“Acquired” red cell enzyme defects in hematological diseases

Arnold, H.; Blume, K. G.; Löhr, G. W.; Boulard, Mathieu; Najean, Y

doi:10.1016/0009-8981(74)90429-x

Cited by 34 publications

(15 citation statements)

References 10 publications

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“…Although it is possible that such a mutation was present and was missed for technical reasons, it is more likely that some of these mutations represent substitutions in the promoter region or in splice sites. For patient 4, it is possible that the PK deficiency was not actually hereditary but rather was acquired (15)(16)(17); in this case, no mutation would be expected.…”

mentioning

confidence: 99%

Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.

Baronciani

Beutler

1993

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

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confidence: 99%

Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.

Baronciani

Beutler

1993

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

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“…The early observations of Canellakis and Tarver (15) are particularly pertinent in that the CH3S group of methionine became bound to enzyme proteins and could be liberated by reducing agents. Acquired enzyme deficiencies represent a relatively common anomaly of RBC in malignant disorders and in dyserythropoietic syndromes (16)(17)(18)(19), the commonest of which is a substantial, though partial, deficiency of pyruvate kinase (16 (20,21). These include xanthine oxidase (22), aldehyde oxidase (23), cytochrome c reduction by GSH (nonenzymatic) (24), succinic dehydrogenase (25), malic dehydrogenase (26), nitrate reductase (27), ferredoxin (28), and adrenodoxin (29).…”

Section: Resultsmentioning

confidence: 99%

Modification of erythrocyte enzyme activities by persulfides and methanethiol: possible regulatory role.

Valentine¹,

Toohey²,

Paglia³

et al. 1987

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

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Sulfhydryl modification of 22 human erythrocyte enzymes was achieved by exposing intact erythrocytes, hemolysates, and partially purified enzymes to (i) persulfides (RSSH) generated nonenzymatically from cystine in the presence of pyridoxal phosphate and (ii) mercaptopyruvate, which donates its sulfur to suitable acceptors with the mediation of the carrier enzyme, mercaptopyruvate sulfurtransferase (EC 2.8.1.2). The inhibition pattern was qualitatively similar for persulfides and that previously reported by us for the methylthio-group donor, methyl methanethiosulfonate. Thirteen activities were inhibited, and 9 were minimally or not at all affected. Pyruvate kinase was similarly modified by all systems in terms of phosphoenolpyruvate kinetics, thermostability, and interaction with the negative effector ATP. Partial-to-complete reversal of inhibition was documented in a subset of activities inhibited by mercaptopyruvate upon 30-min incubation with 1 mM dithiothreitol. A possible physiologic role for methylthio groups and for persulfides is discussed.In previous studies (1, 2) we have reported the effects of methyl methanethiosulfonate, CH3SO2SCH3, a CH3S donor developed by Smith et al. (3), on certain erythrocyte enzymes. CH3SO2SCH3 is one of a family of alkyl alkanethiosulfonates and delivers its CH3S group under mild conditions to accessible cysteinyl residues of enzyme proteins. It readily traverses the erythrocyte (RBC) membrane and produces profound alterations in certain enzyme properties, including catalytic activity and thermostability (1, 2).Persulfides are intermediates in sulfur compound transformations in which -SH is bonded to another sulfur atom to form RSSH. Accumulating evidence of a potential physiological role for persulfide sulfur in biological systems (partially reviewed in ref 4) prompted the present study comparing persuffide effects with those of CH3SO2SCH3 on RBC enzymes. Since low molecular weight persulfides are unstable near pH 7, it was necessary to use incubation systems in which persulfide was continuously generated. The first of these was initially described by Cavallini et al. (5), who showed that pyridoxal with a metal causes the P-elimination reaction of cystine, with the nonenzymatic formation of cysteine persulfide, ammonia, and pyruvate. The second incubation system utilized mercaptopyruvate as the sulfur donor (4). This sulfhydryl compound is the substrate for sulfurtransferase (EC 2.8.1.2) (6), which accepts, transports, and transfers its sulfur to form persulfides with suitable acceptors. This enzyme is present in human RBC (7). METHODS RBC and Hemolysates. Blood treated with the anticoagulant heparin was washed and freed of leukocytes by passage with saline over a column of microcellulose (8). After washing, centrifugation, and resuspension in saline, the RBC were adjusted to =4-4.5 x 106 per A.l. Where indicated, cells were lysed as described in text.Partially Purified Lysates. Hemolysates were largely freed of Hb precipitated by ZnSO4 at pH 8.0 in 0.1 M Tris HCl ...

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“…In some cases of dyserythropoiesis including MDS, decreased enzyme activity of pyruvate kinase with a concomitant increase in other enzyme activities and increase in red blood cell GSH, which were not related to reticulocytosis have been documented [3,4].…”

Section: Discussionmentioning

confidence: 99%

“…Some enzymatic and biochemical investigations in dyserythropoiesis have been reported recently. Enzyme deficiencies of glycolytic enzymes including pyruvate kinase, changes in antigen (A, B, H, and I), and increased hemoglobin F levels have been observed in the peripheral red blood cells of patients with dyserythropoiesis [2][3][4].…”

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confidence: 99%

Role of Free Radical Reactions in Myelodysplastic Syndrome

Imanishi

Misawa

Takino

et al. 1988

J. Clin. Biochem. Nutr.

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SummaryActivities of glutathione linked enzymes in red blood cells and concentrations of other free radical scavengers in red blood cells and in plasma were assayed in patients with myelodysplastic syndromes (MDS). Glutathione peroxidase (GSH-Px) activity, concentrations of both reduced glutathione and oxidized glutathione in red blood cells, and lipid peroxide levels in plasma were all significantly increased in MDS patients. Levels of other free radical scavengers in plasma (total vitamin B2, FAD, and coenzyme Q10), however, were decreased. The data suggest that MDS patients may have been exposed to free radicals, and may be hypersensitive to the oxygen intoxication.

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“Acquired” red cell enzyme defects in hematological diseases

Cited by 34 publications

References 10 publications

Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.

Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.

Modification of erythrocyte enzyme activities by persulfides and methanethiol: possible regulatory role.

Role of Free Radical Reactions in Myelodysplastic Syndrome

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