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  1 / 1952 MEDLINE  
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PMID:27777179
Autor:Colombo G; Clerici M; Altomare A; Rusconi F; Giustarini D; Portinaro N; Garavaglia ML; Rossi R; Dalle-Donne I; Milzani A
Endereço:Department of Biosciences, Università degli Studi di Milano, Milan, Italy. Electronic address: graziano.colombo@unimi.it.
Título:Thiol oxidation and di-tyrosine formation in human plasma proteins induced by inflammatory concentrations of hypochlorous acid.
Fonte:J Proteomics; 152:22-32, 2017 01 30.
ISSN:1876-7737
País de publicação:Netherlands
Idioma:eng
Resumo:In this study, we assessed the oxidative damage occurring in plasma proteins when human blood was exposed to inflammatory concentrations of hypochlorous acid (HOCl). We used specific thiol labelling and Western blot analyses to determine protein thiol oxidation, as well as analytical gel filtration HPLC coupled to fluorescence detection to explore formation of high molecular weight (HMW) protein aggregates. Thiol-containing proteins oxidized by HOCl were identified by redox proteomics. Mass spectrometry (MS) analysis was performed to elucidate the protein composition of HMW aggregates. α1-antitrypsin, transthyretin, and haptoglobin showed thiol oxidation at HOCl concentrations higher than those causing complete oxidation of albumin. At the highest HOCl concentrations, formation of carbonylated and di-tyrosine cross-linked HMW protein aggregates also occurred. MS analysis identified fibrinogen, complement C3 and apolipoprotein A-I as components of HMW protein aggregates. These results could be relevant for human diseases characterized by inflammatory conditions in which myeloperoxidase and HOCl are involved. BIOLOGICAL SIGNIFICANCE: In this study we evaluated the oxidative damage occurring on plasma proteins when reconstituted human blood was exposed to inflammatory concentrations of hypochlorous acid (HOCl). Pathophysiological concentrations of HOCl are able to induce different modifications on plasma proteins such as carbonylation, sulfhydryl oxidation and formation of high molecular weight (HMW) protein aggregates characterized by di-tyrosine fluorescence. There are two relevant aspects emerging from this paper. The first one consists on identifying low abundant proteins undergoing sulfhydryl oxidation by biotin-maleimide derivatization followed by MALDI-TOF mass spectrometry. This approach suggests three low-abundant proteins undergoing HOCl-induced oxidation: transthyretin, α1-antitrypsin, and haptoglobin. In addition, we analysed HMW protein aggregates forming after HOCl exposure. These aggregates are characterized by carbonylation, intra- and/or intermolecular di-tyrosine bridges. After their isolation from SDS-PAGE gel electrophoresis, using electrospray tandem mass spectrometry coupled to reversed-phase nanoscale capillary liquid chromatography, we identified some protein constituents of these HMW aggregates such as α, ß, γ fibrinogen chains, apolipoprotein A-I and complement C3. In particular, our work highlights how fibrinogen is an important constituent of HOCl-induced HMW protein aggregates validating the mass spectrometry result with additional experiments. Further investigations are required in order to evaluate the possibility to use carbonylated and di-Tyr cross-linked HMW protein aggregates as (early) biomarkers for disease progression in inflammatory conditions in which myeloperoxidase and HOCl are involved.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (APOA1 protein, human); 0 (Apolipoprotein A-I); 0 (Biomarkers); 0 (Blood Proteins); 0 (Complement C3); 0 (Protein Aggregates); 0 (Sulfhydryl Compounds); 42HK56048U (Tyrosine); 712K4CDC10 (Hypochlorous Acid); 9001-32-5 (Fibrinogen); EC 1.11.1.7 (Peroxidase)


