Studies on the variability of glutathione S-transferase from human erythrocytes

Strange, Richard C.; Johnson, Peter H.; Lawton, Andrew I.; Moult, J.; Tector, Michael J.; Tyminski, Ray J.; Cotton, W G

doi:10.1016/0009-8981(82)90162-0

Cited by 32 publications

(11 citation statements)

References 12 publications

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“…Levels of GSHsynthesizing enzymes in several tissues (including human erythrocytes) and plasma 90 are higher in females than males. [91][92][93] Levels of these GSHsynthesizing enzymes can be altered by both estrogens 94,95 and testosterone. 96,97 GSH is typically reduced under conditions of enhanced oxidative stress due to the enhanced destruction of GSH in the process of neutralizing free radicals.…”

Section: Glutathionementioning

confidence: 99%

Contributions of the sympathetic nervous system, glutathione, body mass and gender to blood pressure increase with normal aging: influence of heredity

Kennedy

Rao

Botiglieri³

et al. 2005

J Hum Hypertens

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Body mass and sympathetic activity increase with aging and might underlie blood pressure (BP) elevation. Increased body mass index (BMI) may elevate BP by increasing sympathetic activity. Glutathione (GSH) can decrease BP, and declines with aging. We measured systolic (SBP) and diastolic BP, BMI, plasma (NE pl ) and urine norepinephrine (NE u ), and plasma GSH in n ¼ 204 twins across the age spectrum. BP correlated directly with BMI, NE pl , and NE u , but inversely with GSH. Age correlated with BP, BMI, NE pl , and NE u . BP, BMI, NE pl , and NE u were higher in older subjects than younger subjects, whereas GSH was lower with aging. In older subjects with high (above median) NE pl , SBP was 8 mmHg higher than in those of comparable age with low NE. In younger subjects with high GSH, BP was significantly lower than in younger subjects having low GSH. NE u was significantly reduced in young high-BMI subjects vs young low-BMI subjects. The heritability (h 2 ) of NE pl, NE u , and GSH ranged from B50 to B70%, and these biochemical quantities were considerably more heritable than BP. We conclude that increases in sympathetic activity contribute to aging-induced SBP elevations, especially in older females. GSH reductions apparently participate in aging-induced BP elevations, most strongly in males. BMI increases contribute to BP elevations, particularly in younger subjects. BMI elevations apparently raise BP mainly by peripheral mechanisms, with generally little sympathetic activation. Substantial h 2 for plasma GSH, NE, and urine NE suggests that such traits may be useful 'intermediate phenotypes' in the search for genetic determinants of BP.

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Section: Glutathionementioning

confidence: 99%

Contributions of the sympathetic nervous system, glutathione, body mass and gender to blood pressure increase with normal aging: influence of heredity

Kennedy

Rao

Botiglieri³

et al. 2005

J Hum Hypertens

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“…Where indicated, platelets and lymphocytes were removed from blood samples by using cellulose columns, and haemoglobin was removed by using CM-Sephadex (Strange et al, 1982). Starch-gel electrophoresis Horizontal starch-gel electrophoresis was performed with 100mM-Tris/citrate electrode buffer, pH 7.50.…”

Section: Materials and Methods Preparation Oflysatesmentioning

confidence: 99%

“…Glutathione S-transferase activity and haemoglobin concentration were assayed as described previously (Strange et al, 1982).…”

Section: A Nalyticalmentioning

confidence: 99%

“…The possibility, however, that more than one form of the GST3 enzyme exists is suggested by the finding, in several human tissues, of at least two enzyme forms with the characteristically fast anodal mobilities of the erythrocyte form (Strange et al, 1983). Furthermore, recent studies have shown an extensive but unexplained variation (about 10-fold) in activity in erythrocytes from healthy individuals (Scott & Wright, 1980;Strange et al, 1982), and also in the stability of the enzyme at 520C: tj= 13.4+5.1 (S.D.) min, n = 67 (R. (Wurzinger & Mohrenweiser, 1982).…”

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confidence: 99%

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Erythrocyte glutathione S-transferase. Electrophoretic identification of two enzyme forms

Strange¹,

Hirrell²,

Kitley³

et al. 1983

Biochemical Journal

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“…Catalase activity was determined using the method of Cohen et al 15) Superoxide disumutase (SOD) was assayed by the method of McCord and Fridovich. 16) Glutathione S-transferase (GST) activity was determined by the method of Strange et al 17) Glutathione peroxidase (GPX) activity was determined using the method of Flohé et al 18) and Grx activity was determined according to the method of Mieyal et al 19) Other RBC enzymes were assayed according to methods of the International Committee for Standardization 20) with minor modifications, and all assays were carried out at 37°C in the absence of thiols (reducing agents). A unit of enzyme was defined as the amount catalyzing the conversion of 1 mmol of substrate per min under each assay conditions.…”

Section: Methodsmentioning

confidence: 99%

Pyruvate Kinase Is Protected by Glutathione-Dependent Redox Balance in Human Red Blood Cells Exposed to Reactive Oxygen Species

Ogasawara

Funakoshi

Ishii

2008

Biological & Pharmaceutical Bulletin

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To determine the antioxidant role of glutathione (GSH) in human red blood cells (RBCs), we investigated the effect of disrupting GSH homeostasis on the oxidative modification of thiol-dependent enzymes by exposure to tert-butyl hydroperoxide (BHP). When hemolysate was incubated with BHP, significant decreases in enzyme activity were observed. However, the inactivation did not occur in intact RBC suspensions that were exposed to BHP. In this study, we used two independent treatments aimed at decreasing the level of reduced form of GSH, pre-incubation with a glutathione reductase inhibitor or glucose-free medium to examine the influences of preventing GSH-dependent antioxidant and reactivation activity on thiol-dependent enzyme. Pyruvate kinase (PK) activity clearly decreased along with depletion of GSH compared to other glycolytic enzyme activities by BHP exposure in RBCs. The addition of GSH, but not glucose, before BHP exposure completely prevented the inactivation of PK in hemolysate; however, partial reactivation of inactivated PK was observed by post-addition of both GSH and glutaredoxin at an early stage during BHP exposure. Moreover, hydroxyl radicals but not hydrogen peroxide inactivated PK. These results suggest that PK is highly susceptible to radicals and that GSH is essential to protect PK activity by not only directly scavenging radicals but also by systematically reactivating oxidized enzyme in human RBCs.

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Studies on the variability of glutathione S-transferase from human erythrocytes

Cited by 32 publications

References 12 publications

Contributions of the sympathetic nervous system, glutathione, body mass and gender to blood pressure increase with normal aging: influence of heredity

Contributions of the sympathetic nervous system, glutathione, body mass and gender to blood pressure increase with normal aging: influence of heredity

Erythrocyte glutathione S-transferase. Electrophoretic identification of two enzyme forms

Pyruvate Kinase Is Protected by Glutathione-Dependent Redox Balance in Human Red Blood Cells Exposed to Reactive Oxygen Species

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