Na/K-ATPase and related ATPases : proceedings of the 9th International Conference on the Na/K-ATPase and related ATPases, Sapporo, Japan, 18-23 August 1999
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書誌事項
Na/K-ATPase and related ATPases : proceedings of the 9th International Conference on the Na/K-ATPase and related ATPases, Sapporo, Japan, 18-23 August 1999
（International congress series, no. 1207）
Elsevier, 2000
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Includes bibliographical references and index
内容説明・目次
内容説明
In 1997, J.C. Skou was awarded the Nobel Prize in Chemistry for his discovery of Na/K-ATPase, which has led to widespread appreciation of this enzyme in the scientific community. This volume contains the latest findings and insights in the field and acts as a reference source containing a comprehensive overview of the present state of knowledge. It includes a proposal that Na/K-ATPase plays a role as a transducer of signal transduction, and, amongst other topics, covers the oligomericity of the enzyme, the site directed mutagenesis of P-type ATPases and the role of g-subunit. The book will serve as an important resource, not only for work on Na/K-ATPase, but also for the investigation of other P-type ATPases.
目次
- Preface. Part 1. What did we learn from Na/K-ATPase and other ATPases? The identification of the sodium-potassium pump (J.C. Skou). Discovery of the phosphorylated intermediate (R.L. Post). Significance of protein-protein interactions to Na+/K+-ATPase functions (A. Askari). The Na/K-ATPase: a current-generating enzyme (P. De Weer, D.C. Gadsby, R.F. Rakowski). Past achievements and future perspectives of Na, K-ATPase research (J.B. Lingrel). Structure of renal Na, K-ATPase as observed by cryo-EM of 2-D crystals (H. Herbert et al.). Endogenous cardiotonic steroids: facts and open questions (W. Schoner). Rotational catalysis by F-type ATPase (Y. Sambongi et al.). GFP-FRET detects swings of the lever-arm of myosin motor (K. Sutoh). Single molecule techniques in biophysics (T. Yanagida et al.). Rotation of ATP synthase (R. Yasuda et al.). Part 2. Structure-function relationship of the Na/K-, H/K- and Ca-pumps. Identification of amino acid residues involved in Na+ or K+ (Tl+) binding in Na, K-ATPase
- contributions to Na+/K+ specificity (P.L. Jorgensen et al.). The Na, K-ATPase alpha-beta subunit assembly site (D.M. Fambrough, L. Huynh, B. Hwang). Metal-catalysed oxidative cleavage of Na+,K+-ATPase. A tool for study of spatial organisation of the protein and the energy transduction mechanism (R. Goldshleger et al.). Dissecting and mapping two nucleotide binding sites in Na, K-ATPase (J.D. Cavieres, K.S. Lilley, D.G. Ward). Characteristics of fully active Na, K-ATPase from duck nasal glands (D.W. Martin, J.R. Sachs). Real concentrations of isoforms of Na, K-ATPase from western blots of tissue homogenates (O. Hansen). Structural and functional properties of human ouabain-sensitive H, K-ATPase (N.N. Modyanov et al.). Relation between ion binding and (de)phosphorylation in H+,K+-ATPase and Na+,K+-ATPase (J.J.H.H.M. De Pont et al.). Topology and plasticity of the membrane bound domains of sarcoplasmic reticulum Ca2+-ATPase and Na+, K+-ATPase (J.V. Moller et al.). A chimeric H+, K+-ATPase inhibitable with both ouabain and SCH 28080 (S. Asano et al.). Adenovirus vectors increase the efficiency of exogenous SERCA cDNA transfer into cultured cells, making possible direct measurements of Ca2+ binding by recombinant ATPase mutants (G. Inesi, Z. Zhang, C. Strock). Ion-transporting ATPases and ion channels: fundamentally similar mechanisms of ion