Effects of oxidative stress on the cardiac myocyte proteome: modifications to peroxiredoxins and small heat shock proteins

Cullingford, Tim E.; Wait, Robin; Clerk, Angela; Sugden, Peter H.

doi:10.1016/j.yjmcc.2005.10.004

Cited by 30 publications

(28 citation statements)

References 74 publications

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“…The abundance of spot 602 was increased by 13 or 17% (P b 0.05) in PFTN RST compared to TN or HS, respectively. Previous studies have indicated that oxidation of the active cysteine residue results in the shift to a more acidic pI [92,93]. Peroxiredoxins 3 and 6 have been identified as potential biomarkers for warm ischemia in a donation after circulatory death model in pig kidneys [94].…”

Section: Antioxidant Proteinsmentioning

confidence: 99%

Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress

Cruzen

Pearce

Baumgard

et al. 2015

Journal of Proteomics

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Section: Antioxidant Proteinsmentioning

confidence: 99%

Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress

Cruzen

Pearce

Baumgard

et al. 2015

Journal of Proteomics

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“…Because of the ubiquity and necessity of heat shock proteins for stress signaling in the heart (4 -7), it is not surprising that other proteomic studies utilizing distinct models of cardiac stress signaling observed alterations in heat shock protein expression and modification. Changes involved ␣B-crystallin and HSP27 in a tachycardia-induced model of congestive heart failure in dogs (5) and alterations in multiple HSPs (potentially including phosphorylation) in response to oxidative stress in neonatal rat cardiomyocytes (6).…”

Section: Proteomic Analysis In Diseased Cardiac Phenotypesmentioning

confidence: 99%

Proteomics-based Development of Biomarkers in Cardiovascular Disease

Mayr

Zhang²,

Greene

et al. 2006

Molecular & Cellular Proteomics

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“…␣B-crystallin does not have any cysteine residues (31), but its activity may be modified by oxidation of its other amino acid residues (41). Furthermore, the activity and actions of all of the HSPs may be influenced by oxidation of their potential target proteins (5,40,42,44,50).…”

mentioning

confidence: 99%

Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers

Larkins

Murphy

Lamb

2012

American Journal of Physiology-Cell Physiology

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Larkins NT, Murphy RM, Lamb GD. Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. Am J Physiol Cell Physiol 303: C654 -C665, 2012. First published July 3, 2012; doi:10.1152/ajpcell.00180.2012.-Heat shock proteins (HSPs) help maintain cellular function in stressful situations, but the processes controlling their interactions with target proteins are not well defined. This study examined the binding of HSP72, HSP25, and ␣B-crystallin in skeletal muscle fibers following various stresses. Rat soleus (SOL) and extensor digitorum longus (EDL) muscles were subjected in vitro to heat stress or strongly fatiguing stimulation. Superficial fibers were "skinned" by microdissection and HSP diffusibility assessed from the extent of washout following 10-to 30 min exposure to a physiological intracellular solution. In fibers from nonstressed (control) SOL muscle, Ͼ80% of each HSP is readily diffusible. However, after heating a muscle to 40°C for 30 min ϳ95% of HSP25 and ␣B-crystallin becomes tightly bound at nonmembranous myofibrillar sites, whereas HSP72 bound at membranous sites only after heat treatment to Ն44°C. The ratio of reduced to oxidized cytoplasmic glutathione (GSH:GSSG) decreased approximately two-and fourfold after heating muscles to 40°and 45°C, respectively. The reducing agent dithiothreitol reversed HSP72 binding in heated muscles but had no effect on the other HSPs. Intense in vitro stimulation of SOL muscles, sufficient to elicit substantial oxidation-related loss of maximum force and approximately fourfold decrease in the GSH:GSSG ratio, had no effect on diffusibility of any of the HSPs. When skinned fibers from heat-treated muscles were bathed with additional exogenous HSP72, total binding increased approximately two-and 10-fold, respectively, in SOL and EDL fibers, possibly reflective of the relative sarco(endo)plasmic reticulum Ca 2ϩ -ATPase pump densities in the two fiber types. Phosphorylation at Ser59 on ␣B-crystallin and Ser85 on HSP25 increased with heat treatment but did not appear to determine HSP binding. The findings highlight major differences in the processes controlling binding of HSP72 and the two small HSPs. Binding was not directly related to cytoplasmic oxidative status, but oxidation of cysteine residues influenced HSP72 binding. oxidation; stress response; skinned fiber; chaperones HEAT SHOCK PROTEINS (HSPs) are highly conserved and ubiquitously expressed proteins that act as protein chaperones and in stress situations bind and interact with various proteins to help preserve or restore their function (23,32). A great deal of work in skeletal muscle has focused on the increase in HSP protein and/or mRNA expression levels occurring in hours to days after various stressful stimuli, such as eccentric exercise (11,17,26,27,39), oxidative stress (50), heat (4, 35), and glycogen depletion (12). The present study focuses instead on the acute responses of HSPs to stresses, examining the effects of heat, contraction, and o...

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Effects of oxidative stress on the cardiac myocyte proteome: modifications to peroxiredoxins and small heat shock proteins

Cited by 30 publications

References 74 publications

Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress

Proteomic changes to the sarcoplasmic fraction of predominantly red or white muscle following acute heat stress

Proteomics-based Development of Biomarkers in Cardiovascular Disease

Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers

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