Analysis of peroxiredoxin decreasing oxidative stress in hypertensive aortic smooth muscle

Lee, Chang-Kwon; Kim, Hyo Jin; Lee, Youn Ri; So, Hyeon Ha; Park, Hyojun; Won, Kyung‐Jong; Park, Taekyu; Lee, Kyung-Yung; Lee, Hwan Myung

doi:10.1016/j.bbapap.2007.04.018

Cited by 27 publications

(24 citation statements)

References 35 publications

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“…Proteomics provides useful tools for identifying proteins, e.g., membrane proteins involved in various physiological or pathophysiological conditions in cells [15]. Recently, we identified the whole proteome of the rat aorta using 2-dimensional gel electrophoresis (2-DE)-based proteomics [16] and also found a protein related to a cofactor of NO synthase in hypertensive vessels [17].…”

Section: Introductionmentioning

confidence: 99%

Monoclonal Antibody against α-Actinin 4 from Human Umbilical Vein Endothelial Cells Inhibits Endothelium-Dependent Vasorelaxation

et al. 2013

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Background: This study was attempted to identify new molecules expressed on the plasma membrane of human umbilical vein endothelial cells (HUVECs) using monoclonal antibody-based proteomics technology and to determine the effect of the identified antibody on vascular reactivity. Methods: Twenty-two antibodies were developed from rats inoculated with HUVECs, and their effects were determined by observing vascular reactivity. Results: Among the 22 antibodies, the C-7 antibody significantly inhibited endothelium-dependent vasorelaxation in response to acetylcholine (ACh) but not to histamine. Moreover, the C-7 antibody did not affect norepinephrine-induced contraction in either the endothelium-intact or -denuded aorta. A proteomics study involving immunoprecipitation of the C-7 antibody with biotinylated HUVECs showed that this antibody binds to plasma membrane proteins corresponding to immunoglobulin heavy chain (VHDJ region), chaperonin-containing T-complex polypeptide 1 and α-actinin 4. The muscarinic M3 ACh receptor and α-actinin 4 were colocalized on the plasma membrane of HUVECs, and the colocalization was found to increase in response to ACh and was inhibited by pretreatment with the C-7 antibody. Conclusions: These results demonstrate that monoclonal C-7 antibody exerts an inhibitory effect on endothelium-dependent vasorelaxation induced by ACh and that this response may at least partially result from the inhibition of α-actinin 4.

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Section: Introductionmentioning

confidence: 99%

Monoclonal Antibody against α-Actinin 4 from Human Umbilical Vein Endothelial Cells Inhibits Endothelium-Dependent Vasorelaxation

et al. 2013

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“…This proposal is supported by the alterations in the biochemical index, including an increase in the MDA content and a decrease in SOD activity, which suggest that a redox imbalance occurs in the mouse kidney after ASB treatment. [35,36] . Several mechanisms for the in vivo upregulation of PRDX6 have been described, including the high level of superoxide caused by a lack of NO to scavenge superoxide in the nNOS-knockout mouse [30] , the excessive ROS generated by complex I due to increased glutathione oxidation after ischemia-reperfusion [37] , and the high level of endogenous ROS resulting from the markedly reduced GSH level in a CFTR-defective mouse lung [38] .…”

Section: Protein Involved In Cellular Energeticsmentioning

confidence: 99%

Proteomic alterations in mouse kidney induced by andrographolide sodium bisulfite

et al. 2011

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Aim: To identify the key proteins involved in the nephrotoxicity induced by andrographolide sodium bisulfite (ASB). Methods: Male ICR mice were intravenously administrated with ASB (1000 or 150 mg·kg -1 ·d -1 ) for 7 d. The level of malondialdehyde (MDA) and the specific activity of superoxide dismutase (SOD) in kidneys were measured. The renal homogenates were separated by two-dimensional electrophoresis, and the differential protein spots were identified using a matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF)/TOF mass spectrometry. Results: The high dose (1000 mg/kg) of ASB significantly increased the MDA content, but decreased the SOD activity as compared to the control mice. The proteomic analysis revealed that 6 proteins were differentially expressed in the high-dose group. Two stressresponsive proteins, ie heat shock cognate 71 kDa protein (HSC70) and peroxiredoxin-6 (PRDX6), were regulated at the expression level. The remaining 4 proteins involving in cellular energy metabolism, including isoforms of methylmalonyl-coenzyme A mutase (MUT), nucleoside diphosphate-linked moiety X motif 19 (Nudix motif19), mitochondrial NADH dehydrogenase 1 alpha subcomplex subunit 10 (NDUFA10) and nucleoside diphosphate kinase B (NDK B), were modified at the post-translational levels. Conclusion: Our findings suggest that the mitochondrion is the primary target of ASB and that ASB-induced nephrotoxicity results from oxidative stress mediated by superoxide produced by complex I.

