Oxidized proteins as a marker of oxidative stress during coronary heart surgery

Pantke, Ulrich; Volk, Thomas; Schmutzler, M.; Kox, Wolfgang J.; Sitte, Nicolle; Grune, Tilman

doi:10.1016/s0891-5849(99)00144-6

Cited by 107 publications

(78 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…PCC increased during the early phase of reperfusion (2 min) and remained constant for hours. At 18 h, PCC level was markedly reduced to Ϸ50% of the value at early reperfusion (2 min to 4 h) (38). In another animal study it was indicated that muscle PCC level was unaffected by extensive exercise or age (39,40).…”

Section: Discussionmentioning

confidence: 95%

Plasma antioxidant status and cell injury after severe physical exercise

Chevion

Moran

Heled

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

221

137

View full text Add to dashboard Cite

Strenuous exercise leads to an increase in metabolic rate, increased production of reactive oxygen species, and compromised antioxidant defense systems. To study the effects of oxidative stress during strenuous exercise, a homogeneous group of 31 male subjects participated in a 6-month, 5 days͞week training schedule involving two extreme marches of 50 km and 80 km at sea level, separated by 2 weeks of regular training. Each participant carried 35 kg of extra weight. Blood samples were drawn imediately before and after each march. Twenty-nine subjects completed the 50-km march, and only 16 completed the 80-km march. Plasma levels of reduced ascorbic acid, total ascorbate, and dehydroascorbate did not undergo significant changes during either march. However, the 50-and 80-km marches led to 25% and 37% increases, respectively, in plasma levels of uric acid; due presumably to increases in the metabolic rate and consequent pyrimidine nucleotide metabolism. Both marches led to Ϸ10-fold increase leakage of creatine phosphokinase into the plasma. Likewise, plasma levels of aspartate transaminase, a characteristic marker of liver injury, increased Ϸ4-fold. Plasma levels of bilirubin, creatine, urea, and glucose also increased. Plasma protein carbonyl content, a marker of protein oxidative damage, decreased significantly during each march. These results are discussed with respect to the consideration that elevation of the respiration rate during exercise leads to production of more reactive oxygen species than the antioxidant systems can scavenge. Plausible explanations for leakage of molecules into the plasma are discussed.

show abstract

Section: Discussionmentioning

confidence: 95%

Plasma antioxidant status and cell injury after severe physical exercise

Chevion

Moran

Heled

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

221

137

View full text Add to dashboard Cite

show abstract

“…Effect of obesity on SERCA2a oxidation and SERCA activity Persistent oxidative stress leads to oxidative damage to proteins such as SERCA [27,35,36]. Given that protein carbonyl formation, a fundamental measure of oxidative damage in cardiac proteins [22,37], is elevated in Lep/Lep heart, we evaluated oxidative damage to SERCA2a by quantitative immunoprecipitation of SERCA2a from cell lysates using specific SERCA2a antibody followed by immunoprobe of the protein carbonyl content. The total expression of immunoprecipitated SERCA2a proteins did not differ among lean myocytes, Lep/Lep myocytes and cells treated with apocynin or angiotensin.…”

Section: Mechanical Properties Of Cardiomyocytesmentioning

confidence: 99%

Cardiac contractile dysfunction in Lep/Lep obesity is accompanied by NADPH oxidase activation, oxidative modification of sarco(endo)plasmic reticulum Ca2+-ATPase and myosin heavy chain isozyme switch

et al. 2006

View full text Add to dashboard Cite

Aims/hypothesis: Obesity is an independent risk factor for heart diseases but the underlying mechanism is not clear. This study examined cardiac contraction, oxidative stress, oxidative modification of sarco(endo) plasmic reticulum Ca 2+ -ATPase (SERCA) and the myosin heavy chain (MHC) isoform switch in obese mice. Methods: Mechanical properties were evaluated in ventricular myocytes from C57BL/6J lean and Lep/Lep obese mice (formerly known as ob/ob mice), including peak shortening (PS), time to 50 or 90% PS, time to 50 or 90% relengthening (TR 50 , TR 90 ), maximal velocity of shortening/relengthening (±dL/dt), intracellular Ca 2+ and its decay (τ). Oxidative stress, lipid peroxidation, protein damage and SERCA activity were assessed by glutathione/glutathione disulfide, malondialdehyde, protein carbonyl and 45 Ca 2+ uptake, respectively. NADPH oxidase was determined by immunoblotting. Results: Myocytes from Lep/Lep mice displayed depressed PS and ± dL/dt, prolonged TR 50 , TR 90 , elevated resting [Ca 2+ ] i , prolonged τ, reduced contractile capacity at high stimulus frequencies and diminished responsiveness to extracellular Ca 2+ compared with lean controls. Cardiac glutathione/glutathione disulfide was decreased whereas malondialdehyde, protein carbonyl, membrane p47 phox and membrane gp91 phox were increased in the Lep/Lep group. SERCA isoenzyme 2a was markedly modified by oxidation in Lep/ Lep hearts and associated with decreased 45 Ca 2+ uptake. The MHC isozyme displayed a shift from the α to the β isoform in Lep/Lep hearts. Short-term incubation of angiotensin II with myocytes mimicked the mechanical defects, SERCA oxidation and 45 Ca 2+ uptake seen in Lep/ Lep myocytes. Incubation of the NADPH oxidase inhibitor apocynin with Lep/Lep myocytes alleviated contractile defects without reversing SERCA oxidation or activity. Conclusions/interpretation: These data indicate that obesity-related cardiac defects may be related to NADPH oxidase activation, oxidative damage to SERCA and the MHC isozyme switch.

