activity was higher in cardiomyocytes undergoing stress-induced apoptosis in restraint-stressed rats compared with cardiomyocytes in non-stressed rats, which indicated that the Fas signaling pathway was activated after restraint stress. Geranylgeranylacetone (GGA) induced an increase in HSP70 expression, which reduced stress-induced apoptosis. Additionally, overexpression of HSP70 via transfection with the pEGFP-rHSP70 plasmid attenuated norepinephrine (NE)-induced apoptosis. FAF1 expression increased during stressinduced apoptosis, and overexpression of FAF1 exacerbated NE-induced apoptosis. We also found that HSP70 interacted with FAF1. Overexpression of HSP70 inhibited the binding of FAF1 to FAS in H9C2 cells, which indicated that HSP70 suppressed NE-induced apoptosis by competitively binding to FAF1. An N-terminal deletion mutant of HSP70 (HSP70-△N) was unable to interact with FAF1. After HSP70-△N was transfected into H9C2 cells, the cells were unable to attenuate the NE-induced increases in caspase-8 and apoptosis. These results indicate that the 1-120 sequence of HSP70 binds to FAF1, which alters the interactions between FAS and FAF1 and inhibits the activation of the Fas signaling pathway and apoptosis.

show abstract

Proteomic analysis of mitochondrial proteins in cardiomyocytes from chronic stressed rat

Cited by 55 publications

References 27 publications

Prohibitin protects against oxidative stress-induced cell injury in cultured neonatal cardiomyocyte

Prohibitin protects against oxidative stress-induced cell injury in cultured neonatal cardiomyocyte

Cardiac mitochondrial proteomic expression in inbred rat strains divergent in survival time after hemorrhage

HSP70 inhibits stress-induced cardiomyocyte apoptosis by competitively binding to FAF1

Contact Info

Product

Resources

About