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E-raamat: Handbook of H+-ATPases

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  • Ilmumisaeg: 19-Mar-2014
  • Kirjastus: Pan Stanford Publishing Pte Ltd
  • Keel: eng
  • ISBN-13: 9789814411929
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Handbook of H+-ATPasesSuurem pilt
  • Formaat: PDF+DRM
  • Ilmumisaeg: 19-Mar-2014
  • Kirjastus: Pan Stanford Publishing Pte Ltd
  • Keel: eng
  • ISBN-13: 9789814411929
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Nakamura presents research in medicine and basic science on V-type proton pumps, with brief mentions of P-type pumps and overall focus on the relationship of these ATPases to glucose metabolism and signaling, diabetes, and related pathologies. The first couple of chapters discuss assembly and structure, followed by the role of V-ATPases in gluconeogenic enzyme degradation and Npt2a trafficking and regulation by pH and glucose concentrations. Several contributions explore connections to diabetes, kidney function, and cancer, discussing regulatory pathways, protein structure and function, gene expression, and polymorphisms. The last couple of chapters present studies on the maintenance of neural stem cells and the role of P-type pumps in glucose signaling. Distributed by CRC Press. Annotation ©2014 Ringgold, Inc., Portland, OR (protoview.com)

This handbook on vacuolar and plasma membrane H+-ATPases is the first to focus on an essential link between vacuolar H+-ATPase and the glycolysis metabolic pathway to understand the mechanism of diabetes and the metabolism of cancer cells. It presents recent findings on the structure and function of vacuolar H+-ATPase in glucose promoting assembly and signaling. It also describes the regulatory mechanisms of vacuolar H+-ATPase in yeast cells, neural stem cells, kidney cells, cancer cells, and under diabetic conditions.

Preface xv
1 Vacuolar H+-ATPase Assembly
1(30)
Anne M. Smardon
Patricia M. Kane
1.1 Introduction
1(1)
1.2 V-ATPase Subunit Composition and Mechanism
2(3)
1.3 Biosynthetic Assembly of the V-ATPase
5(4)
1.4 Assembly State Regulates V-ATPase Activity
9(11)
1.4.1 Reversible Dissociation of V1V0 Complex
9(2)
1.4.2 Control of Reversible Disassembly
11(1)
1.4.2.1 The RAVE complex (regulator of the ATPase of vacuolar and endosomal membranes)
11(1)
1.4.2.2 Glycolytic enzymes and V-ATPase assembly
12(2)
1.4.2.3 PKA-dependent regulation of V-ATPase assembly
14(2)
1.4.2.4 Structural organization and V-ATPase reversible disassembly
16(3)
1.4.2.5 Isoform-specific regulation of V-ATPase assembly
19(1)
1.5 Summary
20(11)
2 Structure of Prokaryotic V-Type ATPase/Synthase
31(20)
Ken Yokoyama
Jun-ichi Kishikawa
2.1 Introduction: Model for Eukaryotic V-ATPases
32(1)
2.2 Evolutionary Relationship between V-Type and F-Type ATPases
33(1)
2.3 Structure of Prokaryotic V-ATPases
34(13)
2.3.1 Subunit Structure of T. Thermophilus V-ATPase
34(1)
2.3.2 Cryo EM Map of Intact T. Thermophilus V-ATPase
