Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes.

Waugh, Stephen M.; Willardson, Barry M.; Kannan, Rama; Labotka, Richard; Low, Philip S.

doi:10.1172/jci112696

Cited by 104 publications

(51 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this case as pointed out by Waugh et a!. [11] no clustering of Band 3 can be expected. We used exactly the same experimental procedures for red cell separation and Heinz-body formation as were employed by Low et al [10].…”

mentioning

confidence: 51%

“…In another experiment we compared the intensity of the phenylhydrazine-induced fluorescence detected at the excitation range of rhodamine to that of the specific immunofluorescence of red cells in which an intracellular antigen spectrin was detected using rabbit antihuman spectrin and rhodamine-conjugated goat antirabbit IgG. While in recent experiments performed or~ haemoglobinopathic erythroeytes [11,12] the red cell autofluorescence was found to be negligible compared to the specific immunofluorescence, our experiment (where photography and printing of both samples were also carried out identically) showed that the intensity of phenylhydrazine-induced fluorescence is in fact comparable to that of the speci!ic immunofluorescence (data not sho,m,. ).…”

mentioning

confidence: 99%

“…The possible coloc~iz~lion of H.zinz, hodie~ and surface-bound IgG which was detectea by ,,ring fluorescein-labelled anti-human IgG [10] can only be confirmed or disproved by using morphological techniques other than fluorescence microscopy. Similarly, it is beyond the scope of this work to deal with Heinz-body-reduced clustering of Band 3 detected by fight microscopy in erythrocytes of patients with different haemoglobinopathies [11,12]. Using frc.eze-fraeture and immunocytochemical electron microscopy these questions will be studied later on.…”

mentioning

confidence: 99%

See 2 more Smart Citations

The distribution and aggregatability of intramembrane particles in phenylhydrazine-treated human erythrocytes

Lelkes

Fodor

Hollán

et al. 1988

Biochimica et Biophysica Acta (BBA) - Biomembranes

View full text Add to dashboard Cite

Freeze-fracture analysis of phenylhydrazine-treated, unfixed human erythroeytes showed a ramlom distribution of intramembran¢ particles both over membrane-bound Heinz.bodies and in the intervening areas when examined after fast freezing in liquid pr~,pane. The same results was obtained when unfixed, glyeerinated red cells were frozen in liquid Freon. In contrast to previously published data (Low et al. (1985) Science 227, 531-533) these results indicate that binding of Heinz-bodies to the red cell membrane cannot cause morphologically detectable clustering of Band 3 in phenylhydrazine-treated red cells. Over numerous Heinz-bodles a decreased Acridine orange-induced particle aggregation was observed. The phenomenon of the oxidant-induced red cell fluorescence is described.In recent years haemoglobin-erythrocyte membrane interaction has been the subject of considerable investigation. The cytoplasmic pole of the membrane-spanning protein Band 3 has been identified as the high-Mfinity binding site for haemoglobin [1][2][3][4]. More recently, interaction of denatured haemoglobin derivatives with the erythrocyte membrane was also investigated. Waugh and Low [5] reported that haemichromes induced by phenylhydrazine-treatment of haemoglobin have a much higher affinity for the cytoplasmic domain of Band 3 than native haemoglobin and that these haemichromes caused the isolated cytoplasmic segment of Band 3 to precipitate in solution.

show abstract

mentioning

confidence: 51%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

The distribution and aggregatability of intramembrane particles in phenylhydrazine-treated human erythrocytes

Lelkes

Fodor

Hollán

et al. 1988

Biochimica et Biophysica Acta (BBA) - Biomembranes

View full text Add to dashboard Cite

show abstract

“…Multiple physiologic events are thought to contribute to vaso-occlusion, including hemoglobin S polymerization with consequent RBC deformation [1], cell dehydration leading to increased hemoglobin polymerization [2,3], RBC adhesion to endothelial cells and extracellular matrix (ECM) proteins [4], and activation of coagulation [5][6][7]. Red blood cells containing predominantly hemoglobin S (SS RBC) adhere most avidly to laminin among ECM proteins [8].…”

