The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins

Jacob, Harry S.; Winterhalter, Kaspar H.

doi:10.1172/jci106421

Cited by 72 publications

(26 citation statements)

References 34 publications

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“…With the loss of heme from the P-chain imposing a strain on the aP-dimer interface and consequently distorting the a-chain, this tendency will be increased. Evidence for this is the stabilization of Hb K6ln and heme depleted Hb A (a2hemep2o) by carbon monoxide and cyanide (19), both of which must react with the a-chain hemes.…”

Section: -Chainsmentioning

confidence: 99%

Studies of Hemoglobin Denaturation and Heinz Body Formation in the Unstable Hemoglobins

Winterbourn¹,

Carrell²

1974

J. Clin. Invest.

111

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Section: -Chainsmentioning

confidence: 99%

Studies of Hemoglobin Denaturation and Heinz Body Formation in the Unstable Hemoglobins

Winterbourn¹,

Carrell²

1974

J. Clin. Invest.

111

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“…Intracellular denaturation of Hb can cause significant changes in the erythrocyte membrane. For example, in Heinz body hemolytic anemia denatured hemoglobin precipitates to form insoluble hemichromes that bind to the inner surface of erythrocytes (Jacob and Winterhalter, 1970;Rachmilewitz, 1969;Rachmilewitz, 1974;Rifkind et al, 1994;Schneider et al, 1972;Winterbourn and Carrell, 1974). The consequent release of reactive oxygen intermediates increases membrane permeability and induces premature hemolysis (Hebbel, 1990).…”

Section: Introductionmentioning

confidence: 99%

Band 3 modifications inPlasmodium falciparum-infected AA and CC erythrocytes assayed by autocorrelation analysis using quantum dots

Tokumasu

Fairhurst

Ostera

et al. 2005

Journal of Cell Science

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The molecular stability of hemoglobin is critical for normal erythrocyte functions, including oxygen transport. Hemoglobin C (HbC) is a mutant hemoglobin that has increased oxidative susceptibility due to an amino acid substitution (β6: Glu to Lys). The growth of Plasmodium falciparum is abnormal in homozygous CC erythrocytes in vitro, and CC individuals show innate protection against severe P. falciparum malaria. We investigated one possible mechanism of innate protection using a quantum dot technique to compare the distribution of host membrane band 3 molecules in genotypically normal (AA) to CC erythrocytes. The high photostability of quantum dots facilitated the construction of 3D cell images and the quantification of fluorescent signal intensity. Power spectra and 1D autocorrelation analyses showed band 3 clusters on the surface of infected AA and CC erythrocytes. These clusters became larger as the parasites matured and were more abundant in CC erythrocytes. Further, average cluster size (500 nm) in uninfected (native) CC erythrocytes was comparable with that of parasitized AA erythrocytes but was significantly larger (1 μm) in parasitized CC erythrocytes. Increased band 3 clustering may enhance recognition sites for autoantibodies, which could contribute to the protective effect of hemoglobin C against malaria.

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“…INTRODUCTION Heme loss occurs spontaneously from certain abnormal hemoglobins (1-3) and can be induced by oxidation of the sulffiydryl groups of normal hemoglobin (3,4). After heme loss, Heinz bodies precipitate (1)(2)(3), and the affected erythrocytes exhibit abnormal cation flux (3) and reduced deformability (5). The possibility that Heinz bodies may cause hemolysis has been studied extensively (6,7).…”

mentioning

confidence: 99%

Mechanism of hemolysis induced by ferriprotoporphyrin IX.

Chou¹,

Fitch²

1981

J. Clin. Invest.

171

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A B S T R A C T Incubation of a 0.5% suspension of washed, normal mouse erythrocytes with ferriprotoporphyrin IX (FP) at 37°C and pH 7.4 caused potassium loss, swelling, increased susceptibility to hypotonic lysis, and finally hemolysis. Hemolysis was not inhibited by incubation in the dark, malonyldialdehyde was not produced, and various free radical scavengers had no effect on the hemolysis. Only the sulfhydryl compounds, cysteine, dithiothreitol, and mercaptoethanol protected erythrocytes from FP. Potassium loss reached 90% within 30 min of exposure to 5 uM FP. This amount of FP caused >50% hemolysis within 2.5 h. Sucrose (0.1 M) completely prevented hemolysis but had no effect on potassium loss. Likewise, reducing the temperature from 37 to 25°C greatly retarded hemolysis but had no effect on potassium loss. These observations indicate that FP impairs the erythrocyte's ability to maintain cation gradients and induces hemolysis by a colloid-osmotic mechanism.

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The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins

Cited by 72 publications

References 34 publications

Studies of Hemoglobin Denaturation and Heinz Body Formation in the Unstable Hemoglobins

Studies of Hemoglobin Denaturation and Heinz Body Formation in the Unstable Hemoglobins

Band 3 modifications inPlasmodium falciparum-infected AA and CC erythrocytes assayed by autocorrelation analysis using quantum dots

Mechanism of hemolysis induced by ferriprotoporphyrin IX.

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