35(3)
2.3.3 Structure of Rotor Ring
38(2)
2.3.4 Structure of V1 Domain (A3B3DF)
40(3)
2.3.5 Structure of Central Rotor Subunit C (Vo-d)
43(1)
2.3.6 Structure of DF Rotor
44(2)
2.3.7 Structure of EG Peripheral Stalk
46(1)
2.4 Perspective
47(4)
3 The Function of V-ATPase in the Degradation of Gluconeogenic Enzymes in Yeast Vacuoles
51(26)
Jingjing Liu
Hui-Ling Chiang
3.1 Introduction
51(1)
3.2 The Structure and Function of Vacuolar ATPase
52(4)
3.2.1 The Structure of V-ATPase
52(1)
3.2.1.1 The V1 domain
53(1)
3.2.1.2 The V0 domain
54(1)
3.2.2 The Assembly of V-ATPase
54(1)
3.2.3 The Function of V-ATPase in Organelle Acidification and Homotypic Vacuolar Fusion
55(1)
3.3 Catabolite Inactivation
56(4)
3.3.1 FBPase Can Be Degraded in the Proteasome or in the Vacuole Depending on Growth Conditions
57(1)
3.3.2 The Vacuole-Dependent Pathway
58(1)
3.3.3 The Discovery of Vid Vesicles
58(1)
3.3.4 Vid24p and the COPI Coatomer Proteins are Components of Vid Vesicles
59(1)
3.4 V-ATPase and the Vid Pathway
60(7)
3.4.1 An in vitro System to Study the Fusion of Vid Vesicles and Vacuoles
60(1)
3.4.2 V-ATPase is Involved in the Fusion of Vesicles with Vacuoles
61(1)
3.4.3 The Assembly of V-ATPase in Prolonged-Starved Cells
62(1)
3.4.4 The Acidification of the Vacuole is Required for the Vid Pathway
62(1)
3.4.5 Distinct Functions of Stv1p and Vph1p in the Vid Pathway
63(1)
3.4.6 The Vid Pathway Converges with the Endocytic Pathway
63(2)
3.4.7 In vivo Studies of VPH1 Functions in the Vid Pathway
65(2)
3.5 Conclusions and Future Perspectives
67(10)
4 The Role of Vacuolar ATPase in the Regulation of Npt2a Trafficking
77(22)
Eleanor Lederer
Syed Jalal Khundmiri
4.1 Introduction
77(1)
4.2 Npt2a: Structure, Function, and Regulation
78(10)
4.2.1 Role of pH in Regulation of Npt2a Function
81(2)
4.2.2 The Role of Vacuolar H+-ATPase in Npt2a Trafficking
83(5)
4.3 Conclusion
88(11)
5 Cytosolic pH Regulated by Glucose Promotes V-ATPase Assembly
99(24)
Reinhard Dechant
Matthias Peter
5.1 Introduction
100(2)
5.2 Factors Regulating V-ATPase Assembly
102(9)
5.2.1 Signaling Pathways
102(1)
5.2.1.1 Yeast
102(3)
5.2.1.2 Higher eukaryotes
105(1)
5.2.2 RAVE Complex
105(1)
5.2.3 Regulation of V-ATPase by Metabolic Signals
106(1)
5.2.4 Regulation of V-ATPase by pH
107(1)
5.2.4.1 Sensing of luminal pH by V-ATPase
107(1)
5.2.4.2 V-ATPase assembly is regulated by cytosolic pH in yeast
108(1)
5.2.4.3 V-ATPase subunit `a' is regulated by pH in vitro
109(2)
5.3 Cytosolic pH Is Regulated by Glucose
111(1)
5.4 V-ATPase as a Cytosolic pH Sensor
112(11)
5.4.1 Coupling of Cytosolic and Luminal pH
112(2)
5.4.2 Linking Cellular Physiology to Signal Transduction
114(9)
6 Vacuolar H+-ATPase (V-ATPase) Activated by Glucose: A Possible Link to Diabetes
123(28)
Suguru Nakamura
6.1 Introduction
123(1)
6.2 Glucose Activates V-ATPase Activity in LLC-PK1 Cells
124(1)
6.3 Glucose Activates Vacuolar H+-ATPase Activity in Rat Proximal Tubule
125(2)
6.4 Glucose Activation of V-ATPase Requires Glycolysis
