Sodium–Calcium Exchange and the Plasma Membrane Ca2+–ATPase in Cell Function: Fifth International Conference, Volume 1099

Ca2+ homeostasis and the plasma membrane Na+/Ca2+ exchanger are vital to many cellular functions and physiological processes. This volume, which is the proceedings of the fifth in a series of international conferences, includes contributions that merge molecular biology, biochemistry, biophysics, and physiology, providing novel insights that significantly advance our understanding of Na+/Ca2+ exchanger in areas ranging from molecular mechanisms to the involvement in human disease.
Several important themes are addressed: (1) structure–function relationships of the exchanger; (2) regulation of the exchanger; (3) Na/Ca exchanger gene regulation; (4) cellular location and targeting of the exchanger; (5) NC(K)X and PMCA KO mice; (6) Na/Ca exchanger interactions with other proteins; (7) Na/Ca exchange in cardiac function; (8) Na/Ca exchange in neuronal function; (9) Ca2+–extruding mechanisms and apoptosis; (10) Na/Ca exchange in smooth muscle, kidney, and endocrine function; (11) Na/Ca exchange inhibitors: therapeutic opportunities. Experts in the field of the plasma membrane Ca2+–ATPase (PMCA) have also contributed.
The rate of progress in this field has been rapidly increasing, and new concepts have emerged regarding the relation between molecular structure and physiological function. New ideas on physiological modes of regulation have been increasingly testable through the use of transgenic animal models.
This volume and the conference that preceded it continue the tradition of sharing information to fuel new advances in this exciting and important area of research.
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Spis treści:
Preface: Andre Herchuelz.
Historical Note Regarding the Discovery of the Na/Ca Exchanger and the PMCA: Andre Herchuelz.
Part I: Structure–Function Relationships of the Exchanger:.
1. What We Know about the Structure of NCX1 and How It Relates to Its Function: Debora A. Nicoll, Xiaoyan Ren, Michela Ottolia, Martin Phillips, Alfredo R. Paredes, Jeff Abramson, and Kenneth D. Philipson.
2. Structural Basis for Ca2+ Regulation in the Na+/Ca2+ Exchanger: Mark Hilge, Jan Aelen, Anastassis Perrakis, and Andgeerten W. Vuister.
3. Structure–Function Relationships of the NCKX2 Na+/Ca2+–K+ Exchanger: Y. Shibukawa, K.J. Kang, T.G. Kinjo, R.T. Szerencsei, H.F. Altimimi, P. Pratikhya, R.J. Winkfein, and P.P.M. Schnetkamp.
4. Examining Ca2+ Extrusion of Na+/Ca2+–K+ Exchangers: Haider F. Altimimi and Paul P.M. Schnetkamp.
5. Topologic Investigation of the NCKX2 Na+/Ca2+–K+ Exchanger α–Repeats: Tashi G. Kinjo, Robert T. Szerencsei, and Paul P.M. Schnetkamp.
6. Transmembrane Segments I, II, and VI of the Canine Cardiac Na+/Ca2+ Exchanger Are in Proximity: Xiaoyan Ren, Debora A. Nicoll, and Kenneth D. Philipson.
7. Effect of Ca2+ on Protein Kinase A–Mediated Phosphorylation of a Specific Serine Residue in an Expressed Peptide Containing the Ca2+–Regulatory Domain of Scallop Muscle Na+/Ca2+ Exchanger: C. Ryan, G. Shaw, and P.M.D. Hardwicke.
Part II. Regulation of the Exchanger:.
8. Regulation of the Cardiac Na+/Ca2+ Exchanger by Calcineurin and Protein Kinase C: Munekazu Shigekawa, Yuki Katanosaka, and Andshigeo Wakabayashi.
9. New Modes of Exchanger Regulation: Physiological Implications: John P. Reeves, Madalina Condrescu, Jason Urbanczyk, and Olga Chernysh.
10. Shedding Light on the Na+/Ca2+ Exchanger: Michela Ottolia, Scott John, Yi Xie, Xiaoyan Ren, and Kenneth D. Philipson.
11. The Regulation of the Na/Ca Exchanger and Plasmalemmal Ca2+ ATPase by Other Proteins: Abdul M. Ruknudin and Edward G. Lakatta.
12. Phosphorylation and Other Conundrums of Na/Ca Exchanger, NCX1: Abdul M. Ruknudin, Shao–Kui Wei, Mark C. Haigney, W.J. Lederer, and Dan H. Schulze.