Section: Introductionmentioning

confidence: 99%

B‐CAM/LU expression and the role of B‐CAM/LU activation in binding of low‐ and high‐density red cells to laminin in sickle cell disease

et al. 2004

View full text Add to dashboard Cite

Red blood cells from patients with sickle cell disease (SS RBC) adhere to laminin and over-express the high-affinity laminin receptor basal cell adhesion molecule/Lutheran protein (B-CAM/LU). This receptor has recently been shown to undergo activation in vitro through a protein kinase A-dependent mechanism. Low-density SS RBC express twothirds more B-CAM/LU than high-density SS RBC. However, high-density SS RBC have been identified as most adherent to laminin under flow conditions. We investigated the ability of low-and high-density SS RBC to interact with laminin under various conditions and explored factors that might be responsible for the differences in B-CAM/LU-laminin interaction between high-and low-density SS RBC. We confirmed that high-density SS RBC adhere to laminin more strongly than low-density SS RBC under flow conditions. However, low-density SS RBC bind soluble laminin most strongly and are the most adherent to laminin under static conditions. Soluble recombinant Lutheran extracellular domain protein completely blocked SS RBC adhesion to laminin under both static and flow conditions. The protein kinase A inhibitor 14-22 amide inhibited adhesion to laminin during flow by high-density SS RBC from patients with strongly adherent cells but had no effect on adhesion observed after a static phase. Deletion of the cytoplasmic domain of B-CAM as well as mutation of the juxtamembranous tyrosine residue failed to reduce B-CAM-mediated adhesion to laminin by transfected MEL cells. These studies confirm that B-CAM/LU is the most critical receptor mediating adhesion to laminin under both static and flow conditions. Dense SS RBC are most adherent to laminin despite bearing fewer laminin receptors, apparently due to a reversible protein kinase A-dependent process that is unlikely to involve direct phosphorylation of B-CAM/LU. Our results also suggest that the nature of the interaction of B-CAM/LU with laminin may be different under static and flow conditions. Am.

show abstract

“…A second postulate suggests that disulfide-linked hemoglobin adducts to critical membrane skeletal proteins, formed via hemoglobin thiyl radical attack of the protein free sulfhydryl groups, initiates red cell sequestration Jollow and McMillan, 1998). In support of this postulate, a number of investigators have shown that hemoglobin attachment to the cytosolic domain of band 3 causes alterations in the lateral distribution of this integral membrane protein leading to the binding of autologous antibodies on the external cell surface, which initiates erythrophagocytosis (Lutz et al, 1984;Waugh et al, 1986Waugh et al, , 1987Turrini et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

Primaquine-Induced Hemolytic Anemia: Effect of 6-Methoxy-8-hydroxylaminoquinoline on Rat Erythrocyte Sulfhydryl Status, Membrane Lipids, Cytoskeletal Proteins, and Morphology

Bolchoz

Morrow

Jollow

et al. 2002

J Pharmacol Exp Ther

View full text Add to dashboard Cite

Previous studies have shown that 6-methoxy-8-hydroxylaminoquinoline (MAQ-NOH), an N-hydroxy metabolite of the antimalarial drug, primaquine, is a direct-acting hemolytic agent in rats. To investigate the mechanism underlying this hemolytic activity, the effects of hemotoxic concentrations of MAQ-NOH on rat erythrocyte sulfhydryl status, membrane lipids, skeletal proteins, and morphology have been examined. Treatment of rat erythrocytes with a TC 50 concentration of MAQ-NOH (350 M) caused only a modest and transient depletion of reduced glutathione (GSH) (ϳ30%), which was matched by modest increases in the levels of glutathione disulfide and glutathione-protein mixed disulfides. Lipid peroxidation, as measured by thiobarbituric acidreactive substances and F 2 -isoprostane formation, was induced in a concentration-dependent manner by MAQ-NOH. However, the formation of disulfide-linked hemoglobin adducts on membrane skeletal proteins and changes in erythrocyte morphology were not observed. These data suggest that hemolytic activity results from peroxidative damage to the lipid of the red cell membrane and is not dependent on skeletal protein thiol oxidation. However, when red cell GSH was depleted (Ͼ90%) by titration with diethyl maleate, hemolytic activity of MAQ-NOH was markedly enhanced. Of interest, exacerbation of hemotoxicity was not matched by increases in lipid peroxidation, but by the appearance of hemoglobin-skeletal protein adducts. Collectively, the data are consistent with the concept that MAQ-NOH may operate by more than one mechanism; one that involves lipid peroxidation in the presence of normal amounts of erythrocytic GSH, and one that involves protein oxidation in red cells with low levels of GSH, such as are seen in individuals with glucose-6-phosphate dehydrogenase deficiency.

show abstract

Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes.

Cited by 104 publications

References 38 publications

The distribution and aggregatability of intramembrane particles in phenylhydrazine-treated human erythrocytes

The distribution and aggregatability of intramembrane particles in phenylhydrazine-treated human erythrocytes

B‐CAM/LU expression and the role of B‐CAM/LU activation in binding of low‐ and high‐density red cells to laminin in sickle cell disease

Primaquine-Induced Hemolytic Anemia: Effect of 6-Methoxy-8-hydroxylaminoquinoline on Rat Erythrocyte Sulfhydryl Status, Membrane Lipids, Cytoskeletal Proteins, and Morphology

Contact Info

Product

Resources

About