Red blood cell membranes: structure, function, clinical implications

Cover......Page 1
Half Title......Page 2
Series Page......Page 3
Title Page......Page 6
Copyright Page......Page 7
Dedication Page......Page 8
Series Introduction......Page 10
Preface......Page 12
Contributors......Page 14
Contents......Page 18
 I. Introduction......Page 28
 II. The Current Conceptual Model of the Erythrocyte Membrane Skeleton......Page 29
 III. Recently Identified Erythrocyte Membrane-Skeletal Proteins......Page 31
 IV. New Interactions and Modalities of Regulation of Protein 4.1 and Ankyrin......Page 42
 V. Future Perspectives......Page 47
 References......Page 49
 I. Introduction......Page 58
 II. Purification and Characterization......Page 59
 IV. Structure and Function......Page 60
 V. The Glucose Transporter in Other Tissues......Page 66
 VII. Future Studies......Page 68
 References......Page 69
 I. Introduction......Page 74
 II. Intermediate Filaments: General Structure and Developmentally Regulated Expression......Page 75
 III. General Features of the Mammalian and the Avian Red Blood Cell......Page 76
 IV. Intracellular Interactions of Vimentin Filaments......Page 79
 V. Functional Implications of Divergent Cytoskeletal Gene Expression in Avian and Mammalian Red Blood Cells......Page 80
 VI. Assembly of Vimentin Filaments from a Soluble Precursor Subunit Pool......Page 82
 VII. Regulation of Vimentin Expression in Erythropoiesis Occurs at the mRNA Level......Page 83
 VIII. The Vimentin Gene: Structure and Regulation......Page 85
 IX. Transcriptional and Posttranscriptional Regulation of Vimentin mRNA Levels in Differentiating Murine Erythroleukemia Cells......Page 87
 X. Evolutionary Divergence of the Mechanisms Governing Vimentin Gene Expression in Avian and Mammalian Erythropoiesis......Page 88
 XI. Expression of Vimentin Filaments from Transfected Chicken Vimentin Genes in Differentiating Murine Erythroleukemia Cells......Page 90
 XII. Conclusion......Page 91
 References......Page 93
 II. Hereditary Elliptocytosis......Page 104
 III. Hereditary Spherocytosis......Page 124
 References......Page 131
 I. Introduction......Page 138
 II. Normal Spectrin Genes......Page 139
 III. Abnormal Spectrin Genes......Page 147
 IV. Conclusion......Page 153
 References......Page 155
 I. Introduction......Page 162
 II. Structure of the α Subunit......Page 167
 III. Na,K-ATPase α Subunit Isoforms......Page 174
 IV. Structure of the β Subunit......Page 179
 V. Structure of the γ Subunit......Page 182
 VI. Structure of the Na,K-ATPase......Page 183
 References......Page 184
 I. Introduction......Page 194
 II. Protein 4.1 cDNA Cloning......Page 196
 III. Characterization of Erythrocyte Protein 4.1 cDNA......Page 198
 IV. Primary and Secondary Structure of Protein 4.1......Page 200
 VI. Assignment of the Protein 4.1 Gene to Chromosome 1......Page 202
 VII. Molecular Basis of Hereditary Elliptocytosis......Page 204
 References......Page 210
 I. Introduction......Page 214
 II. Glycophorin May Regulate Cell Shape by Interacting with the Cytoskeleton......Page 215
 III. Association of Protein 4.1 with Glycophorin......Page 219
 IV. There Are Two Protein 4.1 Binding Receptors on the Membranes......Page 226
 V. A Phosphoinositide Is a Cofactor for Glycophorin-Protein 4.1 Associations......Page 232
 VI. Do Nonerythroid Protein 4.1 Analogues Require a Phosphoinositide for Membrane Binding?......Page 244
 VII. Implications......Page 253
 References......Page 257
 I. Interaction of Native Hemoglobin with Band 3......Page 264
 II. Interaction of Denatured Hemoglobin with Band 3......Page 271
 References......Page 280
 I. Introduction......Page 288
 II. Structural Components and Small Reconstituted Ensembles......Page 290
 III. Ultrastructure of Complexes Derived from Intact Skeletons......Page 293
 IV. Ultrastructure of Intact Skeletons......Page 300
 V. Molecular Basis of Erythrocyte Elasticity......Page 309
 VI. Conclusion and Future Perspectives......Page 316
 References......Page 317
 I. Introduction......Page 326
 II. The Polysaccharide Antigens......Page 327
 III. The Glycoprotein Antigens......Page 332
 IV. The Lipoprotein Antigens......Page 335
 V. Other Protein Antigens......Page 338
 References......Page 341
 I. Introduction......Page 352
 II. Structure and Organization of the Transferrin Receptor......Page 353
 III. Receptor Pools......Page 360
 IV. De Novo Synthesis of the Receptor: Posttranslational Modification and Factors Controlling Receptor Synthesis......Page 361
 V. Regulation of the Synthesis of Transferrin Receptors......Page 363
 VI. Acute Up- and Downregulation of the Transferrin Receptor......Page 364
 VII. Transferrin Receptors and the Development of Erythroid Cells......Page 366