13. Regulation of Cardiac Na+/Ca2+ Exchanger by Phospholemman: Joseph Y. Cheung, Lawrence I. Rothblum, J. Randall Moorman, Amy L. Tucker, Jianliang Song, Belinda A. Ahlers, Lois L. Carl, Ju Fang Wang, and Xue–Qian Zhang.
14. The Squid Preparation as a General Model for Ionic and Metabolic Na+/Ca2+ Exchange Interactions: Physiopathological Implications: R. Dipolo and L. Beauge.
15. Some Biochemical Properties of the Upregulation of the Squid Nerve Na+/Ca2+ Exchanger by MgATP and Phosphoarginine: Graciela Berberian, Reinaldo Dipolo, and Luis Beauge.
16. Ionic Selectivity of NCKX2, NCKX3, and NCKX4 for Monovalent Cations at K+–Binding Site: Ju–Young Lee, Won–Kyung Ho, and Suk–Ho Lee.
17. In Bovine Heart Na+/Ca2+ Exchanger Maximal Ca2+ i Affinity Requires Simultaneously High pHi and PtdIns–4,5–P2 Binding to the Carrier: Velia Posada, Luis Beauge, and Graciela Berberian.
18. NCX Current in the Murine Embryonic Heart: Development–Dependent Regulation by Na+: Michael Reppel, Hannes Reuter, Philipp Sasse, Jurgen Hescheler, and Bernd K. Fleischmann.
19. Gender Differences in Na/Ca Exchanger Current and β–Adrenergic Responsiveness in Heart Failure in Pig Myocytes: Shao–Kui Wei, John M. McCurley, Stephen U. Hanlon, and Mark C.P. Haigney.
20. Roles of NCX and PMCA in Basolateral Calcium Export Associated with Mineralization Cycles and Cold Acclimation in Crayfish: M.G. Wheatly, Y. Gao, L.M. Stiner, D.R. Whalen, M. Nade, F. Vigo, and A.E. Golshani.
Part III: Na/Ca Exchanger Gene Regulation :.
21. Modulation Pathways of NCX mRNA Stability: Involvement of RhoB: Sachiko Maeda, Isao Matsuoka, and Junko Kimura.
22. Regulation of Ncx1 Gene Expression in the Normal and Hypertrophic Heart: Donald R. Menick, Ludivine Renaud, Avery Buchholz, Joachim G. Muller, Hongming Zhou, Christiana S. Kappler, Steven W. Kubalak, Simon J. Conway, and Lin Xu.
23. Cyclosporin A–Dependent Downregulation of the Na+/Ca2+ Exchanger Expression: H. Rahamimoff, B. Elbaz, A. Alperovich, C. Kimchi–Sarfaty, M.M. Gottesman, Y. Lichtenstein, M. Eskin–Shwartz, and J. Kasir.
Part IV: Cellular Location of the Exchanger:.
24. Functional Significance of Na+/Ca2+ Exchangers Co–localization with Ryanodine Receptors: Anna A. Sher, Robert Hinch, Penelope J. Noble, David J. Gavaghan and Denis Noble.
25. Three Types of Muscles Express Three Sodium–Calcium Exchanger Isoforms: Dmitri O. Levitsky.
Part V: Structure–Function Relationship of the Plasma Membrane Ca2+–ATPase:.
26. Plasma Membrane Ca2+ ATPases as Dynamic Regulators of Cellular Calcium Handling: Emanuel E. Strehler, Ariel J. Caride, Adelaida G. Filoteo, Yuning Xiong, John T. Penniston, and Agnes Enyedi.
27. Functional Specificity of PMCA Isoforms?: Teuta Domi, Francesca Di Leva, Laura Fedrizzi, Alessandro Rimessi, and Marisa Brini.
28. Plasma Membrane Calcium ATPase and Its Relationship to Nitric Oxide Signaling in the Heart: Elizabeth J. Cartwright, Delvac Oceandy, and Ludwig Neyses.
29. Functional Importance of PMCA Isoforms in Growth and Development of PC12 Cells: Ludmila Zylinska, Anna Kozaczuk, Janusz Szemraj, Christos Kargas, and Iwona Kowalska.
Part VI: NC(K)X and PMCA KO Mice:.
30. Na+/Ca2+ Exchanger Knockout Mice: Plasticity of Cardiac Excitation–Contraction Coupling: Christian Pott, Scott A. Henderson, Joshua I. Goldhaber, and Kenneth D. Philipson.
31. Distinct Phenotypes among Plasma Membrane Ca2+–ATPase Knocko