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“…Protein samples were prepared essentially as described in Lee et al [8] reports. The cultured cells were harvested with 2-DE lysis buffer containing 8 M Urea, 2 M thiourea, 100 mM DTT, 4% CHAPS and 1 × complete protease inhibitor cocktail (Roche Applied Science, Germany).…”

Section: Cell Culture Differentiation In Vitro and Sample Preparationmentioning

confidence: 99%

“…[8] Briefly, the protein spots were digested with trypsin and desalted with ZipTip C 18 (Millipore). The peptide samples were mixed with CHCA matrix solution and then analyzed by MALDI-TOF/TOF (AB4700, Applied Biosystems) in the reflector mode.…”

Section: -De In-gel Digestion and Mal-di-tof/tof Msmentioning

confidence: 99%

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Analysis of proteomic profiling of mouse embryonic stem cells derived from fertilized, parthenogenetic and androgenetic blastocysts

Cui¹,

Shen²,

Lee³

et al. 2011

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Embryonic stem cells (ESCs) are derived from the inner cell mass (ICM) of preimplantation embryos. ESCs exhibit true pluripotency, i.e., the ability to differentiate into cells of all three germ layers in the developing embryo. We used 2-DE MALDI-TOF/TOF to identify differentially expressed proteins among three types of mouse embryonic stem cells (ESCs) derived from fertilized, parthenogenetic, and androgenetic (fESC, pESC and aESC, respectively) blastocysts. We detected more than 800 proteins on silverstained gels of whole protein extracts from each type of ESC. Of these, 52 differentially expressed proteins were identified by the MALDI-TOF/TOF analyzer, including 32 (fESCs vs. pESCs), 28 (fESCs vs. aESCs) and 17 (pESCs vs. aESCs) prominent proteins with significantly higher or lower expression relative to the comparison cells. Among the 32 proteins from fESCs, 12 were significantly increased in expression and 20 were reduced in expression in fESCs compared with pESCs. Similarly, 10 of 28 and 8 of 17 proteins were more highly expressed in fESCs and pESCs compared with aESCs, respectively. In contrast, 18 of 28 and 9 of 17 proteins were reduced in expression in fESCs and pESCs compared with aESCs, respectively. Of the eight protein candidates in fESCs, four were increased and four were decreased in expression relative to both pESCs and aESCs in the 2-DE analysis. Differential expression of these proteins were confirmed by mRNA expression analysis using real time RT-PCR. For three proteins, ANXA5, CLIC1 and SRM, Western blot analysis corroborated the expression patterns indicated by the 2-DE results. ANXA5 and CLIC1 were increased in expression and SRM was decreased in expression in fESCs compared with both pESCs and aESCs. The differentially expressed proteins identified in the present study warrant further investigation towards the goal of their potential application in ESC therapy.

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Analysis of peroxiredoxin decreasing oxidative stress in hypertensive aortic smooth muscle

Cited by 27 publications

References 35 publications

Monoclonal Antibody against α-Actinin 4 from Human Umbilical Vein Endothelial Cells Inhibits Endothelium-Dependent Vasorelaxation

Monoclonal Antibody against α-Actinin 4 from Human Umbilical Vein Endothelial Cells Inhibits Endothelium-Dependent Vasorelaxation

Proteomic alterations in mouse kidney induced by andrographolide sodium bisulfite

Analysis of proteomic profiling of mouse embryonic stem cells derived from fertilized, parthenogenetic and androgenetic blastocysts

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