 VIII. The Transferrin Receptor and Reticulocyte Maturation......Page 367
 X. Diagnosis of Malignancy and Erythropoiesis......Page 376
 XII. Conclusion......Page 377
 References......Page 378
 I. Introduction......Page 394
 II. Models of Membrane Protein and Lipid Diffusion......Page 396
 III. Measurements of Membrane Protein and Lipid Diffusion......Page 399
 IV. Band 3 and Glycophorin Diffusion......Page 405
 V. Phospholipid and Cholesterol Diffusion......Page 416
 VI. Conclusion and Future Prospects......Page 418
 References......Page 419
 I. Introduction......Page 428
 II. Structure of the Red Blood Cell Membrane: I......Page 429
 III. Bending or Shear?......Page 430
 IV. The Source of Membrane Bending Resistance......Page 433
 V. Albumin, pH, and Red Blood Cell Shape......Page 434
 VI. Crenation and Cupping: The Bilayer Couple Hypothesis......Page 436
 VII. Crenation and Cupping: The Protein Gel-Lipid Bilayer Hypothesis......Page 437
 VIII. Structure of the Red Blood Cell Membrane: II......Page 438
 IX. Crenation and Cupping: A Speculative Hypothesis Based on the Duplex Bilayer Model......Page 439
 X. The Spectrin Net......Page 443
 References......Page 445
 I. Introduction......Page 450
 II. Membrane Deformation: Theory and Experiment......Page 452
 III. Structural Implications......Page 470
 IV. Structural Defects......Page 475
 References......Page 478
 I. Introduction......Page 482
 II. Transport Modes of the Sodium Pump......Page 484
 III. Regulation of the Sodium Pump......Page 500
 References......Page 501
 I. Introduction......Page 508
 II. Some Hard Facts Concerning the Plasma Membrane Calcium Pump......Page 511
 III. Activation of the Calcium Pump by Calmodulin......Page 512
 IV. Anticalmodulin Agents as Inhibitors of the Calcium Pump......Page 514
 V. The Calcium Pump in Many Cells with Other Pumps......Page 516
 VI. Isolation of the Calcium Pump ATPase and Its Sequelae......Page 517
 VII. The Status of the Plasma Membrane Calcium Pump in the Red Blood Cell......Page 518
 References......Page 525
 I. Introduction......Page 534
 II. Cotransport......Page 536
 III. Calcium-Dependent K Channel (The Gardos Pathway)......Page 552
 IV. Passive Calcium Movements and Ca/Na Exchange......Page 560
 V. Band 3-Mediated Cation Movements......Page 563
 VI. Na(Li)-Na(Li) Countertransport......Page 564
 VII. Na-H Exchange......Page 567
 IX. Concluding Remarks......Page 570
 References......Page 571
 I. Functions of Anion Transport......Page 590
 II. Characteristics of Band 3 Transport......Page 601
 III. Clinical Implications......Page 616
 References......Page 618
 I. Introduction......Page 624
 II. The Methodology Used in Studies of Glucose Transport Kinetics......Page 625
 III. Inhibition of Glucose Transport......Page 640
 IV. Irreversible Inhibitors......Page 647
 V. Effects of ATP......Page 648
 VI. Thermodynamics of the Glucose Carrier Mechanism......Page 650
 VII. Conclusion......Page 655
 References......Page 656
 I. Introduction......Page 662
 II. The Nucleoside Transport System of Human Erythrocytes: A Reversible Carrier with Low Substrate Specificity......Page 663
 III. Fluxes of Nucleosides Across Human Erythrocytes Membranes Are Rapid......Page 665
 IV. Potent, High-Affinity Inhibitors Have Been Valuable Probes of Nucleoside Transport Systems in Erythrocytes......Page 666
 V. Not All Erythrocytic Nucleoside Transport Systems Are of High Sensitivity to NBMPR......Page 671
 VI. Nonnucleoside Drugs Are Also Potent Inhibitors of Nucleoside Permeation......Page 672
 VII. Nucleoside Transport Systems of High and Low Sensitivity to NBMPR Are Differentially Sensitive to Nonpenetrating Thiol Reagents......Page 674
 VIII. Exploration of the Molecular Properties of Erythrocyte Nucleoside Transport Systems with Nucleoside Transport Inhibitors......Page 675
 IX. Conclusion......Page 680
 References......Page 681
 I. Introduction......Page 690
 II. Ion Transport Regulated by Changes in Cell Volume......Page 691
 III. Catecholamine-Stimulated Ion Transport......Page 705
 IV. Other Physiological Effectors of Ion Transport......Page 710
 V. (K + Cl) Cotransport in Red Blood Cell Disorders......Page 711
 VI. Summary......Page 712
 References......Page 713
 II. The Sickle Erythrocyte......Page 718
 III. The Hemoglobin CC Erythrocyte......Page 724
 IV. The Stomatocyte......Page 725
 References......Page 727
 I. A Corpuscular Defect......Page 734
 II. Spherocytosis in Mice......Page 735
 III. Recessive Spherocytosis in Humans......Page 737
 V. Correlations with Spectrin Deficiency......Page 744
 VI. Genetic Defects Resulting in Spectrin Deficiency......Page 746
 VII. Pathogenesis of Spherocytosis Membranes......Page 748
 References......Page 751
Index......Page 754