transport? (G. Scheiner-Bobis). The 11A resolution projection structure of Na+ /K+-ATPase (Y. Tahara et al.). Three-dimensional structural study of Ca2+-ATPase from sarcoplasmic reticulum (C. Toyoshima, M. Nakasako, H. Nomura). Tubular crystallization of Na+, K+-ATPase (W.J. Rice et al.). Functional expression of Na Pump alpha1T in two mammalian expression systems (J.C. Allen et al.). Functional role of the Na, K-ATPase alpha subunit cysteines and their reactivity with extracellular Hg2+ (J.M. Arguello et al.). Long-term protection of solubilized sarcoplasmic reticulum Ca2+-ATPase by an amphipathic polymer, amphipol A8-35 (Ph. Champeil et al.). Mutagenesis of glutamate-795 affects cation binding of gastric H+, K+-ATPase (H.P.H. Hermsen et al.). Structural and functional characteristics of the Na, K-ATPase beta Subunit (U. Hasler et al.). Determination of Na, K-ATPase membrane topology by labeling of extracellular cysteine residues (Y.-K. Hu, J.H. Kaplan). Mutations Gly263 Ala and Arg264 Ala in the small cytoplasmic domain of rat kidney Na+, K+-ATPase stabilize the E1 and E1P forms (M.T. Jensen, M. Hauge, B. Vilsen). Mutants in the large cytoplasmic loop connecting TM4 and TM5 in pig kidney Na, K-ATPase are temperature sensitive folding mutants (J.R. Jfrgensen, P.A. Pedersen). The effect of ligands on the proteolysis pattern of SR Ca2+-ATPase: Information about the initial steps of the interaction of the ATPase with Ca2+ (B. Juul, J.V. Moller). High pressure-induced changes in lipid bilayer-protein interface of transmembrane Na+, K+-ATPase from pig kidney (M. Kato et al.). Chimeric analysis of beta-subunits between H+, K+-ATPase and Na+, K+-ATPase for the functional expression of gastric H+, K+-ATPase (T. Kimura et al.). K+-dependent association of solubilized Na+ /K+-ATPase and its reversal by Na+ (T. Kobayashi et al.). Residues of fourth transmembrane domain of the H, K- and Na, K-ATPases are important for ion selectivity (M. Mense et al.). Change in the thermal sensitivity of sarcoplasmic reticulum Ca-ATPase by chemical modifications and mutagenesis of specific Cys residues (T. Yamamoto, Y. Nagata, J. Nakamura). The fifth member of X, K-ATPase beta-subunit family possesses an atypical N-terminal domain (N.B. Pestov et al.). The beta subunit of the Na+, K+-ATPase in Xenopus laevis (S. Sagar et al.). The D804A mutant of Na+, K+-ATPase favours the E1 conformation in the absence of Na+, resulting in phosphorylation by ATP and a constitutive ATPase activity (H.G.P. Swarts et al.). Chimeric analysis of the first disulfide-bonded loop of the Na, K-ATPase beta-subunit (K. Takeda et al.). Does Na, K-ATPase need an oligomeric structure for ATP hydrolytic activity? (K. Takeda, M. Kunimoto, M. Kawamura). Na+, K+-ATPase mutant Phe788 Leu is inhibited by micromolar K+ and exhibits high Na+-ATPase activity at low Na+ concentrations (B. Vilsen). Molecular cloning of Na+-ATPase cDNA from marine alga Heterosigma akashiwo (M. Wada, M. Shono, Y. Hara). Truncation of the N-terminus of the Na, K-ATPase alpha-subunit affects ion transport functions of the sodium pump (C.H. Wu et al.). Diversity of P-type ATPase in vertebrate and invertebrate (J.C. Yasuhara et al.). Deletions or specific substitutions of a few residues in the NH2-terminal Ala3-Thr9 region of sarcoplasmic reticulum Ca2+-ATPase cause inactivation and rapid degradation of the enzyme expressed in COS-1 cells (T. Daiho et al.). Mutations of arginine-198 in sarcoplasmic reticulum Ca2+-ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate (K. Yamasaki et al.). Solubilization of Na+ K+ ATPase by non-ionic detergents with full retention of Rb occlusion (M. Carradus et al.). alpha4 is a functional isoform of the Na, K-ATPase and displays similar kinetics when associated with the beta1 or beta3 subunits (G. Blanco et al.). Part 3. Mechanism of the Na/K-pump and the related pumps. The influence of ionic strength on the rate of ATP-release from Na, K-ATPase (M. Esmann, N.U. Fedosova). Properties of the sodium-pump ion binding sites in state E1 (A. Schneeberger, H.