Universität zu Köln

Schulz, Christian, Fork, Christian, Bauer, Tim, Golz, Stefan, Geerts, Andreas, Schoemig, Edgar and Gruendemann, Dirk (2014). SLC22A13 catalyses unidirectional efflux of aspartate and glutamate at the basolateral membrane of type A intercalated cells in the renal collecting duct. Biochem. J., 457. S. 243 - 262. LONDON: PORTLAND PRESS LTD. ISSN 1470-8728

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Abstract

In vertebrates, SLC22A13 is an evolutionarily conserved transport protein of the plasma membrane. In humans and rat, it is principally expressed in the kidney. The precise localization and physiological function are unknown. In the present study, immunohistochemistry revealed that expression of SLC22A13 is confined to the basolateral membrane of type A intercalated cells in rat kidney. Double-staining confirmed that SLC22A13 co-localizes with anion exchanger 1. LC-MS difference shading showed that heterologous expression of human and rat SLC22A13 in HEK (human embryonic kidney)-293 cells stimulates efflux of guanidinosuccinate, aspartate, glutamate and taurine. Time courses of uptake of [H-3]aspartate and [H-3]glutamate revealed that SLC22A13 counteracted endogenous uptake. By contrast, OAT2 (organic anion transporter 2), a bidirectional glutamate transporter, increased accumulation of [H-3]glutamate. Thus SLC22A13 catalyses unidirectional efflux. Velocity of efflux of standard amino acids was measured by LC-MS/MS. Expression of SLC22A13 strongly stimulated efflux of aspartate, taurine and glutamate. When the intracellular concentrations of aspartate and taurine were increased by pre-incubation, velocities of efflux increased linearly. We propose that in type A intercalated cells, SLC22A13 compensates luminal exit of protons by mediating the basolateral expulsion of the anions aspartate and glutamate. In this context, unidirectional efflux is essential to avoid anion reentering. Loss of SLC22A13 function could cause distal tubular acidosis.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Schulz, Christian UNSPECIFIED UNSPECIFIED UNSPECIFIED Fork, Christian UNSPECIFIED UNSPECIFIED UNSPECIFIED Bauer, Tim UNSPECIFIED UNSPECIFIED UNSPECIFIED Golz, Stefan UNSPECIFIED UNSPECIFIED UNSPECIFIED Geerts, Andreas UNSPECIFIED UNSPECIFIED UNSPECIFIED Schoemig, Edgar UNSPECIFIED UNSPECIFIED UNSPECIFIED Gruendemann, Dirk UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-448456
DOI:	10.1042/BJ20130654
Journal or Publication Title:	Biochem. J.
Volume:	457
Page Range:	S. 243 - 262
Date:	2014
Publisher:	PORTLAND PRESS LTD
Place of Publication:	LONDON
ISSN:	1470-8728
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language RETICULUM-ASSOCIATED DEGRADATION; ENDOPLASMIC-RETICULUM; CAENORHABDITIS-ELEGANS; PROTEIN; P97; COMPLEX; ER; STRESS; TRANSLOCATION; DISLOCATION Multiple languages Biochemistry & Molecular Biology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/44845