3 edition of Na/K-Atpase and Related Transport Atpases found in the catalog.
by New York Academy of Sciences
Written in English
|Contributions||Luis A. Beauge (Editor), David C. Gadsby (Editor), Patricio J. Garrahan (Editor)|
|The Physical Object|
|Number of Pages||850|
The cell membrane Na,K-ATPase is a member of the P-type family of active cation transport proteins. Recently the molecular structure of the related sarcoplasmic reticulum Ca-ATPase in an E conformation has been determined at Å resolution. Furthermore, theoretical models of the Ca-ATPase in E conformations are available. As a result of these developments, these structural data have allowed. Start studying Cell Membrane Channels and Na+/K+ ATPase. Learn vocabulary, terms, and more with flashcards, games, and other study tools.
Exploring the Mechanism of Lipid Transport by a Flippase ATP-dependent flippases art closely related in their structures to ion pumps like the plasma membrane Na +, K +-ATPase and sarcoplasmic reticulum Ca 2+-ATPase, but they contend with a novel dilemma not shared by the ion transport systems. Consult the following reference and. summarize the. The Na + /K + ATPase pump is a pump found in the membrane of animal cell which uses the hydrolysis of ATP to pump 3Na + out of the cell and 2K + into the is a primary active transport and belongs to the family of P-type regulates the osmolarity of the cytosol by controlling the solute concentration inside the main function of the N+/K+ ATPase pump is to maintain.
The Na +/K -ATPase is the receptor of digitalis steroids used to treat heart failure. Na+/K+-ATPase is one of a family of cation pumps, the P-type ATPases, which includes also sarcoplasmic reticulum Ca2+-ATPase, gastric cell membrane H +/K -ATPase, plasma membrane Ca2+-ATPase, plant cell membrane H+-ATPase, heavy metal-dependentFile Size: KB. The Na +,K +-ATPase and the H +,K +-ATPases are closely related members of the P-type family of ion transporting ATPases. Despite their homology, these pumps are sorted to different domains in polarized epithelial cells, and their enzymatic activities are subject to .
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Na⁺/K⁺-ATPase (sodium–potassium adenosine triphosphatase, also known as the Na⁺/K⁺ pump or sodium–potassium pump) is an enzyme (an electrogenic transmembrane ATPase) found in the membrane of all animal cells. It performs several functions in cell physiology. The Na + /K +-ATPase enzyme is active (i.e.
it uses energy from ATP).For every ATP molecule that the pump uses, three BRENDA: BRENDA Na/K-Atpase and Related Transport Atpases book. COVID Resources. Reliable information about the coronavirus (COVID) is available from the World Health Organization (current situation, international travel).Numerous and frequently-updated resource results are available from this ’s WebJunction has pulled together information and resources to assist library staff as they consider how to handle coronavirus.
The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of Na + /K + + /K +-ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma gradients are essential for osmoregulation, for sodium-coupled transport of a variety Aliases: ATP1A1, ATPase, Na+/K+ transporting, alpha 1.
P-type ATPases: These all form phosphorylated intermediates in the pump mechanism, like that shown for the Na,K-ATPase in Figure Among these are gastric H +-ATPase that is responsible for acidification of the stomach contents; Na +,K +-ATPase that is responsible for maintaining ionic gradients in most cells; PMCA (for plasma membrane calcium ATPase) responsible for pumping Ca 2+ out of.
The Na +, K +-ATPase (NKA) is an ubiquitous enzyme consisting of α, β and γ subunits, and is responsible for the creation and maintenance of the Na + and K + gradients across the cell membrane by transporting 3 Na + out and 2 K + into the cell. Sodium pump regulation is tissue as well as isoform specific.
Intracellular messengers differentially regulate the activity of the individual NKA Cited by: 1 Na,K-ATPaseandRelatedP-typeTransportATPases:Structure, Biology,andMedicine.
GeoffreyHunt 2 GolgiCalciumPumpSecretoryPathwayCalciumATPase1 (SPCA1. NA/K-ATPASE AND RELATED TRANSPORT ATPASES: Editors: LA Beauge, DC Gadsby, PJ Garrahan: Place of Publication: NEW YORK: Publisher: New York Academy of Sciences: Pages: Number of pages: 3: ISBN (Print) Publication status: Published - Event: VIIIth International Conference on the Na/K-ATPase (and Related Transport Cited by: 3.