-J. Apell). Reactivity of the Na+, K+-ATPase while cycling as Na+-ATPase (L. Beauge). Interaction between the catalytic phosphorylation site and the cation transport sites of P-type ATPases (I. Klodos, N.U. Fedosova, F. Cornelius). K+ induced charge translocation in the phosphoenzyme formed from inorganic phosphate (F. Tadini-Buoninsegni et al.). Contribution of quaternary protein interactions to the mechanism of energy transduction in Na+/K+-ATPase (J.P. Froehlich et al.). Na+- and K+-dependent change in oligomeric structure of solubilized Na+/K+-ATPase and effect of chaotropic anions (Y. Hayashi et al.). Tetraprotomeric hypothesis of Na/K-ATPase (K. Taniguchi et al.). Oligomer of two types of conformational variants of sarcoplasmic reticulum Ca2+-ATPase molecules (J. Nakamura, G. Tajima, T. Furukohri). Only half of the Ca2+-ATPase molecules present in sarcoplasmic reticulum vesicles can be phosphorylated with ATP or inorganic phosphate (H. Suzuki et al.). The catalytic domain of P-type pumps: evidence for two nucleotide sites (L.D. Faller et al.). Differential pump kinetics between alpha1 and alpha3 isoforms of the Na/K-ATPase (Y. Hara, T. Furukawa). Transition state like configuration of the active site in Ca2+-ATPase mutant Asp351 Ala following activation by Ca2+ (D.B. McIntosh et al.). Fast kinetic measurements of mutational effects on conformational changes in SR Ca2+-ATPase (T.L.-M. Soirensenet al.). Mutational analysis of the role of Thr353 in phosphorylation of the SR Ca2+-ATPase (J.D. Clausen, J.P. Andersen). The effect of nonionic radiocontrast media on the activity of purified human kidney Na+, K+ ATPase (F.G. Bino et al.). Photoinactivation of Na, K-ATPase by 2N3-ATP: protection by nucleotides and the puzzling effect of eosin Y (D. Burdon et al.). Dielectric constant in the phosphorylation site of Na, K-ATPase (N.U. Fedosova). Kinetic analysis of Na, K-pump-Rb influx in a medium replacing chaotropic ions in high K and high glutathione dog red blood cells (H. Fujise, T. Ka, M. Katoh). Cation-induced conformational changes in the ATP-binding domain of the Na, K-ATPase alter the reactivity of Lys-501 and Cys-577 (C. Gatto, S.J. Thornewell, J.H. Kaplan). The kinetic identity between occluded Rb+ formed in the Na+/K+-ATPase by the direct or by the physiological route (R.M. Gonzalez-Lebrero et al.). Na, K-ATPase on a waveguide sensor: supramolecular assembly and side directed binding studies by surface-confined fluorescence (E. Grell et al.). Quantifying transient conformational transitions of Na, K-ATPase: volume changes and activation volumes (Ch. Saudan et al.). Micellar Na, K-ATPase: mechanism of formation, functional properties and structural studies employing small-angle neutron and X-ray scattering (E. Schick et al.). Na pump isoforms in human red blood cells (J.F. Hoffman et al.). Effect of oligomycin on interaction of Na+ with Na+, K+-ATPase (H. Homareda, T. Ishii, K. Takeyasu). ATP induced fluorescence changes of a BIPM and an RH-421 probes in pig kidney Na/K-ATPase (T. Yokoyama et al.). Effect of amino acid substitutions in the 5th transmembrane region of the Na, K-ATPasealpha-Subunit on the kinetics and VM dependence of K+ 0-dependent ion transport (R.D. Peluffo, J.M. Arguello, J.R. Berlin). A microscale method to determine phosphorylated intermediates (M.M. Echarte et al.). Modeling the dependence of the thermal stability of the plasma membrane calcium pump on the micelle composition (V. Levi et al.). Effects of extracellular pH on the function of the Na+, K+-ATPase (P.S. Salonikidis et al.). Active transport of Ca2+ at the step of E1+ATP E1P as well as E1P E2P during the reaction of SR Ca2+-ATPase (M. Ushimaru,d Y. Fukushima). Part 4. Regulation of the Na/K-pump and related pumps at the level of genes, proteins, cells and tissues. Structure/function studies of the gamma subunit of renal Na, K-ATPase (A.G. Therien et al.). The renal Na, K-ATPase ancillary gamma subunit: fine-tuning of substrate ion affinities (E. Arystarkhova et al.). Regulation of Na+, K+-ATPase activity by hormones and second messengers (A. Aperia et al.). Molecular mechanism responsible for hormonal regulation of renal Na+-pump (R. Efendiev et al.). Molecular mechanisms of covalent regulation of the Na+ /K+-ATPase by protein kinases (L.A. Vasiletset al.). Sorting and Function of P-type ATPases in polarized epithelial cells (L.A. Dunbar et al.). Functional differences in Na, K-ATPase isoforms expressed in Xenopus oocytes (J.-D. Horisberger, S. Kharoubi-Hess). Regulation of SERCA pumps by phospholamban and sarcolipin (D. H. MacLennan et al.). Subunit interaction in the early stage of biogenesis of Na, K-ATPase (S. Noguchi, N. Sone, M. Kawamura). Splice variants of the Na,K-ATPase gamma subunit (K.J. Sweadner et al.). K+ /Na+ antagonism at cytoplasmic sodium activation sites of the Na, K-ATPase is a tissue-specific mechanism of pump regulation (A.G. Therien, R. Blostein). Regulation of myocardial K and Na, K-ATPase during high K intake (H. Bundgaard, K. Kjeldsen). Phospholemman as a putative regulatory protein of shark Na, K-ATPase (F. Cornelius, Y.A. Mahmmoud, H. Vorum). Physiological and pharmacological properties of human Na, K-ATPase isozymes (G. Crambert et al.). Effects of cholesterol,omega3 fatty acids and Omegacoeur(R), a mediterranean nutritional complement, on Na, K-ATPase activity in human endothelial cells (M.-J. Duran et al.). Role of nitric oxide and cGMP in modulating Na, K-ATPase activity in secretory epithelium (D.Z. Ellis, J.A. Nathanson, K.J. Sweadner). Does membrane composition determine the molecular activity of the sodium pump? (P.L. Else, B.J. Wu). Phosphorylation detection in intact cells with phosphorylation-sensitive antibodies: PKC and PKA phosphorylation of Na, K-ATPase (M.S. Feschenko, K.J. Sweadner). NMR analysis of kinases dependent N-terminal phosphorylatable portion in pig stomach H+, K+-ATPase (N. Fujitani et al.). Mechanism of regulation of sodium pump isoform activities in cultured cerebral neurons (N. Inoue, T. Soga, T. Kato). N-terminal phosphorylation of gastric H/K-ATPases both in vitro and in vivo (M. Kanagawa et al.). Variable protein kinase C targeting to the N- and C-terminal domains of shark Na, K-ATPase induced by detergent (Y.A. Mahmmoud, F. Cornelius). Na, K-ATPase in diabetic rat liver. Upregulation ofbeta1-subunit protein and mRNA (S. Sennoune et al.). Mass Spectrometric Analysis of the gamma Subunit of Na, K-ATPase (B. Kuster et al.). Regulation of sodium pump isoforms in cultured rat cerebellar granule cells (T. Sogaet al.). Characterization of intrinsic protein phosphatases which dephosphorylate phosphorylated Tyr and Ser residues of thealpha-chain of pig gastric H/K-ATPase (S.Watanabe et al.). Nitric oxide protects Na+, K+-ATPase function against hydroxyl radical induced inhibition (K.Y. Xu). Part 5. Physiology