Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023473 (chronic myeloid leukemia)
 18,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The major palmitoylated human erythrocyte membrane protein has an M(r) of 55,000. It is distinct from the glucose transporter and is not derived from band 3 or ankyrin. It resists salt extraction suggesting a high affinity for the membrane. Pulse chase experiments demonstrate that palmitoylation is a dynamic process, and it may therefore have regulatory significance in membrane protein-protein or protein-lipid interaction. Slower dynamics of palmitoylation in erythrocytes from patients suffering from chronic myelogenous leukemia, which are less stable than normal erythrocytes, strengthen this view.
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PMID:Fatty acylation of a 55 kDa membrane protein of human erythrocytes. 163 37

Two mechanisms have been proposed for maintenance of transbilayer phospholipid asymmetry in the erythrocyte plasma membrane, one involving specific interactions between the aminophospholipids of the inner leaflet of the bilayer and the cytoskeleton, particularly spectrin, and the other involving the aminophospholipid translocase. If the former mechanism is correct, then erythrocytes which have lost their asymmetric distribution of phospholipids should display altered bilayer/cytoskeleton interactions. To test this possibility, normal erythrocytes, erythrocytes from patients with chronic myelogenous leukemia or sickle disease, and lipid-symmetric and -asymmetric erythrocyte ghosts were labeled with the radioactive photoactivable analogue of phosphatidylethanolamine, 2-(2-azido-4-nitrobenzoyl)-1-acyl-sn-glycero-3-phospho[14C]ethanolamine ([14C]AzPE), previously shown to label cytoskeletal proteins from the bilayer. The labeling pattern of cytoskeletal proteins in pathologic erythrocytes and lipid-asymmetric erythrocyte ghosts was indistinguishable from normal erythrocytes, indicating that the probe detects no differences in bilayer/cytoskeleton interactions in these cells. In contrast, in lipid-symmetric erythrocyte ghosts, labeling of bands 4.1 and 4.2 and actin, and to a lesser extent ankyrin, by [14C]AzPE was considerably reduced. Significantly, however, labeling of spectrin was unaltered in the lipid-symmetric ghosts, suggesting that its relationship with the bilayer is normal in these lipid-symmetric cells. These results do not support a model in which spectrin is involved in the maintenance of an asymmetric distribution of phospholipids in erythrocytes.
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PMID:Bilayer/cytoskeleton interactions in lipid-symmetric erythrocytes assessed by a photoactivable phospholipid analogue. 186 52

Chronic myelogenous leukemia (CML) is a hematologic malignancy characterized by excessive growth of myeloid cells and their progenitors. The proportion of spectrin dimers compared to tetramers extracted from membranes at 4 degrees C, under low ionic strength conditions, increased in CML erythrocytes. These also displayed abnormal thermal sensitivity (between 45 and 46 instead of 49 degrees C). Crosslinking with the bifunctional reagent, dimethyl adipimidate (8.6 A) showed significant organizational modification of not only spectrin, but other cytoskeletal components such as ankyrin, bands 4.2 and 5. Enhanced concanavalin A (Con-A) agglutinability of CML erythrocytes also suggests altered topographic distribution of a functionally important membrane protein, band 3. The anion transport activities of erythrocytes from patients with CML and normal donors were comparable. In CML erythrocytes, significant reduction in the number of ankyrin-binding sites, present in the cytoplasmic domain of band 3, may lead to partial loss of cytoskeletal anchorage to the bilayer and account for their increased Con-A agglutinability and heat sensitivity and may lead to their premature removal from the circulation.
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PMID:Abnormalities of the erythrocyte membrane in chronic myelogenous leukemia. 214 40

Chronic myelogenous leukemia (CML) is a hematologic malignancy arising from an abnormal hemopoietic stem cell. Our earlier studies have identified defects in spectrin tetramer formation and organization of cytoskeletal proteins (Basu et al., Biochim. Biophys. Acta 1988, 121-126); and decreased ankyrin binding to ankyrin-depleted vesicles in CML patients. These may lead to clustering of band 3 and increased binding of autologous IgG. This has now been explored by studying the binding of 125I-protein A to normal and CML erythrocytes. There is increased binding of 125I-protein A in CML erythrocytes compared to normal erythrocytes. Since binding of autologous IgG is responsible for removal of erythrocytes from the circulation, the above findings suggest that CML erythrocytes are likely to be prematurely removed from the circulation, accounting for anemia.
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PMID:Chronic myelogenous leukemia: alterations in red cell membrane band 3 and increased IgG binding. 215 1

The anion transport activities of erythrocytes from patients with chronic myelogenous leukemia (CML) and normal donors were comparable. In CML erythrocytes, significant reduction in the number of ankyrin-binding sites, present in the cytoplasmic domain of band 3, may lead to partial loss of cytoskeletal anchorage to the bilayer and account for their increased Con-A agglutinability and heat-sensitivity (Basu, J., Kundu, M., Rakshit, M.M. and Chakrabarti, P. (1988) Biochim. Biophys. Acta 945, 121-126).
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PMID:Abnormalities in erythrocyte membrane band 3 in chronic myelogenous leukemia. 252 93

Chronic myelogenous leukaemia (CML) is a haematologic malignancy characterised by excessive growth of myeloid cells and their progenitors. Our studies show that there are several abnormalities in CML red blood cells. The proportion of spectrin dimers compared to tetramers extracted from membranes at 4 degrees C, under low ionic strength conditions, increased in CML erythrocytes. These also displayed abnormal thermal sensitivity (between 45 and 46 instead of 49 degrees C). Decreased spectrin tetramer formation observed in several hereditary anaemias has been associated with decreased red cell deformability leading to splenic sequestration. This could also be one of the causes of the severe anaemia observed in CML. Crosslinking with the bifunctional reagent, dimethyl adipimidate (8.6 A) showed significant organizational modification of not only spectrin, but other cytoskeletal components such as ankyrin, bands 4.2 and 5. Enhanced concanavalin A agglutinability of CML erythrocytes also suggests altered topographic distribution of a functionally important membrane protein, band 3.
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PMID:Abnormal erythrocyte membrane cytoskeleton structure in chronic myelogenous leukaemia. 319 Nov 16