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Skip to Search Results- 3Fliegel, Larry
- 1Alvarez, Bernando
- 1Casey, Joseph R.
- 1Coccaro, Ersilia
- 1Dyck, Jason R. B.
- 1Herasymowych, Oksana Sonia.
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2002-01-01
Li, Xiuju J., Alvarez, Bernando, Casey, Joseph R., Reithmeier, Reinhart A. F., Fliegel, Larry
We examined the ability of carbonic anhydrase II to bind to and affect the transport efficiency of the NHE1 isoform of the mammalian Na+/H+ exchanger. The C-terminal region of NHE1 was expressed in Escherichia coli fused with an N-terminal glutathionineS-transferase or with a C-terminal...
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Mitogen-activated protein kinase-dependent activation of the na+/H+ exchanger is mediated through phosphorylation of amino acids ser(770) and ser(771)
Download2007-01-01
Malo, Mackenzie E., Li, Liang, Fliegel, Larry
We investigated regulation of the type 1 isoform of the Na+/H+ exchanger by phosphorylation. Four specific groups of serine and threonine residues in the regulatory carboxyl-terminal tail were mutated to alanine residues: group 1, S693A; group 2, T718A and S723A/S726A/S729A; group 3,...
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Sustained acidosis and phenylephrine activate the myocardial Na+/H+ exchanger through phosphorylation of Ser770 and Ser771
DownloadSpring 2010
The mammalian Na+/H+ exchanger isoform 1 (NHE1) is a ubiquitously expressed membrane protein that regulates myocardial intracellular pH. Inhibition of NHE1 prevents hypertrophy and reduces ischemia-reperfusion (I/R) injury in animal models. To understand the regulation of NHE1 in the myocardium...