1: Nippon Rinsho. 1996 Mar;54(3):586-94.


[Na, K-ATPase--its structure, function and intracellular transport]

[Article in Japanese]

Omori K, Matsuda H.

Department of Physiology, Kansai Medical University, Japan.

Na, K-ATPase is an integral plasma membrane protein and plays essential roles such as maintaining sodium and potassium ion gradients across the plasma membrane. The enzyme consists of the alpha and the beta subunits with the stoichiometry of one to one. Three alpha subunit and two beta subunit isoforms have been detected in animal cells with the tissue-specific expression of both subunits. Recent advances in molecular biological studies on the Na, K-ATPase enable us to understand the structure-function relationships and mechanisms of intracellular transport of the enzyme. In this article we review the findings deduced from these studies, especially on the assembly and transport to the plasma membrane of the alpha and beta subunits.

Publication Types:
English Abstract
Review

PMID: 8904209 [PubMed - indexed for MEDLINE]

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2: Nippon Rinsho. 1993 Jun;51(6):1496-503.


[Na, K-ATPase--its structure, gene isoforms, and possible roles in cardiac cells]

[Article in Japanese]

Nagano K, Kawakami K.

Department of Biology, Jichi Medical School.

A short history of the study of Na, K-ATPase, the Na- and K-transporting enzyme of animal cell membranes, and its present state of investigation are described. Parallelism between the enzyme activity and sodium flux across the cell membrane, subunit constitution and characteristic distribution among different tissues, isoform gene structures and regulation of their specific expression, and especially the inhibition of the enzyme by ouabain are discussed in relation to cardiac functions.

Publication Types:
English Abstract
Review

PMID: 8391593 [PubMed - indexed for MEDLINE]

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3: Nauchnye Doki Vyss Shkoly Biol Nauki. 1990;(6):120-31.


[Concepts of the oligomeric structure and function of Na, K-ATPase based on the results of studying ligand binding and of determining the size of the molecular target]

[Article in Russian]

Norby JG.

This review is devoted to the discussion of the sizes and molecular structure of the minimal functional unit of Na, K-ATPase. Special attention is paid to the data obtained by radiation inactivation method and studies on ligand binding. The model for the stepwise radiation inactivation of Na, K-ATPase is proposed. The conclusion is drawn that Na, K-ATPase has a dimeric structure, the interactions between its alpha-subunits stabilize the quaternary structure of the pump. Functionally, each alpha-subunit in a stabilized structure possesses a full hydrolytic activity.

Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review

PMID: 2169909 [PubMed - indexed for MEDLINE]

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4: Tanpakushitsu Kakusan Koso. 1988 Oct;33(13):2371-81.


[Structure of ion transport ATPase--progress in active site structure and primary structure of Na+, K+-ATPase]

[Article in Japanese]

Ohta T.

Publication Types:
Review

PMID: 2854641 [PubMed - indexed for MEDLINE]

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5: Biochim Biophys Acta. 1985 Dec 9;822(3-4):319-34.


Interaction of (Na+ + K+)-ATPase with artificial membranes. I. Formation and structure of (Na+ + K+)-ATPase-liposomes.

Anner BM.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 2998473 [PubMed - indexed for MEDLINE]

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6: Tanpakushitsu Kakusan Koso. 1983 Sep;28(10):1121-30.


[Structure of Na+, K+-ATPase]

[Article in Japanese]

Kawamura M, Oota T, Nagano K.

Publication Types:
Review

PMID: 6314433 [PubMed - indexed for MEDLINE]

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7: Biochim Biophys Acta. 1982 Aug 11;694(1):27-68.


Mechanism of the Na+, K+ pump. Protein structure and conformations of the pure (Na+ +K+)-ATPase.

Jørgensen PL.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 6289898 [PubMed - indexed for MEDLINE]