127(8)
6.5 Glucose Activation of V-ATPase Requires PI3K Activity
135(4)
6.6 V-ATPase Activity in the Perfused Collecting Duct in Diabetic Animals
139(3)
6.7 Immunocytochemical Studies in the Collecting Duct in Diabetic Animals
142(9)
7 Vacuolar Proton Pump (V-ATPase) and Insulin Secretion
151(18)
Ge-Hong Sun-Wada
Yoh Wada
7.1 Introduction
151(1)
7.2 Structure and Regulation of V-ATPase
152(7)
7.2.1 The V-ATPase Complex
152(3)
7.2.2 The Rotational Catalysis of V-ATPase
155(1)
7.2.3 Regulation of the Activity of V-ATPase
155(1)
7.2.3.1 Function of isoforms of subunit a in enzyme targeting
156(1)
7.2.3.2 Regulation of V-ATPase enzyme activity via reversible dissociation
157(1)
7.2.3.3 Regulation of luminal acidification via other ion channels
157(2)
7.3 Secretory Granules and V-ATPase
159(2)
7.3.1 Secretory Hormones and Luminal Acidic pH
159(1)
7.3.2 Function of V-ATPase in Glucose Signaling
159(1)
7.3.3 Acidification of Secretory Granules by V-ATPase with a3 Subunit Isoforms
160(1)
7.4 V-ATPase in Vesicle Fusion
161(8)
8 Role of V-ATPase, Cytohesin-2/Arf6, and Aldolase in Regulation of Endocytosis: Implications for Diabetic Nephropathy
169(32)
Vladimir Marshansky
8.1 Endocytic Pathways: Uptake, Signaling, Recycling, or Degradation of Receptors/Ligand Complexes
170(1)
8.2 Regulation of Endocytosis by V-ATPase and the Luminal pH of Endosomal/Lysosomal Compartments
171(5)
8.2.1 Structure, Targeting, and Function of the V-ATPase Proton-Pumping Rotary Nano-Motor
171(4)
8.2.2 Role of V-ATPase in Trafficking and Function of Receptors and Their Regulatory Proteins along Endocytic Pathway
175(1)
8.3 Regulation of Endocytic Trafficking, Receptors Signaling and Gene Expression by Cytohesin-2 and Arf6 GTP-binding Proteins
176(3)
8.3.1 Role of Cytohesin-2 and Arf6 in Regulation of Endocytosis
176(2)
8.3.2 Emerging Role of Cytohesins in Receptors Signaling and Gene Expression
178(1)
8.4 Regulation of Endocytic Protein Degradation Pathway in Kidney Proximal Tubules: Implications for Development of Diabetic Nephropathy
179(22)
8.4.1 Kidney Proximal Tubule Megalin/Cubilin-Mediated Endosomal/Lysosomal Proteins Degradation Pathway
179(3)
8.4.2 Diabetes, Glucose Handling by Kidney Proximal Tubules and Diabetic Nephropathy
182(2)
8.4.3 Aldolase: Novel Roles of the "Old" Enzyme in Regulation of Endocytic Trafficking and Actin Cytoskeleton Rearrangement
184(1)
8.4.4 Role of V-ATPase, Cytohesin-2/Arf6 and Aldolase in Regulation of Megalin/Cubilin-Mediated Endosomal/Lysosomal Protein Degradation Pathway: Implications for Diabetic Nephropathy
185(16)
9 Kidney Vacuolar H+-ATPase Regulation
201(54)
Patricia Valles
Daniel Batlle
9.1 Introduction
202(1)
9.2 Structure and Molecular Organization of Vacuolar H+-ATPases
203(6)
9.2.1 The Cytosolic V1 Domain
205(1)
9.2.2 The Membrane-Associated V0 Domain
206(2)
9.2.3 The Stalk-Subunit Arrangement in the Stalk Regions
208(1)
9.3 Proton Transport by the V-ATPases
209(1)
9.4 Kidney-Specific Subunits of the Vacuolar H+-ATPase
210(1)
