Association of hemoglobin C with erythrocyte ghosts.

Reiss, Gwen H.; Ranney, Helen M.; Shaklai, Nurith

doi:10.1172/jci110706

Cited by 34 publications

(26 citation statements)

References 19 publications

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“…Increasing the amount of HbF decreases the amount of degradation product present, which may be due either to reduction of polymer formation by γ, or to stabilization of β S in the heterotetramer (α H 2 β S γ). Both HbS [24] and HbC [25] have an excess positive charge relative to HbA and have been shown to preferentially bind to Band 3. The presence of γ or α mouse in heterotetramers may reduce the amount of membrane-associated, unstable β-chains.…”

Section: Discussion Fluorescence In Pathological Rbcmentioning

confidence: 99%

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Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease

Nagababu

Fabry

Nagel

et al. 2008

Blood Cells, Molecules, and Diseases

103

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Red blood cells with abnormal hemoglobins (Hb) are frequently associated with increased hemoglobin autoxidation, accumulation of iron in membranes, increased membrane damage and a shorter red cell life span. The mechanisms for many of these changes have not been elucidated. We have shown in our previous studies that hydrogen peroxide formed in association with hemoglobin autoxidation reacts with hemoglobin and initiates a cascade of reactions that results in heme degradation with the formation of two fluorescent emission bands and the release of iron. Heme degradation was assessed by measuring the fluorescent band at ex 321 nm. A 5.6 fold increase in fluorescence was found in red cells from sickle transgenic mice that expressed exclusively human globins when compared to red cells from control mice. When sickle transgenic mice co-express the γM transgene, that expresses HbF and inhibits polymerization, heme degradation is decreased. Mice expressing exclusively hemoglobin C had a 6.9 fold increase in fluorescence compared to control. Heme degradation was also increased 3.5 fold in β-thalassemic mice generated by deletion of murine β major . Membrane bound IgG and red cell metHb were highly correlated with the intensity of the fluorescent heme degradation band. These results suggest that degradation of the heme moiety in intact hemoglobin and/or degradation of free heme by peroxides are higher in pathological RBCs. Concomitant release of iron appears to be responsible for the membrane damage that leads to IgG binding and the removal of red cells from circulation.

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Section: Discussion Fluorescence In Pathological Rbcmentioning

confidence: 99%

“…HbS and HbC have a higher affinity for band 3 than HbA [24,25]. Hydrogen peroxide generated by autoxidation of membrane associated Hb may be relatively inaccessible to catalase and generate more heme degradation products [29].…”

Section: Membrane Damage Associated With In Vivo Heme Degradationmentioning

confidence: 99%

Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease

Nagababu

Fabry

Nagel

et al. 2008

Blood Cells, Molecules, and Diseases

103

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“…10 There is evidence that this dehydration is due to an interaction between the HbC and KCC molecules present in the red cell membrane, although the exact mechanism is unknown. 9 HbC is known to bind to the cytoplasmic region of band 3, 11 although it is unclear how this leads to erythrocyte dehydration. 12 KCC activation has been established to be central to the pathophysiology of HbSC disease, with many experiments demonstrating its importance in vitro.…”

Section: Introductionmentioning

confidence: 99%

The clinical significance of K-Cl cotransport activity in red cells of patients with HbSC disease

et al. 2015

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“…Based on the effect of ionic strength on binding, it was proposed that the excess of HbS and C was due to the increasing positive charge in the series A Ͻ S Ͻ C. 15,16 In 1973, Steck 17 demonstrated that the reversible binding of both HbA and HbS was competitive with that of glyceraldehyde-3-phosphate dehydrogenase (GAPD), an enzyme that binds to the N-terminal of the anion exchanger (AE1 or band 3), and that HbS can displace HbA. Reiss et al 18 demonstrated that HbC also competes with GAPD when it binds to inside-out vesicles (IOVs) and that the same amount of GAPD can displace more HbA than HbC. These observations are consistent with known negative charge on the N-terminal of AE1 that has been shown to bind in the central cavity of hemoglobin.…”

Section: Introductionmentioning

confidence: 99%

Expression of HbC and HbS, but not HbA, results in activation of K-Cl cotransport activity in transgenic mouse red cells

Romero

Suzuka

Nagel

et al. 2004

Blood

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Association of hemoglobin C with erythrocyte ghosts.

Cited by 34 publications

References 19 publications

Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease

Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease

The clinical significance of K-Cl cotransport activity in red cells of patients with HbSC disease

Expression of HbC and HbS, but not HbA, results in activation of K-Cl cotransport activity in transgenic mouse red cells

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