2 edition of Ecto-ATPases and related ectonucleotidases found in the catalog.
Ecto-ATPases and related ectonucleotidases
International Workshop on Ecto-ATPases and Related Ectonucleotidases (2nd 1999 Diepenbeek, Belgium)
Includes bibliographical references and index.
|Statement||edited by Luc Vanduffel & Raf Lemmens.|
|Contributions||Vanduffel, Luc., Lemmens, Raf.|
|LC Classifications||QP609.A3 I575 1999|
|The Physical Object|
|Pagination||xx, 345 p. :|
|Number of Pages||345|
By biochemical purification and functional validation using knockout animals, ENPP1 is now defined as a major hydrolase for 2′,3′-cGAMP, a cyclic dinucleotide generated during antiviral innate Cited by: Detection of Mouse and Rat CD39L1/ENTPD2 by Western Blot. Western blot shows lysates of mouse salivary gland tissue and rat placenta tissue. PVDF Membrane was probed with 1 µg/mL of Sheep Anti-Mouse/Rat CD39L1/ENTPD2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # .
Proceedings of the Second International Workshop on Ecto-ATPases and Related Ectonucleotidases Chapter: Molecular and Functional Properties of E-NTPDase 1, E-NTPDase 2 and Ecto-5'-nucleotidase in Nervous Tissue Page 18 - 25 Zimmermann H, Braun N, Heine P, Kohring K, Sevigny J & Robson SC. Background and purpose: ARL , 6‐N,N‐Diethyl‐ D ‐β‐γ‐dibromomethylene adenosine triphosphate, originally named FPL , is the only commercially available inhibitor of ecto‐ATPases. Since the first report on this molecule, various ectonucleotidases responsible for the hydrolysis of ATP at the cell surface have been cloned and by:
Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases. (). Comparative hydrolysis of extracellular adenine nucleotides and adenosine in synaptic membranes from porcine brain cortex, hippocampus, cerebellum and medulla oblongata. CD39L1, also known as ENTPD2 and NTPDase2, is an ecto-nucleotidase belonging to the CD39 family. It is found on the surface of vascular adventitial cells and accessory vascular cells (1).
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Ecto-ATPases Recent Progress on Structure and Function. Editors: Plesner, Liselotte, Kirley, Terence L., Knowles, Aileen F. (Eds.) Free Preview. Buy this book eB49 € price for Spain (gross) Buy eBook ISBN Evidence for Ectonucleotidases in the Guinea-Pig Cochlea.
Pages 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 : Liselotte Plesner.
Ecto-ATPases Recent Progress on Structure and Function. Editors (view affiliations) Search within book. Front Matter. Pages i-xiv. PDF. Ecto-ATPase: Characterization and Localization. Front Matter. Pages PDF. ECTO-Atpases of the Nervous System. Agnes K. Nagy. Pages Evidence for Ectonucleotidases in the Guinea-Pig Cochlea.
Srdjan. ISBN: OCLC Number: Description: 1 online resource: Contents: I. Ecto-ATPase: Characterization and Localization Ecto-ATPases of the Nervous System Evidence for Ectonucleotidases in the Guinea-Pig Cochlea: In Vivo and in Vitro Biochemical Studies Solubilization and Characterization of an.
ISBN: OCLC Number: Notes: "Proceedings of the First International Workshop on Ecto-ATPases, held August, in Mar de Plata, Argentina"--Title page verso. Similar to the rat hepatoma cell surface ATPase, the ecto-ATPases of Li-7A and SCLC cells are inhibited by mercurials, e.g., pCMB and pCMPS, but it is unaffected by high concentrations of azide, an inhibitor of a membrane bound ATP diphosphohydrolase (25).
Ectonucleotidases are ectoenzymes that hydrolyze extracellular nucleotides to the respective nucleosides. Within the past decade, ectonucleotidases belonging to several enzyme families have been discovered, cloned and by: Ecto-nucleotidases, molecular properties and functional impact Article in Anales de la Real Academia Nacional de Farmacia 73(2) January with 36.
On the history of ecto-ATPases: The role of W. Engelhardt more than ten ectonucleotidases, including ecto-ATPases, were cloned from the mammalian genome [7, 8]. the thesis of this book Author: Sergei N Orlov. Ectonucleotidases produce key molecules for purine salvage and consequent replenishment of ATP stores within multiple cell types.