9.5 Distribution and Role of the Vacuolar H+-ATPase in the Kidney
211(8)
9.5.1 Proximal Tubule
211(2)
9.5.2 Loop of Henle
213(2)
9.5.3 Cortical Collecting Duct
215(3)
9.5.4 Medullary Collecting Duct
218(1)
9.6 Function of the Vacuolar H+-ATPase: Chloride Dependence
219(2)
9.7 Endocytosis and Acidification of Intracellular Vesicles
221(2)
9.8 Interaction of the Vacuolar H+-ATPase with SNARE Proteins
223(2)
9.9 Mechanisms of Regulation of Kidney Vacuolar H+-ATPase Activity
225(3)
9.10 Metabolic Regulation of the Vacuolar H+-ATPase Activity
228(2)
9.10.1 Metabolic Acidosis
228(1)
9.10.2 Metabolic Alkalosis
228(2)
9.11 Regulation of the Vaculoar H+-ATPase by the Renin-Angiotensin-Aldosterone System
230(5)
9.12 Functional Characterization of (pro)Renin Receptor in Association with V-ATPase
235(20)
10 Long-Term Regulation of Vacuolar H+-ATPase by Angiotensin II in Proximal Tubule Cells
255(16)
Luciene Regina Carraro-Lacroix
Thaissa Dantas Pessoa
Gerhard Malnic
10.1 General Considerations
255(1)
10.2 Angiotensin II Action on H+-ATPase
256(7)
10.3 V-ATPase is Associated with (Pro)-Renin Receptor
263(8)
11 Vacuolar H+-ATPase in Distal Renal Tubular Acidosis and Diabetes
271(22)
Irfan Shukrullah
Patricia Valles
Daniel Batlle
11.1 Introduction
271(2)
11.2 Renal Tubular Acidosis (RTA)
273(4)
11.2.1 ATP6VIB1 Mutations in dRTA
274(1)
11.2.2 ATP6V0A4 Mutations in dRTA
275(2)
11.3 Hearing Impairment in Hereditary dRTA
277(1)
11.4 Diabetes
278(4)
11.5 Connection with the (Pro)renin Receptor and Possible Role in Hypertension, Cardiovascular, and Renal Diseases
282(3)
11.6 Cancer
285(8)
12 Vacuolar H+-ATPase in Cancer and Diabetes
293(62)
Souad R. Sennoune
Raul Martinez-Zaguilan
12.1 Introduction
293(4)
12.1.1 Elevated Glycolysis in Cancer Induces Significant Acid Production
295(2)
12.2 Structure and Functions of Vacuolar H+-ATPases
297(4)
12.2.1 Accessory Proteins in Vacuolar H+-ATPase
298(1)
12.2.2 Inhibitors of Vacuolar H+-ATPase
299(1)
12.2.3 Physiological Significance of Vacuolar H+-ATPase
300(1)
12.3 Vacuolar H+-ATPase in Endomembranous Compartments and Vesicular Trafficking
301(2)
12.3.1 Vacuolar H+-ATPase in Membrane Trafficking
302(1)
12.4 Physiological and Pathological Significance of Vacuolar H+-ATPase at the Plasma Membrane
303(2)
12.4.1 Vacuolar H+-ATPases are Essential for Enveloped Virus Replication in Host Cells
304(1)
12.5 Significance of Vacuolar H+-ATPase in Diabetes and Cancer
305(1)
12.6 Regulation of Vacuolar H+-ATPase by Reversible Dissociation of V0 and V1 Domains
306(3)
12.7 Regulation of Vacuolar H+-ATPase by Glucose in Cancer
309(1)
12.8 Regulation of Vacuolar H+-ATPase by Phosphorylation
310(2)
12.9 Insulin Signaling and Vacuolar H+-ATPase
312(3)
12.10 Vacuolar H+-ATPase and Insulin Secretion
315(1)
12.11 ATP6ap2 and its Relationship with Vacuolar H+-ATPase
316(7)
12.11.1 Wnt Signaling Pathway Crosstalk with Vacuolar H+-ATPase
318(2)
12.11.2 (P)RR/ATP6ap2 Crosstalk with Vacuolar H+-ATPase
320(3)
