Divalent cation binding to erythrocyte spectrin

Wallis, Cleatus J.; Babitch, Joseph A.; Wenegieme, Elizabeth F.

doi:10.1021/bi00070a011

Cited by 27 publications

(16 citation statements)

References 48 publications

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“…Also, Mg 2+ was shown to increase erythrocyte membrane stability [125]. It is noteworthy that spectrin has binding sites for both Mg 2+ and Ca 2+ [126] (Fig 3B). As for DPG levels in mammals, there are significant inter-species differences [127,128] and regulation of DPG metabolism has been analyzed mathematically [129][130][131].…”

Section: +mentioning

confidence: 86%

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Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

Barvitenko

Adragna

Weber³

2005

Cell Physiol Biochem

135

104

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Erythrocytes play a key role in human and vertebrate metabolism. Tissue O₂ supply is regulated by both hemoglobin (Hb)-O₂ affinity and erythrocyte rheology, a key determinant of tissue perfusion. Oxygenation-deoxygenation transitions of Hb may lead to re-organization of the cytoskeleton and signalling pathways activation/deactivation in an O₂-dependent manner. Deoxygenated Hb binds to the cytoplasmic domain of the anion exchanger band 3, which is anchored to the cytoskeleton, and is considered a major mechanism underlying the oxygenation-dependence of several erythrocyte functions. This work discusses the multiple modes of Hb-cytoskeleton interactions. In addition, it reviews the effects of Mg²⁺, 2,3-diphosphoglycerate, NO, shear stress and Ca²⁺, all factors accompanying the oxygenation-deoxygenation cycle in circulating red cells. Due to the extensive literature on the subject, the data discussed here, pertain mainly to human erythrocytes whose O₂ affinity is modulated by 2,3-diphosphoglycerate, ectothermic vertebrate erythrocytes that use ATP, and to bird erythrocytes that use inositol pentaphosphate.

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Section: +mentioning

confidence: 86%

“…Effects of Ca 2+ on red cell mechanical properties are mediated by direct binding of Ca 2+ to cytoskeletal proteins (e.g. spectrin [126]), via calmodulin [180][181][182] and via Ca 2+ -dependent enzymes (e.g. calpain [198]).…”

Section: +mentioning

confidence: 99%

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

Barvitenko

Adragna

Weber³

2005

Cell Physiol Biochem

135

104

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“…From the small dependence of the observed 7Li relaxation values on Li+ concentration and the small values of the T1/T2 ratios, we conclude that only weak Li+ interactions with SA are present for the Li+ levels typically present in RBCs. Ca*+, and to a smaller extent Mg2+, binds strongly to erythroid spectrin (Wallis et al, 1993); it is therefore unlikely that therapeutic concentrations of Li+ would compete with physiological intracellular concentrations of Ca2+ and Mg2+. The small values, and the small concentration dependence, of the T1/T2 ratios observed with Li+ solutions containing physiological concentrations of BPG and ATP (Table I) also indicate weak Li+-BPG and Li+-ATP interactions.…”

