Cation Selectivity of Gastric H,K-ATPase and Na,K-ATPase Chimeras
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چکیده
منابع مشابه
Cation selectivity of gastric H,K-ATPase and Na,K-ATPase chimeras.
Chimeras of the catalytic subunits of the gastric H,K-ATPase and Na, K-ATPase were constructed and expressed in LLC-PK1 cells. The chimeras included the following: (i) a control, H85N (the first 85 residues comprising the cytoplasmic N terminus of Na,K-ATPase replaced by the analogous region of H,K-ATPase); (ii) H85N/H356-519N (the N-terminal half of the cytoplasmic M4-M5 loop also replaced); a...
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The hitherto unknown NT-regulated mechanism of NaK-ATPase localized in the nerve ending membranes is found. The mechanism certainly has a functional significance and must be involved in the regulation – modulation of chemical synaptic transmission. On the other hand , the availability of the discovered specific protein, regulators (SFa and SFi) of synaptic origin, makes it possible to consider ...
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PURPOSE To localize NaK ATPase sites on cultured human retinal pigment epithelium (RPE). METHODS Cultured human RPE from fetal, 2-year-old, and 21-year-old donors was grown to confluence in microporous culture wells for 4 months to 2 years, mounted in a small-volume Ussing chamber, and perfused with growth medium. Ouabain (10(-5)-M) was applied to the basal and apical sides of the RPE. Change...
متن کاملCryo-EM structure of gastric H+,K+-ATPase with a single occupied cation-binding site.
Gastric H(+),K(+)-ATPase is responsible for gastric acid secretion. ATP-driven H(+) uptake into the stomach is efficiently accomplished by the exchange of an equal amount of K(+), resulting in a luminal pH close to 1. Because of the limited free energy available for ATP hydrolysis, the stoichiometry of transported cations is thought to vary from 2H(+)/2K(+) to 1H(+)/1K(+) per hydrolysis of one ...
متن کاملThe parietal cell gastric H, K-ATPase also functions as the Na, K-ATPase and Ca-ATPase in altered states
This article offers an explanation for the apparent lack of Na, K-ATPase activity in parietal cells although ouabain has been known to inhibit gastric acid secretion since 1962. The gastric H, K-ATPase (proton-pump) seems to be acting in altered states, thus behaving like a Na, K-ATPase (Na-pump) and/or Ca-ATPase (Ca-pump) depending on cellular needs. This conclusion is based on the following ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1999
ISSN: 0021-9258
DOI: 10.1074/jbc.274.26.18374