  2 / 1952 MEDLINE  
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PMID:28645608
Autor:Ge L; Zhang G; You B; Cheng G; Chen L; Shi R
Endereço:Department of Cardiovascular Medicine, Xiangya Hospital, Central South University, Changsha 410008, China; Department of Cardiovascular Medicine, The First People's Hospital of Changde City, Changde 415000, Hunan, China.
Título:The role of losartan in preventing vascular remodeling in spontaneously hypertensive rats by inhibition of the H O /VPO1/HOCl/MMPs pathway.
Fonte:Biochem Biophys Res Commun; 493(1):855-861, 2017 Nov 04.
ISSN:1090-2104
País de publicação:United States
Idioma:eng
Resumo:Vascular peroxidase 1 (VPO1) has been proved to be associated with vascular endothelial cell apoptosis by producing reactive oxygen species. However, the contribution of VPO1 to the development of vascular remodeling (VR) remains to be fully characterized. We explored the role of VPO1 in VR in spontaneously hypertensive rats (SHRs) and the underlying mechanism of losartan in inhibiting VR. Compared to Wistar-Kyoto (WKY) rats, the SHR showed remodeling of their vascular walls. The level of VPO1 and the hydrogen peroxide (H O ) concentration were increased in the SHRs. However, the SHRs pretreated with losartan showed significant inhibition of blood pressure and VR and decreased levels of VPO1 and H O compared to the non-treated SHRs. Angiotensin II significantly increased the expressions of MMP-2, MMP-9 and the concentrations of H O and hypochlorous acid (HOCl) in vascular smooth muscle cells (VSMCs). However, only the H O level increased in VSMCs when transfected with VPO1 shRNA. These results support a critical but previously unrecognized role of VPO1 in VR and suggest that therapies to reduce VPO1 may be novel approaches for VR.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Antihypertensive Agents); 712K4CDC10 (Hypochlorous Acid); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (Peroxidases); EC 1.11.1.- (VPO1 protein, human); EC 3.4.24.- (Matrix Metalloproteinases); JMS50MPO89 (Losartan)


  3 / 1952 MEDLINE  
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PMID:28628976
Autor:Chong GG; He YC; Liu QX; Kou XQ; Huang XJ; Di JH; Ma CL
Endereço:Advanced Catalysis and Green Manufacturing Collaborative Innovation Center, Jiangsu Key Laboratory of Advanced Catalytic Materials and Technology, Changzhou University, Changzhou, China.
Título:Effective enzymatic in situ saccharification of bamboo shoot shell pretreated by dilute alkalic salts sodium hypochlorite/sodium sulfide pretreatment under the autoclave system.
Fonte:Bioresour Technol; 241:726-734, 2017 Oct.
ISSN:1873-2976
País de publicação:England
Idioma:eng
Resumo:In this study, dilute alkali salts (0.6% NaClO, 0.067% Na S) pretreatment at 10% sulfidity under the autoclave system at 120°C for 40min was used for pretreating bamboo shoot shell (BSS). Furthermore, FT-IR, XRD and SEM were employed to characterize the changes in the cellulose structural characteristics (porosity, morphology, and crystallinity) of the pretreated BSS solid residue. After 72h, the reducing sugars and glucose from the enzymatic in situ hydrolysis of 50g/L pretreated BSS in dilute NaClO/Na S media could be obtained at 31.11 and 20.32g/L, respectively. Finally, the obtained BSS-hydrolysates containing alkalic salt NaClO/Na S resulted in slightly negative effects on the ethanol production. Glucose in BSS-hydrolysates was fermented from 20.0 to 0.17g/L within 48h, and an ethanol yield of 0.41g/g glucose, which represents 80.1% of the theoretical yield, was obtained. This study provided an effective strategy for potential utilization of BSS.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Sulfides); 3K9958V90M (Ethanol); 712K4CDC10 (Hypochlorous Acid); DY38VHM5OD (Sodium Hypochlorite); EC 3.2.1.4 (Cellulase); YGR27ZW0Y7 (sodium sulfide)