and pharmacology of the Na/K-pumps including regulation by cardiac glycosides. Na/K-ATPase as a signal transducer: regulation of growth-related pathways by cardiac glycosides (Z. Xie et al.). The sodium pump goes to the nucleus: when, how and why? (S.H. Yoshimura et al.). How ouabain works: control of subplasmalemmal Na+ and Ca2+, and their influence on Ca2+ signaling (M.P. Blaustein, A. Arnon, J.M. Hamlyn). Involvement of Na+, K+-ATPase inhibitors in cataract formation (D. Lichtstein et al.). Marinobufagenin, an endogenous bufodienolide sodium pump inhibitor (A.Y. Bagrov, E.G. Lakatta, O.V. Fedorova). Ouabain is endogenously produced in cultured PC12 cells with progesterone as the substrate (H. Takahashi, Y. Komiyama). Putative roles of ouabain-like compound in the pathophysiology of salt-dependent hypertension (A. Goto et al.). Alpha-1 adrenergic receptors stimulate secretion of endogenous ouabain from human and bovine adrenocortical cells (J. Laredo et al.). Newborn endogenous digitalis-like compound is similar to ouabain and different from ouabagenin (S. Balzan et al.). Marinobufagenin and cardiovascular remodeling in Dahl rats on a high NaCl diet (O.V. Fedorova, E.G. Lakatta, A.Y. Bagrov). Preparation of bioartificial kidney using tubular epithelial cells and its evaluation of Na+ active transport (Y. Fujitaet al.). Early effects of digitoxigenin on the cardiac action potential (S. Zillikens, H.G. Glitsch). Long-term effect of ouabain: transcriptional regulation of the Na/K-ATPase alphal subunit gene under ouabain treatment (T. Ishii, S. H. Yoshimura, K. Takeyasu). Diverse inhibitory effects of general anesthetics on Na+ ,K+-ATPase activity in rabbit brain (I. Kawada et al.). Human myocardial Na,K-ATPase in structural cardiac disease (H. Bundgaard, T.A. Schmidt, K. Kjeldsen). Partial purification and characterization of P-glycoprotein of bovine adrenal gland (M. Kudo et al.). Altered Na, K-ATPase and its preservation in ischemic and related diseases (J.M. Maixent et al.). Activation of cation transport by the anti-psychotic drug chlorpromazine (K. Mansfield, P.L. Else). Expression and digitalis sensitivity of Na, K-ATPase isoforms of human placenta and human erythrocytes (A. Paci et al.). Ginkgo biloba extract (EGb 761) protects Na, K-ATPase isozymes against differential effect of focal ischemia in the mouse (S. Pierre et al.). Kinetics and thermodynamics of enzyme-ouabain interactions (E.H. Hellen, B.C. Yacono, P.R. Pratap). Hypothyroidism stimulates Na, K-ATPase in the rat thyroid gland (T.A. Pressley, A.B. LeGrow, D.C. Fielding). Reversible inhibition of Na, K-ATPase by cis-diammine- dichloroplatinum(II) (CDDP) in human squamous cell carcinoma cell line of the gingiva, Ca9-22 cells (N. Sakakibara et al.). Purification of ouabain and HHIF from bovine hypothalamus and adrenal tissue (O. Gonzalez-Albarran et al.). Digoxin treatment related to human mycocardial and skeletal muscular Na, K-ATPase (T.S. Schmidt, H. Bundgaard, K. Kjeldsen). Inhibition of Na, K-ATPase activity by local anesthetics in rat brain and rabbit brain and kidney (K. Suzuki et al.). Effect of the local anesthetic carticaine on the sarcoplasmic reticulum Ca2+-ATPase (D. Takara et al.). Search for the domains necessary for the intra- and inter-subunit interactions of the Na/K-ATPase using a yeast two-hybrid system (Y. Ogita, K. Takeyasu, S.H. Yoshimura). P-type ATPases of malaria parasites (S. Krishna et al.). The structure of the putative endogenous ligands of the Na+ /K+-ATPase disclosed as derivatives of carbon suboxide (F. Kerek). Index of Authors.
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