Ecto-ATPases: Recent Progress on Structure and Function

Author:   Liselotte Plesner ,  Terence L. Kirley ,  Aileen F. Knowles
Publisher:   Springer-Verlag New York Inc.
Edition:   Softcover reprint of the original 1st ed. 1997
ISBN:  

9781461377290


Pages:   294
Publication Date:   23 October 2012
Format:   Paperback
Availability:   Manufactured on demand   Availability explained
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Ecto-ATPases: Recent Progress on Structure and Function


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Overview

It has been known for almost 50 years that many cells carry enzymes that hydro- lyze extracellular ATP, and the term ""ecto-ATPase"" was used first by Engelhardt 40 years ago. But until the end of the 1970's, the idea of an ATPase with its ATP hydrolyzing site on the outside of the cell membrane was met with substantial skepticism since it was thought that ATP was strictly intracellular. Nevertheless, ecto-ATPase activity was dem- onstrated using a variety of intact cells. Most ecto-ATPase(s) exhibited three common 2 characteristics: 1) activation by either Ca + or Mg2+, 2) insensitivity to the commonly used inhibitors ofF-type, P-type, and V-type ATPases, and 3) ability to hydrolyze nucleo- side triphosphates and often nucleoside diphosphates as well. At the same time, the dominant ATPase activity in many plasma membrane preparations was shown to be dis- tinct from the ion-pump ATPases, but had similar enzymatic properties as the ecto-AT- Pase(s). Thus the term ""E-type ATPase activity"" has been proposed for ATPase activity exhibiting these characteristics, and it is assumed that all ecto-ATPases are E-type AT- Pases. The converse is not true, however, since soluble E-type ATPases were shown to ex- sist in plants, microorganisms, and the saliva of blood sucking insects. These enzymes could be easily purified, and exhibited very high specific activity.

Full Product Details

Author:   Liselotte Plesner ,  Terence L. Kirley ,  Aileen F. Knowles
Publisher:   Springer-Verlag New York Inc.
Imprint:   Springer-Verlag New York Inc.
Edition:   Softcover reprint of the original 1st ed. 1997
Dimensions:   Width: 17.80cm , Height: 1.60cm , Length: 25.40cm
Weight:   0.596kg
ISBN:  

9781461377290


ISBN 10:   1461377293
Pages:   294
Publication Date:   23 October 2012
Audience:   Professional and scholarly ,  Professional & Vocational
Format:   Paperback
Publisher's Status:   Active
Availability:   Manufactured on demand   Availability explained
We will order this item for you from a manufactured on demand supplier.

Table of Contents

I. Ecto-ATPase: Characterization and Localization.- 1. Ecto-ATPases of the Nervous System.- 2. Evidence for Ectonucleotidases in the Guinea-Pig Cochlea: In Vivo and in Vitro Biochemical Studies.- 3. Solubilization and Characterization of an ATP Diphosphohydrolase (EC 3.6.1.5) from Rat Brain Synaptic Plasma Membranes.- 4. The Hydrolysis of Extracellular Adenine Nucleotides by Cultured Vascular Cells and Cardiac Myocytes.- 5. Distribution of Different ATP-Diphosphohydrolase Isoforms in Mammalian Organs.- 6. Solubilized E-Type ATPase Is Released from Intact Rat Tissues in the Simultaneous Presence of Nucleotides and Detergents.- 7. Ecto-ATP-Diphosphohydrolase from Normal and Abnormal Placenta.- 8. ATP-Diphosphohydrolase Activity from Mammary Gland: Regulation and Localization.- 9. Role of Ecto-ATPases, Based on Histochemical Investigations: Evidences and Doubts.- 10. Ecto-ATPase Activity in Goldfish Hepatocytes.- 11. Ecto-ATPases of the Kidney.- 12. Ecto-ATPase Activity in the Kidney.- 13. Inhibition of Porcine Renal Ecto-ATP Diphosphohydrolase by Ca2+ Channel Blockers and Neuroleptic Drugs.- 14. Human Tumor Ecto-ATPases.- II. Ecto-ATPase: Purification and Sequencing.- 15. Purification, Characterization, and Molecular Cloning of the Chicken Gizzard Smooth Muscle Ecto-ATPase.- 16. A Strategy for Monoclonal Antibody Production to Ecto-ATPases.- 17. Ecto-ATPase of Tetrahymena: Role in Purinergic Responses and Purification of a Soluble Form.- 18. Purification and Identification by Immunological Techniques of Different Isoforms of Mammalian ATP Diphosphohydrolases.- 19. ATP Diphosphohydrolase from Schistosoma mansoni Belongs to a New Family of Apyrases.- III. Ecto-ATPases: Function and Pathology.- 20. Immunochemical Expression of Ecto-ATP-Diphosphohydrolase in Experimental andClinical Disease.- 21. Control of Platelet Reactivity by an Ecto-ADPase on Human Endothelial Cells.- 22. Vascular ATP Diphosphohydrolase (CD39/ATPDase).- 23. Expression of Glomerular Ecto-ATPase in Idiopathic Nephrotic Syndrome.- 24. Role of Ecto-ATPase in Lymphocyte Function.- 25. ATP Diphosphohydrolase: A Possible Relation of This Enzyme with Alzheimer’s Disease and Thrombosis.- 26. ATP Diphosphohydrolase and 5?-Nucleotidase Activities from Hippocampal Synaptosomes after Brain Ischemia.- 27.The ATP-Diphosphohydrolase of Schistosoma mansoni: Ecto-Localization and Possible Roles in Host-Parasite Interactions.- 28. Potato Apyrase: An Overview: Characteristics and Localization of ATP-Diphosphohydrolase from Solarium tuberosum Tuber.- IV. Interrelationship of Ecto-ATPase and Purinoceptor Function.- 29. P2 Nucleotide Receptor Structure and Function.- 30. Ectonucleotidases and Purinoceptors in the Cochlea and Their Putative Role in Hearing.- 31. The Role of Eeto-Enzymes (Ecto-ATPase, 5?-Nucleotidase and Alkaline Phosphatase) in the Proliferation of LLC-MK2-Cells.- V. Other Relevant Cell Surface Proteins.- 32. Ubiquitous Expression of the ? - Subunit of H+-Transporting ATP Synthase on the Surface of Tumor Cells: Possible Role in Tumorigenesis and Immune Surveillance.- 33. PP120/C-CAM: Genomic Cloning and Role in Insulin Action and Metabolism.- 34. Is the Rat Liver Ecto-ATPase Identical to C-CAM/PP120, a Cell Adhesion Molecule?.- 35. Relationship of NCAM to E-Type ATPases of Rat Synaptosomes.- Participants.- Author Index.

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