  4 / 1952 MEDLINE  
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PMID:28604692
Autor:Kellner S; DeMott MS; Cheng CP; Russell BS; Cao B; You D; Dedon PC
Endereço:Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Título:Oxidation of phosphorothioate DNA modifications leads to lethal genomic instability.
Fonte:Nat Chem Biol; 13(8):888-894, 2017 Aug.
ISSN:1552-4469
País de publicação:United States
Idioma:eng
Resumo:Genomic modification by sulfur in the form of phosphorothioate (PT) is widespread among prokaryotes, including human pathogens. Apart from its physiological functions, PT sulfur has redox and nucleophilic properties that suggest effects on bacterial fitness in stressful environments. Here we show that PTs are dynamic and labile DNA modifications that cause genomic instability during oxidative stress. In experiments involving isotopic labeling coupled with mass spectrometry, we observed sulfur replacement in PTs at a rate of ∼2% h in unstressed Escherichia coli and Salmonella enterica. Whereas PT levels were unaffected by exposure to hydrogen peroxide (H O ) or hypochlorous acid (HOCl), PT turnover increased to 3.8-10% h after HOCl treatment and was unchanged by H O , consistent with the repair of HOCl-induced sulfur damage. PT-dependent sensitivity to HOCl extended to cytotoxicity and DNA strand breaks, which occurred at HOCl doses that were orders of magnitude lower than the corresponding doses of H O . The genotoxicity of HOCl in PT-containing bacteria suggests reduced fitness in competition with HOCl-producing organisms and during infections in humans.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Phosphorothioate Oligonucleotides); 712K4CDC10 (Hypochlorous Acid); 9007-49-2 (DNA); BBX060AN9V (Hydrogen Peroxide)


  5 / 1952 MEDLINE  
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PMID:28544986
Autor:Kuznetsova T; Kulahava T; Zholnerevich I; Amaegberi N; Semenkova G; Shadyro O; Arnhold J
Endereço:N.I. Pirogov Russian National Research Medical University, Moscow, Russian Federation. Electronic address: tatkuznetsova@list.ru.
Título:Morphometric characteristics of neutrophils stimulated by adhesion and hypochlorite.
Fonte:Mol Immunol; 87:317-324, 2017 Jul.
ISSN:1872-9142
País de publicação:England
Idioma:eng
Resumo:The aim of this work was to compare cell form, size and volume as well as the locomotor activity of polymorphonuclear leukocytes (PMNLs) stimulated by adhesion to glass and exposed to hypochlorous acid at non-toxic dose. After 20min of adhesion to a glass surface, volume, cell surface area and projection area of PMNLs were equaled to 143.1±21.4µm , 288.8±28.8µm and 248.3±32.3µm , respectively. Projection area of PMNLs exposed to NaOCl was noticeably enlarged as compared with control samples. The cell volume of 20min adherent cells exposed to NaOCl was enlarged in comparison with both control cells and 5min adhered exposed to NaOCl cells. NaOCl exposure induced a degranulation of PMNLs as measured by lysozyme release. Granules could be found both above the cell surface and on the substratum near the cell. The S/V ratio for PMNLs increased (from 1.52 to 2.02µm ) with the increasing of cell activation time. But at NaOCl addition the reverse tendency was observed (from 2.10 to 1.87µm ). In cells exposed to NaOCl the redistribution and decrease of concentration of F-actin took place. This observation supports the hypothesis that the priming of PMNLs with hypochlorous acid modifies cell motility and morphology and reflects also on other functions.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Actins); 712K4CDC10 (Hypochlorous Acid); EC 3.2.1.17 (Muramidase)