Dephosphorylated nucleoside derivatives interact with membrane transporters to enable intracellular uptake. Ectonucleotidases modulate P2 purinergic signaling. In addition, ectonucleotidases generate extracellular adenosine, which.
On the history of ecto-ATPases: The role of W. Engelhardt. Orlov SN 1 At the same time, more than ten ectonucleotidases, including ecto-ATPases, Lemmens R (eds) Ecto-ATPases and related ectonucleotidases.
Shaker, Maastricht, pp 1–8. Background and purpose: ARL6-N,N-Diethyl-D-β-γ-dibromomethylene adenosine triphosphate, originally named FPLis the only commercially available inhibitor of the first report on this molecule, various ectonucleotidases responsible for the hydrolysis of ATP at the cell surface have been cloned and by: Jürgen Schnermann, Josephine P.
Briggs, in Molecular and Genetic Basis of Renal Disease, Adenosine. Adenosine exported from cells by equilibrative nucleoside transporters or generated in the extracellular space by ecto-ATPases and nucleotidases exerts its effects through four types of G protein–coupled receptors.
Mice with null mutation of the A2a adenosine. R (eds) Ecto-ATPases and related ectonucleotidases. Shaker, Maastricht, pp 1–8 8.
Robson SC, Sevigny J, Zimmerman H () The E-NTPDase family of ecto-nucleotidases: structure function relationships and pathophysiological significance. Purinergic Signalling – 9. Engelhardt WA () Pyrophosphate metabolism in avian erythrocytes.
Zimmermann H, Beaudoin AR, Bollen M, Goding JW, Guidotti G, Kirley TL, et al., editors. Proposed nomenclature for two novel nucleotide hydrolyzing enzyme families expressed on the cell surface. Ecto-ATPases and Related Ectonucleotidases; ; Diepenbeek: Shaker Publishing BV, Maastricht. Google Scholar.
DEPRETER, LM, T WALKER, K DE SMET, B DE PREST, and Frank Roels. “Localization of ATP, ADP and AMP Hydrolysing Enzyme Activities as a Tool to Assess Hepatocyte Polarity.” In Ecto-ATPases and Related Ectonucleotidases, 61– Maastricht: by: 1.
Vlajkovic SM; Housley GD; Christie DL; Greenwood D; Nikolic P; Beaudoin AR; Thorne PR,'The role of Ecto-NTPDases in Cochlear Function', in Vanduffel L; Lemmens R (ed.), Ecto-ATPases and Related Ectonucleotidases Proceedings of the Second International Workshop on Ecto-ATPases and Related Ecotonucleotidases, Held in Diepenbeek, Belgium.
The extracellular ATPase (ecto-ATPase) is a divalent cation-dependent nucleoside triphosphatase with an unusually high specific activity. Monoclonal antibodies, described previously [Stout, J. G., Strobel, R.
S., & Kirley, T. () J. Biol. Chem.−], and newly generated polyclonal antibodies, both raised against the chicken gizzard ecto-ATPase, were evaluated Cited by: Germline deletion of the nucleoside triphosphate pyrophosphohydrolase (NTPPPH) plasma cell membrane glycoprotein (PC-1) produces abnormal calcification of periarticular tissues.
- Proceedings of the second international workshop on ecto-ATPases and related ectonucleotidases, Maastricht Holland.Cited by: To confirm that this Mg-dependent ATPase was an ecto-ATPase, we used an impermeant inhibitor, 4,4′-diisothiocyanostylbene 2′,2′-disulfonic acid as well as suramin, an antagonist of P 2 purinoreceptors and inhibitor of some ecto-ATPases.
These two reagents inhibited the Mg 2+-dependent ATPaseCited by:. Books Go Search Hello Select your address Best Sellers Customer Service New Releases Find a Gift Whole Foods Registry Gift Cards Sell AmazonBasics #FoundItOnAmazon Free Shipping Shopper Toolkit.The ecto-nucleotidases are important for the regulation of many physiological and pathological signaling processes under purinergic signaling control, including pain perception and maintenance of hemostasis via hydrolysis of the platelet activator, ADP.Zimmermann H, Beaudoin AR, Bollen M, Goding JW, Guidotti G, Kirley TL, Robson SC, Sano K.
Proposed nomenclature for two novel nucleotide hydrolyzing enzyme families expressed on the cell surface. In Vanduffel L, Lemmens R. Proceedings of the Second International Workshop on Ecto-ATPases and Related Ectonucleotidases.