Measuring chlorine bleach in biology and medicine

Kettle, Anthony J.; Albrett, Amelia M.; Chapman, Anna; Dickerhof, Nina; Forbes, Louisa V.; Khalilova, Irada; Turner, Rufus

doi:10.1016/j.bbagen.2013.07.004

Cited by 99 publications

(95 citation statements)

References 175 publications

(234 reference statements)

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“…In addition to tyrosine, a number of endogenous probes have been used to assess MPO activity/HOCl in vivo, including chlorinated DNA bases (39) and lipids such as chlorohydrins (39) and chlorinated plasmalogen (54). A major focus of the present study was to compare the "endogenous probe" tyrosine with exogenously added HE in conjunction with the LC/MS/MS analysis of 3-Cl-Tyr and 2-Cl-E ϩ , respectively, as surrogate measures of MPO activity.…”

Section: Discussionmentioning

confidence: 99%

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Assessment of Myeloperoxidase Activity by the Conversion of Hydroethidine to 2-Chloroethidium

Maghzal

Cergol

Shengule

et al. 2014

Journal of Biological Chemistry

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Background: Myeloperoxidase activity is commonly assessed in vivo by the accumulation of 3-chlorotyrosine. Results: Myeloperoxidase-derived chlorinating species specifically converted hydroethidine to 2-chloroethidium with efficiency superior to that of the corresponding conversion of tyrosine to 3-chlorotyrosine. Conclusion: Hydroethidine is useful to assess myeloperoxidase activity in vivo, in parallel with its simultaneous use to detect superoxide. Significance: 2-Chloroethidium is a useful additional marker of myeloperoxidase activity.

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Section: Discussionmentioning

confidence: 99%

“…3-Cl-Tyr is commonly considered the gold standard for assessing MPO/HOCl activity (25,(37)(38)(39). For this, we activated isolated human PMN and determined the conversion of added HE to 2-Cl-E ϩ in parallel with cellular levels of 3-Cl-Tyr.…”

Section: Assessment Of 2-cl-e ϩ As a Surrogate Marker For Mpo/hocl Acmentioning

confidence: 99%

Assessment of Myeloperoxidase Activity by the Conversion of Hydroethidine to 2-Chloroethidium

Maghzal

Cergol

Shengule

et al. 2014

Journal of Biological Chemistry

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“…Measurement of 3‐cholorotyrosine (3‐Cl‐tyr), a chlorination product of HOCl reaction with tyrosine, was used to compare relative levels of HOCl production 14. 3‐Cl‐tyr levels were evaluated by Western blot.…”

Section: Methodsmentioning

confidence: 99%

VPO1 Modulates Vascular Smooth Muscle Cell Phenotypic Switch by Activating Extracellular Signal‐regulated Kinase 1/2 (ERK 1/2) in Abdominal Aortic Aneurysms

Peng

Zhang

Liu

et al. 2018

JAHA

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BackgroundHydrogen peroxide (H2O2) is a critical molecular signal in the development of abdominal aortic aneurysm (AAA) formation. Vascular peroxidase 1 (VPO1) catalyzes the production of hypochlorous acid (HOCl) from H2O2 and significantly enhances oxidative stress. The switch from a contractile phenotype to a synthetic one in vascular smooth muscle cells (VSMCs) is driven by reactive oxygen species and is recognized as an early and important event in AAA formation. This study aims to determine if VPO1 plays a critical role in the development of AAA by regulating VSMC phenotypic switch.Methods and Results VPO1 is upregulated in human and elastase‐induced mouse aneurysmal tissues compared with healthy control tissues. Additionally, KLF4, a nuclear transcriptional factor, is upregulated in aneurysmatic tissues along with a concomitant downregulation of differentiated smooth muscle cell markers and an increase of synthetic phenotypic markers, indicating VSMC phenotypic switch in these diseased tissues. In cultured VSMCs from rat abdominal aorta, H2O2 treatment significantly increases VPO1 expression and HOCl levels as well as VSMC phenotypic switch. In support of these findings, depletion of VPO1 significantly attenuates the effects of H2O2 and HOCl treatment. Furthermore, HOCl treatment promotes VSMC phenotypic switch and ERK1/2 phosphorylation. Pretreatment with U0126 (a specific inhibitor of ERK1/2) significantly attenuates HOCl‐induced VSMC phenotypic switch.ConclusionsOur results demonstrate that VPO1 modulates VSMC phenotypic switch through the H2O2/VPO1/HOCl/ERK1/2 signaling pathway and plays a key role in the development of AAA. Our findings also implicate VPO1 as a novel signaling node that mediates VSMC phenotypic switch and plays a key role in the development of AAA.Clinical Trial Registration URL: http://www.chictr.org.cn. Unique identifier: ChiCTR1800016922.

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“…Chlorine oxidizes many biological molecules (Kettle et al, 2014), including EGFP expressed in E. coli (Kuruto-Niwa et al, 2002). There was no obvious decrease in fluorescence in suspensions of L. sinensis and D. magna following ingestion of E. coli-EGFP in the absence of chlorination (Fig.…”

Section: Egfp Fluorescence In E Colimentioning

confidence: 95%

Inactivation mechanism of chlorination in Escherichia coli internalized in Limnoithona sinensis and Daphnia magna

2016

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Measuring chlorine bleach in biology and medicine

Cited by 99 publications

References 175 publications

Assessment of Myeloperoxidase Activity by the Conversion of Hydroethidine to 2-Chloroethidium

Assessment of Myeloperoxidase Activity by the Conversion of Hydroethidine to 2-Chloroethidium

VPO1 Modulates Vascular Smooth Muscle Cell Phenotypic Switch by Activating Extracellular Signal‐regulated Kinase 1/2 (ERK 1/2) in Abdominal Aortic Aneurysms

Inactivation mechanism of chlorination in Escherichia coli internalized in Limnoithona sinensis and Daphnia magna

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