  6 / 1952 MEDLINE  
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PMID:28361543
Autor:Tian R; Ding Y; Peng YY; Lu N
Endereço:Key Laboratory of Functional Small Organic Molecule, Ministry of Education, Key Laboratory of Green Chemistry in Jiangxi Province, and College of Chemistry and Chemical Engineering, Jiangxi Normal University , Nanchang, China.
Título:Inhibition of Myeloperoxidase- and Neutrophil-Mediated Hypochlorous Acid Formation in Vitro and Endothelial Cell Injury by (-)-Epigallocatechin Gallate.
Fonte:J Agric Food Chem; 65(15):3198-3203, 2017 Apr 19.
ISSN:1520-5118
País de publicação:United States
Idioma:eng
Resumo:Myeloperoxidase (MPO) plays important roles in various diseases through its unique chlorinating activity to catalyze excess hypochlorous acid (HOCl) formation. Epidemiological studies indicate an inverse correlation between plant polyphenol consumption and the incidence of cardiovascular diseases. Here we showed that (-)-epigallocatechin gallate (EGCG), the main flavonoid present in green tea, dose-dependently inhibited MPO-mediated HOCl formation in vitro (chlorinating activities of MPO: 50.2 ± 5.7% for 20 µM EGCG versus 100 ± 5.6% for control, P < 0.01). UV-vis spectral and docking studies indicated that EGCG bound to the active site (heme) of MPO and resulted in the accumulation of compound II, which was unable to produce HOCl. This flavonoid also effectively inhibited HOCl generation in activated neutrophils (HOCl formation: 65.0 ± 5.6% for 20 µM EGCG versus 100 ± 6.2% for control, P < 0.01) without influencing MPO and Nox2 release and superoxide formation, suggesting that EGCG specifically inhibited MPO but not NADPH oxidase activity in activated neutrophils. Moreover, EGCG inhibited MPO (or neutrophil)-mediated HOCl formation in human umbilical vein endothelial cells (HUVEC) culture and accordingly protected HUVEC from MPO (or neutrophil)-induced injury (P < 0.05, all cases), although it did not induce cytotoxicity to HUVEC (P > 0.05, all cases). Our results indicate that dietary EGCG is an effective and specific inhibitor of MPO activity and may participate in the regulation of immune responses at inflammatory sites.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:712K4CDC10 (Hypochlorous Acid); 8R1V1STN48 (Catechin); BQM438CTEL (epigallocatechin gallate); EC 1.11.1.7 (Peroxidase)


  7 / 1952 MEDLINE  
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PMID:28351015
Autor:Zhang W; Zhou Z; An Y; Du S; Ruan D; Zhao C; Ren N; Tian X
Endereço:College of Environmental and Chemical Engineering, Shanghai University of Electric Power, 2588 Changyang Road, Shanghai 200090, China.
Título:Optimization for zeolite regeneration and nitrogen removal performance of a hypochlorite-chloride regenerant.
Fonte:Chemosphere; 178:565-572, 2017 Jul.
ISSN:1879-1298
País de publicação:England
Idioma:eng
Resumo:Simultaneous zeolites regeneration and nitrogen removal were investigated by using a mixed solution of NaClO and NaCl (NaClO-NaCl solution), and effects of the regenerant on ammonium removal performance and textural properties of zeolites were analyzed by long-term adsorption and regeneration operations. Mixed NaClO-NaCl solution removed more NH exchanged on zeolites and converted more of them to nitrogen than using NaClO or NaCl solution alone. Response surface methodological analysis indicated that molar ratio of hypochlorite and nitrogen (ClO /N), NaCl concentration and pH value all had significant effects on zeolites regeneration and NH conversion to nitrogen, and the optimum condition was obtained at ClO /N of 1.75, NaCl concentration of 20 g/L and pH of 10.0. Zeolites regenerated by mixed NaClO-NaCl solution showed higher ammonium adsorption rate and lower capacity than unused zeolites. Zeolites and the regeneration solution were both effective even after 20 cycles of use. Composition and morphological analysis revealed that the main mineral species and surface morphology of zeolites before and after NaClO-NaCl regeneration were unchanged. Textural analysis indicated that NaClO-NaCl regeneration leads to an increased surface area of zeolites, especially the microporosity. The results indicated that NaClO-NaCl regeneration is an attractive method to achieve sustainable removal of nitrogen from wastewater through zeolite.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Ammonium Compounds); 1318-02-1 (Zeolites); 451W47IQ8X (Sodium Chloride); 712K4CDC10 (Hypochlorous Acid); N762921K75 (Nitrogen)