The Na,K-ATPase consists of two membrane spanning polypeptides, an alpha-subunit of kD and a beta-subunit, which is a glycoprotein of kD. The catalytic properties are associated with the alpha-subunit, which has the binding domain for ATP and the by: (1) and may also be coexpressed with small ion transport regulators of the FXYD family (2,3).
Individual genes of four ﬁ-subunit isoforms and at least three ﬂ-subunit isoforms of Na,K-ATPase have been identiﬁed in mammals (4,5). The isoforms combine to form a number of Na,K-ATPase isozymes that are expressed in a tissue- and cell File Size: 1MB.
The Na +, K + -ATPase generates and maintains the cell membrane potential and the inward Na + gradient thus generated is utilized by other Na + dependent transport systems for uptake of.
ATP1A3 A gene on chromosome 19q that encodes an enzyme belonging to the family of P-type cation transport ATPases and the subfamily of Na+/K+ -ATPases, the latter of which are responsible for establishing and maintaining electrochemical gradients of Na and K ions across the plasma membrane; they are required for osmoregulation in sodium-coupled transport of various organic and inorganic.
Although the Na,K-ATPase has a pivotal role in Na(+) and K(+) transport in the nervous system, a special role for the glial Na,K-ATPase in clearing extracellular K(+) remains controversial. View. ISBN: OCLC Number: Description: vii, pages: illustrations ; 27 cm.
Contents: A. Ion Pumps. The P-ATPases Superfamily. Na+,K+-ATPase is an ATP-powered ion pump that establishes concentration gradients for Na+ and K+ ions across the plasma membrane in all animal cells by pumping Na+ from the cytoplasm and K+ from the extracellular medium.
This heterodimeric enzyme, a member of P-type ATPases, is composed of a catalytic α-subunit with ten transmembrane domains and a heavily glycosylated auxiliary by: 1. •Type III—Includes plasma membrane H+-ATPases from plants and fungi and Mg2+-ATPases from three bacterial species •Type IV—Includes ATPases have been shown to be involved in the transport of phospholipids.
•Type V—ATPases with unknown specificity. This large group are only found in eukaryotes and are believed to be involved in. To maintain the concentration gradients for Na + and K +, it is necessary to transport Na + out of the cell and K + back into the cell. There is located on the sarcolemma an energy dependent (ATP-dependent) pump system (Na + /K +-ATPase) that that performs this function.
Abstract. Na + /K +-ATPase (NKA), a transmembrane protein, facilitates active transport of three Na + out of the cell and two K + into the cell with the expense of an ATP. It plays an important role in regulating the ionic homeostasis and maintaining membrane potential.
Additionally, NKA plays a crucial role in driving a variety of secondary transport processes such as Na +-dependent glucose Cited by: 4. Na+-K+ ATPase or Na-pump ATPase, a member of “P”-type ATPase superfamily, is characterized by association of multiple isoforms mainly of it’s α- and β- subunits.
At present four different α- (α-1,α-2,α-3 and α-4) and three β- (β-1, β-2, and β-3) isoforms have been identified in mammalian cells and their differential expressions Brand: Springer International Publishing.
P-type ATPases are a large group of evolutionary related ion and lipid pumps that have in common that they catalyze a transient phosphorylated intermediate at a key conserved aspartate residue within the pump in order to function. While all the P-type ATPases perform active transport across cellular membranes, they have different transport specificities and serve diverse physiological functions.
Hebert H, Xian R, Thomsen K, Maunsbach AB () Structure of renal Na,K-ATPase as observed by cryo-EM of 2-D crystals. In: Taniguchi K, Kaya S (eds) Na/K-ATPase and related ATPases.
Elsevier, Amsterdam, pp 43–48 Google ScholarCited by: Purification of Na,K-ATPase expressed in Pichia Pastoris We have expressed the porcine α1/His10β1 subunits in Pichia pastoris (Strugatsky et al., ), a methanotrophic yeast which grows to high cell densities and provides a ready source of recombinant Na+/K+-ATPase.A recent.The Na/K- Atpase and Related Transport Atpases: Structure, Mechanism, and Regulation (Annals of the New York Academy of Sciences) n/a Published by New York Academy of Sciences ().