Na,K-ATPase function

Jorgensen, P.L., Hakansson, K.O., Karlish, S.J.D. (2003) Structure and mechanism of Na,K-ATPase functional sites and their interactions. Annu. Rev. Physiol. 65, 817-849. 

In spite of the experimental evidence, the role of the Na-K-ATPase in the formation of the palytoxin channel has not been clarified in detail. The recent advances in the understanding of the Na-K-ATPase function have recently allowed Artigas and Gadsby (2003) to postulate that palytoxin could disrapt the strict coupling between the pump s inner and outer gates, allowing them to both be open. Thus, it is not clear whether the paly toxin-sensitive chaimel is located within the enzyme and the step(s) in the normal functioning of the pump(s) that are affected by palytoxin remain to be elucidated. 

Chlordane blocks the neuronal uptake of chloride ions by blocking the activity of y-amino butyric acid. This results in only a partial depolarization of activated neurons leading to an uncontrolled excited condition. Additionally, chlordane inhibits Ca, Mg -adenosine triphosphate (ATPase) and Na, K -ATPase functions, leading to increased concentrations of intracellular free calcium in neurons and the release of neurotransmitters. This neurotransmitter release potentiates depolarization of adjacent neurons in a chain reaction manner, propagating stimuli through the central nervous system (CNS). 

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See also in sourсe #XX -- [ , ]

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