By K. Kawakami, Y. Suzuki-Yagawa, Y. Watanabe, K. Ikeda, K. Nagano (auth.), Prof. Dr. Ernst Bamberg, Prof. Dr. Wilhelm Schoner (eds.)

ISBN-10: 3642725112

ISBN-13: 9783642725111

ISBN-10: 3642725139

ISBN-13: 9783642725135

The sodium of animal mobilephone membranes converts the chemical power got from the hydrolysis of adenosine five' -triphosphate right into a circulation of the cations Na + and ok + opposed to an electrochemical gradient. The gradient is used subse­ quently as an strength resource to force the uptake of metabolic substrates in polar epithelial cells and to take advantage of it for reasons of communications in excitable cells. The organic value of the sodium pump is clear from the truth that be­ tween 20-70% of the cell's metabolic power is ate up for the pumping professional­ cess. in addition, the sodium pump is a vital organic procedure excited by regulatory methods just like the upkeep of the cells' and organism's water me­ tabolism. it really is accordingly comprehensible that specific mobile calls for are han­ dled greater by means of particular isoforms of the sodium pump, that the expression of the sodium pump and their isoforms is regulated via hormones as is the task of the sodium pump through hormone-regulated protein kinases. also, the sodium pump itself looks a receptor for a putative new workforce of hormones, the endogenous digitalis-like components, which nonetheless must be outlined more often than not of their constitution. This staff of drugs has its chemically renowned coun­ terpart in steroids from plant and toad starting place that are generally called "car­ diac glycosides". they're in clinical use when you consider that a minimum of two hundred years in medication within the remedy of middle diseases.

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Read e-book online The Sodium Pump: Structure Mechanism, Hormonal Control and PDF

The sodium of animal mobile membranes converts the chemical strength received from the hydrolysis of adenosine five' -triphosphate right into a circulation of the cations Na + and ok + opposed to an electrochemical gradient. The gradient is used subse­ quently as an strength resource to force the uptake of metabolic substrates in polar epithelial cells and to exploit it for reasons of communications in excitable cells.

Extra info for The Sodium Pump: Structure Mechanism, Hormonal Control and its Role in Disease

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The phosphorylation of the a-subunit by Pi is stimulated by the presence of ouabain. Although it is more difficult to detect, the Na+/K+-AlPase from the uninfected Sf-9 cells has an identical pattern of phosphorylation (Fig. 4B). The insect Na+/K+-AlPase a-subunit is phosphorylated only in the presence of Na+; EGTA does not affect the Na+dependent phosphorylation and Mg2+ alone cannot support phosphorylation. A completely different type of a-subunit phosphorylation is seen when the a-subunit is expressed in the Ilbsence of the S-subunit (Fig.

5). As shown, phosphorylation of the a-subunit can occur with only Mg2+ present. This Mg2+-dependent phosphorylation is not inhibited by ouabain. however, 150 mM Tris+, K+ or Na+ greatly reduce phosphorylation. The lack of inhibition by ouabain is consistent with the finding that 3H-ouabain does not bind to the unassociated a-subunit (15; unpublished results). The S-independent phosphorylation of the a-subunit is not restricted to the al isoform as both a2 and a3 exhibit identical Mg2+-dependent phosphorylation (data not shown).

Akira Ishiharna for discussion and critical reading of the manuscript. This work was supported by grants from the Ministry of Education, Science and Culture of Japan. References 1. 2. 3. 36 Davis RL, Cheng P-F. Lassar AB. Weintraub H (1990) The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation. Cell 60: 733-746 Herschlag D. Johnson FB (1993) Synergism in transcriptional activation: a kinetic view. Genes Dev 7: 173-179 Orlowski J. Lingrel IB (1988) Tissue-specific and developmental regulation of rat Na,K-ATPase catalytic a.

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The Sodium Pump: Structure Mechanism, Hormonal Control and its Role in Disease by K. Kawakami, Y. Suzuki-Yagawa, Y. Watanabe, K. Ikeda, K. Nagano (auth.), Prof. Dr. Ernst Bamberg, Prof. Dr. Wilhelm Schoner (eds.)


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