  8 / 1952 MEDLINE  
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PMID:28322835
Autor:Zhao H; Liu YJ; Liu ZR; Tang DD; Chen XW; Chen YH; Zhou RN; Chen SQ; Niu HX
Endereço:Division of Nephrology, Zhujiang Hospital, Southern Medical University, Guangzhou 510282, China.
Título:Role of mitochondrial dysfunction in renal fibrosis promoted by hypochlorite-modified albumin in a remnant kidney model and protective effects of antioxidant peptide SS-31.
Fonte:Eur J Pharmacol; 804:57-67, 2017 Jun 05.
ISSN:1879-0712
País de publicação:Netherlands
Idioma:eng
Resumo:Oxidative stress aggravates renal fibrosis, a pathway involved in almost all forms of chronic kidney disease (CKD). However, the underlying mechanism involved in the pathogenesis of renal oxidative stress has not been completely elucidated. In this study, we explored the role and mechanism of hypochlorite-modified albumin (HOCl-alb) in mediating oxidative stress and fibrotic response in a remnant-kidney rat model. Five-sixths nephrectomy (5/6 NX) was performed on the rats and then the animals were randomly assigned to intravenous treatment with either vehicle alone, or HOCl-rat serum albumin (RSA) in the presence or absence of SS-31 (administered intraperitoneally). A sham-operation control group was set up concurrently. Compared with the control group, 5/6 NX animals displayed marked mitochondrial (mt) dysfunction, as evidenced by decrease of mitochondrial membrane potential (MMP), ATP production, mtDNA copy number alterations and manganese superoxide dismutase (MnSOD) activity, release of cytochrome C (Cyto C) from mitochondria to the cytoplasm, and increase of mitochondrial reactive oxygen species in renal tissues. They also displayed increased levels of HOCl-alb in both plasma and renal tissues. These changes were accompanied by accumulation of extracellular matrix, worsened proteinuria, deteriorated renal function, and a marked increase of macrophage infiltration along with up-regulation of monocyte chemoattractant protein (MCP)-1 and transforming growth factor (TGF)-ß1 expression. HOCl-alb challenge further exacerbated the above biological effects in 5/6 NX animals, but these adverse effects were prevented by administration of SS-31, a mitochondrial targeted antioxidant peptide. These data suggest that accumulation of HOCl-alb may promote renal inflammation and fibrosis, probably related to mitochondrial oxidative stress and dysfunction and that the mitochondrial targeted peptide SS-31 might be a novel therapy for renal fibrosis and chronic renal failure (CRF).
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Antioxidants); 0 (Biomarkers); 0 (Oligopeptides); 0 (Serum Albumin); 0 (arginyl-2,'6'-dimethyltyrosyl-lysyl-phenylalaninamide); 712K4CDC10 (Hypochlorous Acid)


  9 / 1952 MEDLINE  
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PMID:28301615
Autor:Totoraitis K; Cohen JL; Friedman A
Título:Topical Approaches to Improve Surgical Outcomes and Wound Healing: A Review of Efficacy and Safety.
Fonte:J Drugs Dermatol; 16(3):209-212, 2017 Mar 01.
ISSN:1545-9616
País de publicação:United States
Idioma:eng
Resumo:

Surgical procedures are an important piece of a dermatologist's daily practice. Therefore, the optimization of post-surgical wound healing is an area of utmost importance and interest. Although low risk, one notable barrier to proper wound healing is surgical site infection.

In an attempt to mitigate this risk and improve surgical outcomes, multiple topical products continue to be used both pre- and postprocedure. Traditionally, this includes both topical antibiotics and antiseptics. However, these products are not without consequence.

