NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes.

NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes. Research Abstract Details 

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NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes. Abstract Text:

Wanyoike Kang'ethe,Karlygash G Aimanova,Ashok K Pullikuth,Sarjeet S Gill,

Following a blood meal, the mosquito Aedes aegypti will have acquired an enormous sodium load that must be rapidly excreted to restore ion homeostasis. It is a process that demands robust sodium and fluid transport capabilities. Even though the identities of the components involved in this ion transport across the mosquito Malpighian tubule epithelia have not been completely determined, electrophysiological studies suggest the contribution of a Na(+)/H(+) exchanger extruding cations into the lumen driven secondarily by the proton gradient created by the V-type H(+)-ATPase in the tubules' apical membrane. We have identified the putative exchanger and designated it AeNHE8. Immunolocalization studies demonstrated that AeNHE8 is expressed in the apical membranes of Malpighian tubules, gastric caecae, and rectum. When heterologously expressed in salt-sensitive yeast cells lacking Na(+) extrusion and Na(+)/H(+) exchange proteins, AeNHE8 rescues the salt-sensitive phenotype and restores the cells' ability to grow in high NaCl media. Furthermore, heterologous expression of AeNHE8 in NHE-deficient fibroblast cells results in an amiloride-sensitive (22)Na(+) uptake. To determine the exchanger's kinetic properties, we reconstituted membranes from yeast cells expressing the protein into lipid proteoliposomes and assayed for cation-dependent H(+) exchange by fluorimetric methods. Our results indicate that AeNHE8 mediates saturable exchange of Na(+) and K(+) for H(+). We propose that AeNHE8 may be coupled to the inward H(+) gradient across the Malpighian tubules and plays a role in the extrusion of excess sodium and potassium while maintaining steady intracellular pH in the principal cells.

NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes. Publishing Authors By Initials

W Kang'ethe,KG Aimanova,AK Pullikuth,SS Gill,

For similar proteins: carrier proteins: membrane transport proteins: ion pumps: antiporters: sodium-hydrogen antiporter research abstracts see: proteins: carrier proteins: membrane transport proteins: ion pumps: antiporters: sodium-hydrogen antiporter research

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NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: American journal of physiology. Renal physiology

VOLUME: 292

Page Numbers: F1501-12

Journal Abbreviation:

ISSN: 0363-6127

DAY: 6

MONTH: 02

YEAR: 2007

NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 100901990

NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes. Keywords Mesh Terms:

KEYWORDS: Sodium-Hydrogen Antiporter

MESH TERMS: physiology

Chemical & Substance for Abstract: NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes. Information

Substance Name: Sodium

Registry Number: 7440-23-5

Grant and Affiliation Information for NHE8 mediates amiloride-sensitive Na+/H+ exchange across mosquito Malpighian tubules and catalyzes Na+ and K+ transport in reconstituted proteoliposomes.

AFFILIATION: Graduate Program in Environmental Toxicology, University of California, Riverside, California 92521, USA.

Country: United States

AGENCY: United States NIAID

GRANT: AI-32572

ACRONYM: AI

MEDLINETA: Am J Physiol Renal Physiol

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