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Investigating the potassium interactions with the palytoxin induced channels in Na+/K+ pump

Paper ID Volume ID Publish Year Pages File Format Full-Text
15424 1412 2009 8 PDF Available
Title
Investigating the potassium interactions with the palytoxin induced channels in Na+/K+ pump
Abstract

K+ has been appointed as the main physiological inhibitor of the palytoxin (PTX) effect on the Na+/K+ pump. This toxin acts opening monovalent cationic channels through the Na+/K+ pump. We investigate, by means of computational modeling, the kinetic mechanisms related with K+ interacting with the complex PTX–Na+/K+ pump. First, a reaction model, with structure similar to Albers–Post model, describing the functional cycle of the pump, was proposed for describing K+ interference on the complex PTX–Na+/K+ pump in the presence of intracellular ATP. A mathematic model was derived from the reaction model and it was possible to solve numerically the associated differential equations and to simulate experimental maneuvers about the PTX induced currents in the presence of K+ in the intra- and extracellular space as well as ATP in the intracellular. After the model adjusting to the experimental data, a Monte Carlo method for sensitivity analysis was used to analyze how each reaction parameter acts during each experimental maneuver involving PTX. For ATP and K+ concentrations conditions, the simulations suggest that the enzyme substate with ATP bound to its high-affinity sites is the main substate for the PTX binding. The activation rate of the induced current is limited by the K+ deocclusion from the PTX–Na+/K+ pump complex. The K+ occlusion in the PTX induced channels in the enzymes with ATP bound to its low-affinity sites is the main mechanism responsible for the reduction of the enzyme affinity to PTX.

Keywords
Palytoxin; Na/K-ATPase; Potassium interactions; Reaction model; Computational simulation
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Investigating the potassium interactions with the palytoxin induced channels in Na+/K+ pump
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Publisher
Database: Elsevier - ScienceDirect
Journal: Computational Biology and Chemistry - Volume 33, Issue 1, February 2009, Pages 14–21
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us