The overuse of topical antibiotics as prophylaxis for infection has contributed to increased bacterial resistance, and in fact is no longer recommended by the American Academy of Dermatology in clean post surgical wounds. Topical antiseptics, including chlorhexidine and povidone-iodine, can have a cytotoxic effect on keratinocytes and may actually impede wound healing as a result. In addition, chlorhexidine in particular can produce both otologic and ocular toxic effects when used on the face. Emerging products, such as hypochlorous acid, may be a potential alternative to the more commonly used agents, as it has effective antimicrobial actions and minimal adverse effects. Therefore, the purpose of this review is to highlight several topical products used to optimize post-surgical wound healing and discuss both their efficacy and safety.

J Drugs Dermatol. 2017;16(3):209-212.

.
Tipo de publicação: JOURNAL ARTICLE; REVIEW
Nome de substância:0 (Anti-Bacterial Agents); 0 (Anti-Infective Agents, Local); 712K4CDC10 (Hypochlorous Acid); 85H0HZU99M (Povidone-Iodine); R4KO0DY52L (Chlorhexidine)


  10 / 1952 MEDLINE  
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PMID:28251264
Autor:Golovach NG; Cheshchevik VT; Lapshina EA; Ilyich TV; Zavodnik IB
Endereço:Department of Biochemistry, Yanka Kupala State University of Grodno, Blvd. Len. Kom. - 50, 230030, Grodno, Belarus.
Título:Calcium-Induced Mitochondrial Permeability Transitions: Parameters of Ca Ion Interactions with Mitochondria and Effects of Oxidative Agents.
Fonte:J Membr Biol; 250(2):225-236, 2017 Apr.
ISSN:1432-1424
País de publicação:United States
Idioma:eng
Resumo:We evaluated the parameters of Ca -induced mitochondrial permeability transition (MPT) pore formations, Ca binding constants, stoichiometry, energy of activation, and the effect of oxidative agents, tert-butyl hydroperoxide (tBHP), and hypochlorous acid (HOCl), on Ca -mediated process in rat liver mitochondria. From the Hill plot of the dependence of MPT rate on Ca concentration, we determined the order of interaction of Ca ions with the mitochondrial sites, n = 3, and the apparent K = 60 ± 12 µM. We also found the apparent Michaelis-Menten constant, K , for Ca interactions with mitochondria to be equal to 75 ± 20 µM, whereas that in the presence of 300 µM tBHP was 120 ± 20 µM. Using the Arrhenius plots of the temperature dependences of apparent mitochondrial swelling rate at various Ca concentrations, we calculated the activation energy of the MPT process. ΔE was 130 ± 20 kJ/mol at temperatures below the break point of the Arrhenius plot (30-34 °C) and 50 ± 9 kJ/mol at higher temperatures. Ca ions induced rapid mitochondrial NADH depletion and membrane depolarization. Prevention of the pore formation by cyclosporin A inhibited Ca -dependent mitochondrial depolarization and Mg ions attenuated the potential dissipation. tBHP (10-150 µM) dose-dependently enhanced the rate of MPT opening, whereas the effect of HOCl on MPT depended on the ratio of HOCl/Ca . The apparent K of tBHP interaction with mitochondria in the swelling reaction was found to be K = 11 ± 3 µM. The present study provides evidence that three calcium ions interact with mitochondrial site with high affinity during MPT. Ca -induced MPT pore formations due to mitochondrial membrane protein denaturation resulted in membrane potential dissipation. Oxidants with different mechanisms, tBHP and HOCl, reduced mitochondrial membrane potential and oxidized mitochondrial NADH in EDTA-free medium and had an effect on Ca -induced MPT onset.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Mitochondrial Membrane Transport Proteins); 0 (mitochondrial permeability transition pore); 712K4CDC10 (Hypochlorous Acid); 955VYL842B (tert-Butylhydroperoxide); SY7Q814VUP (Calcium)



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