Section: Discussionmentioning

confidence: 99%

Lithium-7 NMR relaxation study of lithium binding in human erythrocytes

Rong¹,

Espanol²,

Freitas³

et al. 1993

Biochemistry

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ABSTRACT:We used 7Li N M R spin-lattice (TI) and spin-spin (Tz) relaxation time measurements to investigate the binding of Li+ in human red blood cell (RBC) suspensions. In RBCs containing 1.4 mM Li+, the intracellular 7Li N M R T2 relaxation value (0.30 f 0.03 s) was much smaller than the corresponding TI value (6.0 f 0.1 s), yielding a ratio of TI to T 2 of 20. For 1.5 mM LiCl solutions whose viscosities were adjusted to 5 CP with glycerol, the values of the T1/T2 ratios were as follows: 49 for unsealed RBC membrane (2.0 mg of protein/mL); 4.4 for spectrin (1.9 mg/mL); 1.5 for 5.4 mM 2,3-bisphosphoglycerate (BPG); 2.2 for 2.7 mM carbonmonoxyhemoglobin (COHb); 1.6 for 2.0 mM ATP; and 1.2 for a 50/50% (v/v) glycerol-water mixture. Intracellular viscosity and the electric field gradients experienced by Li+ when traversing the spectrin-actin network therefore are not responsible for the large values of the Tl/ T2 ratios observed in Li+-loaded RBCs. We conclude that the RBC membrane is the major Li+ binding site in Li+-loaded RBCs (KI, = 215 f 36 M-l) and that the binding of Li+ to COHb, BPG, spectrin-actin, or ATP is weak. Partially relaxed 7Li N M R spectra of Li+-containing RBC membrane suspensions indicated the presence of two relaxation components, one broad and one narrow. At the same extravesicular Li+ and protein concentrations, the TI values for right-side-out RBC vesicle suspensions were at least 2-fold larger than those for inside-out RBC vesicle suspensions; the inner layer of the RBC membrane, which has a larger percentage of anionic phospholipids than the outer layer, contributes mostly to Li+ binding.

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“…Nonerythroid spectrin also localizes predominantly along cellular plasma membranes (21). Spectrin binds to a wide range of ligands like hemein and protoporphyrin (24), antitumor antibiotics of aureolic acid group, chromomycin, and mithramycin (25), the local anesthetic dibucaine (26), fluorescence probes like Prodan and pyrene (27,28), metal ions like calcium and molybdenum (29,30), other proteins like actin (31), globin chains and hemoglobin (32)(33)(34), calmodulin (35), and other skeletal proteins like ankyrin, adducin and Band 4.1 (21,36,37). Association of spectrin with other proteins are essential to establish the planar network along with additional interactions of fatty acids (38) and phospholipids (39 -41).…”

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confidence: 99%

Chaperone Activity and Prodan Binding at the Self-associating Domain of Erythroid Spectrin

Bhattacharyya

Ray²,

Bhattacharya

et al. 2004

Journal of Biological Chemistry

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Spectrin, the major constituent protein of the erythrocyte membrane skeleton, exhibits chaperone activity by preventing the irreversible aggregation of insulin at 25°C and that of alcohol dehydrogenase at 50°C. The dimeric spectrin and the two subunits, ␣-spectrin and ␤-spectrin prevent such aggregation appreciably better, 70% in presence of dimeric spectrin at an insulin:spectrin ratio of 1:1, than that in presence of the tetramer of 25%. Our results also show that spectrin binds to denatured enzymes ␣-glucosidase and alkaline phosphatase during refolding and the reactivation yields are increased in the presence of the spectrin derivatives when compared with those refolded in their absence. The unique hydrophobic binding site on spectrin for the fluorescence probe, 6-propionyl-2-(dimethylamino)-naphthalene (Prodan) has been established to localize at the self-associating domain with the binding stoichiometry of one Prodan/both dimeric and tetrameric spectrin. The other fluorescence probe, 1-anilinonaphthalene-8-sulfonic acid, does not show such specificity for spectrin, and the binding stoichiometry is between 3 and 5 1-anilinonaphthalene-8-sulfonic acid/dimeric and tetrameric spectrin, respectively. Regions in ␣-and ␤-spectrins have been found to have sequence homology with known chaperone proteins. More than 50% similarities in ␣-spectrin near the N terminus with human Hsp90 and in ␤-spectrin near the C terminus with human Hsp90 and Escherichia coli DnaJ have been found, indicating a potential chaperone-like sequence to be present near the self-associating domain that is formed by portions of ␣-spectrin near the N terminus and the ␤-spectrin near the C terminus. There are other patches of sequences also in both the spectrin polypeptides, at the other termini as well as in the middle of the rod domain having significant homology with well known chaperone proteins.

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Divalent cation binding to erythrocyte spectrin

Cited by 27 publications

References 48 publications

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance

Lithium-7 NMR relaxation study of lithium binding in human erythrocytes

Chaperone Activity and Prodan Binding at the Self-associating Domain of Erythroid Spectrin

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