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Recent data on characteristics of the structure, functions, and main properties of ankyrins (proteins that are linkers between the spectrin-based cytoskeleton and integral membrane proteins) are summarized. The interactions of ankyrins with band-3 protein, P-type ATPases, ion channels, receptors, and protein kinase C are considered. The structure of ankyrin(More)
Na,K-ATPase is highly sensitive to changes in the redox state, and yet the mechanisms of its redox sensitivity remain unclear. We have explored the possible involvement of S-glutathionylation of the catalytic α subunit in redox-induced responses. For the first time, the presence of S-glutathionylated cysteine residues was shown in the α subunit in duck salt(More)
The decrease in the oxygen content of tissues, which is observed in a number of pathological processes, inevitably leads to damage. One of the main causes of cell damage and death in hypoxia is the failure of the systems that maintain the ionic balance. Na,K-ATPase is the main ion-transporting protein in the plasma membrane of animal cells, and its(More)
Previously, we reported that ouabain and other cardiotonic steroids (CTS) kill renal epithelial and vascular endothelial cells via their interaction with the Na+,K+-ATPase alpha-subunit, but independently of elevation of the [Na+]i/[K+]i ratio. In distinct cell types, side-by-side with inhibition of Na+,K+-ATPase-mediated ion fluxes, CTS trigger [Ca2+]i(More)
Active transport of sodium and potassium ions by Na,K-ATPase is accompanied by the enzyme conformational transition between E1 and E2 states. ATP and ADP bind to Na,K-ATPase in the E1 conformation with similar affinity but the properties of enzyme in complexes with these nucleotides are different. We have studied thermodynamics of Na,K-ATPase binding with(More)
Recently, we reported that ouabain kills renal epithelial and vascular endothelial cells independently of elevation of the [Na(+)](i)/[K(+)](i) ratio. These observations raised the possibility of finding cardiotonic steroids (CTS) that inhibit the Na(+),K(+) pump without attenuating cell survival and vice versa. To test this hypothesis, we compared CTS(More)
Some mechanisms of regulation of Na,K-ATPase activity in various tissues including the phosphorylation of the catalytic subunit of the enzyme by different protein kinases (PKA, PKC, and tyrosine kinase) and the interaction of the alpha-subunit with different proteins (Na,K-ATPase beta- and gamma-subunits, ankyrin, phosphoinositide-3 kinase, and AP-2(More)
Low molecular mass proteins of the FXYD family that affect the sensitivity of Na,K-ATPase to Na+ and K+ are known to be present in Na,K-ATPases in various tissues. In particular, in Na,K-ATPase from kidney a gamma-subunit (with electrophoretic mobility corresponding to molecular mass of about 10 kD) is present, and Na,K-ATPase preparations from heart(More)
The N-terminal sequences of the alpha and beta subunits from the Na/K-ATPase of duck salt gland have been determined by automated Edman degradation chemistry. These sequences were compared to sequences previously reported for Na/K-ATPase subunits from other sources in order to determine the subunit isoform composition of the salt gland enzyme. The(More)
Ca,phospholipid-dependent (PKC) and cAMP-dependent (PKA) protein kinases phosphorylate the alpha-subunit of the Na,K-ATPase from duck salt gland with the incorporation of 0.3 and 0.5 mol 32P/mol of alpha-subunit, respectively. PKA (in contrast to PKC) phosphorylates the alpha-subunit only in the presence of detergents. Limited tryptic digestion of the(More)