show abstract

“…Persistent oxidative stress leads to malfunction of cardiac Ca 2ϩ cycling proteins such as SERCA (19,21). Given that oxidative stress and protein carbonyl formation, fundamental measures of oxidative damage in cardiac proteins (22,23), are elevated in ob/ob cardiomyocytes, we evaluated SERCA function using 45 Ca 2ϩ uptake. Results shown in Figure 4B illustrate a significantly reduced SERCA activity in ob/ob cardiomyocytes, which was ablated by both Cr(D-phe) 3 and Cr(pic) 3 , with a more pronounced effect from Cr(D-phe) 3 .…”

Section: Effect Of Chromium Supplementation On Glucose Uptake Serca mentioning

confidence: 99%

Chromium (d‐Phenylalanine)₃ Improves Obesity‐Induced Cardiac Contractile Defect in ob/ob Mice

Dong

Yang

Nair

et al. 2007

Obesity

View full text Add to dashboard Cite

DONG, FENG, XIAOPING YANG, NAIR SREEJAYAN, AND JUN REN. Chromium (D-phenylalanine) 3 improves obesity-induced cardiac contractile defect in ob/ob mice. Obesity. 2007;15:2699 -2711. Objective: Low-molecular weight chromium compounds, such as chromium picolinate [Cr(pic) 3 ], improve insulin sensitivity, although toxicity is a concern. We synthesized a novel chromium complex, chromium (D-phenylalanine) 3 [Cr(D-phe) 3 ], in an attempt to improve insulin sensitivity with reduced toxicity. The aim of this study was to compare the two chromium compounds on cardiac contractile function in ob/ob obese mice. Research Methods and Procedures: C57BL lean and ob/ob obese mice were randomly divided into three groups: H 2 O, Cr(D-phe) 3 , or Cr(pic) 3 (45 g/kg per day orally for 6 months). Results:The glucose tolerance test displayed improved glucose clearance by Cr(D-phe) 3 but not Cr(pic) 3 . Myocytes from ob/ob mice exhibited depressed peak shortening (PS) and maximal velocity of shortening/relengthening (ϮdL/ dt), prolonged time-to-PS and time-to-90% relengthening (TR90), reduced electrically stimulated rise in intracellular Ca 2ϩ (⌬fura-2 fluorescence intensity), and slowed intracellular Ca 2ϩ decay. Although a 3-month Cr(D-phe) 3 treatment for a separate group of ob/ob and lean 2-month-old mice only rectified reduced ϮdL/dt in ob/ob mice, all mechanical and intracellular Ca 2ϩ abnormalities were significantly attenuated or ablated by 6 months of Cr(D-phe) 3 but not Cr(pic) 3 treatment (except TR90). Sarco(endo)plasmic reticulum Ca 2ϩ ATPase activity and Na ϩ -Ca 2ϩ exchanger expression were depressed in ob/ob mice, which were reversed by both Cr(D-phe) 3 and Cr(pic) 3 , with a more pronounced effect from Cr(D-phe) 3 . Cr(D-phe) 3 corrected reduced insulin-stimulated glucose uptake and improved basal phosphorylation of Akt and insulin receptor, as well as insulin-stimulated phosphorylation of Akt and insulin receptor in ob/ob myocytes. Heart homogenates from ob/ob mice had enhanced oxidative stress and protein carbonyl formation compared with the lean group, which were attenuated by both Cr(D-phe) 3 and Cr(pic) 3 . Discussion: Our data suggest that the new Cr(D-phe) 3 compound possesses better cardio-protective and insulin-sensitizing properties against obesity.

show abstract

Oxidized proteins as a marker of oxidative stress during coronary heart surgery

Cited by 107 publications

References 43 publications

Plasma antioxidant status and cell injury after severe physical exercise

Plasma antioxidant status and cell injury after severe physical exercise

Cardiac contractile dysfunction in Lep/Lep obesity is accompanied by NADPH oxidase activation, oxidative modification of sarco(endo)plasmic reticulum Ca2+-ATPase and myosin heavy chain isozyme switch

Chromium (d‐Phenylalanine)₃ Improves Obesity‐Induced Cardiac Contractile Defect in ob/ob Mice

Contact Info

Product

Resources

About

Oxidized proteins as a marker of oxidative stress during coronary heart surgery

Cited by 107 publications

References 43 publications

Plasma antioxidant status and cell injury after severe physical exercise

Plasma antioxidant status and cell injury after severe physical exercise

Cardiac contractile dysfunction in Lep/Lep obesity is accompanied by NADPH oxidase activation, oxidative modification of sarco(endo)plasmic reticulum Ca2+-ATPase and myosin heavy chain isozyme switch

Chromium (d‐Phenylalanine)3 Improves Obesity‐Induced Cardiac Contractile Defect in ob/ob Mice

Contact Info

Product

Resources

About

Chromium (d‐Phenylalanine)₃ Improves Obesity‐Induced Cardiac Contractile Defect in ob/ob Mice