12.12 Hypoxia-Induced Factor (HIF) Pathway Crosstalk with Vacuolar H+-ATPase
323(5)
12.13 Crosstalk between Diabetes and Cancer
328(2)
12.14 Conclusion
330(25)
13 The a2 Isoform of Vacuolar ATPase and Cancer-Related Inflammation
355(18)
Kenneth Beaman
Christina Kwong
Mukesh Jaiswal
Alice Gilman-Sachs
13.1 Introduction
355(1)
13.2 V-ATPase in Tumors
356(2)
13.3 V-ATPase and Cytokine Induction and Macrophage Development
358(1)
13.4 Vacuolar ATPase in Normal Cellular Processes and Human Disease
359(2)
13.5 The N-Terminus Domain of the a2 Isoform of Vacuolar ATPase (a2NTD) and its Role as an Immune Modulator
361(1)
13.6 Monocyte-Macrophage Polarization and Cancer Related Inflammation
362(1)
13.7 Innate Immune System, Inflammation and ATPase
363(10)
14 V-ATPases in Oral Squamous Cell Carcinoma
373(20)
Mario Perez-Sayans Garcia
Abel Garcia Garcia
14.1 Introduction
373(1)
14.2 Role of V-ATPases in Oral Cancer
374(5)
14.2.1 Role of V-ATPases in the Control of pH
374(1)
14.2.2 Role of V-ATPases in Metastasis
375(1)
14.2.3 Role of V-ATPases in Tumor Cell Growth and Survival
375(2)
14.2.4 Role of V-ATPases in MDR
377(1)
14.2.5 Role of V-ATPases as Therapeutic Target
378(1)
14.3 Role of ATP6V1C1 and Subunit C1 in V-ATPases and OSCC
379(4)
14.4 Conclusions
383(10)
15 Vacuolar H+-ATPase: Functional Mechanism and Potential as a Target for Cancer Chemotherapy
393(20)
Hiroto Izumi
Kimitoshi Kohno
15.1 pH Regulation in Cancer
394(2)
15.2 Structural and Functional Characteristics of V-ATPase
396(4)
15.3 Interacting Molecules with V-ATPase
400(1)
15.4 V-ATPase and Cancer Biology
401(2)
15.5 V-ATPase Inhibitors
403(2)
15.6 Structure of the Promoter of V-ATPase Genes
405(1)
15.7 Prospects
406(7)
16 V-ATPase Maintains Neural Stem Cells in the Developing Mouse Cortex
413(18)
Christian Lange
Silvia Prenninger
Philip Knuckles
Verdon Taylor
Michael Levin
Federico Calegari
16.1 Introduction
414(3)
16.2 YCHE78 Expression Promotes Neurogenesis
417(2)
16.3 YCHE78 Expression Inhibits Endogenous Notch Signaling
419(1)
16.4 YCHE78 Expression Rescues the Phenotype Induced by Activated Notch but Not of NICD
420(3)
16.5 Discussion
423(8)
17 The Relationship between Glucose-Induced Calcium Signaling and Activation of the Plasma Membrane H+-ATPase in Saccharomyces cerevisiae Cells
431(32)
Rogelio Lopes Brandao
17.1 Introduction
432(2)
17.2 General Characteristics of Plasma Membrane H+-ATPases
434(3)
17.3 The Signal Transduction Pathway Involved in the Post-Translational Regulation of the Plasma Membrane H+-ATPases in Yeast Cells
437(12)
17.4 Conclusions and Perspectives
449(14)
Index 463
Dr. Nakamura received his M.D. degree from the Jiangxi Medical University in 1984 and his Ph.D. from the Tokyo Medical and Dental University in 1995. Dr. Nakamura joined Murray State University in 2003 and his current position is Associate Professor of Biological Sciences. His research is focused on the physiological studies of acid-base balance and ion transports in the kidney.
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