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  Sensitivity of rat renal luminal and contraluminal sulfate transport systems to DIDS

Bästlein, C., & Burckhardt, G. (1986). Sensitivity of rat renal luminal and contraluminal sulfate transport systems to DIDS. American Journal of Physiology-Renal Physiology, 250(2 Pt 2), F226-F234. doi:10.1152/ajprenal.1986.250.2.F226.

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Bästlein, Christiane1, Author              
Burckhardt, Gerhard1, Author              
Affiliations:
1Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              

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 Abstract: 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) was tested as an inhibitor of the sulfate transport systems in rat renal brush border and basolateral membrane vesicles. Na+-driven sulfate uptake into brush border membrane vesicles was half-maximally inhibited at 350 microM DIDS. Proton gradient-driven sulfate uptake into basolateral membrane vesicles was competitively inhibited by DIDS with a Ki of 2.4 microM. The Km for delta pH-driven sulfate uptake was 5.4 microM. The different affinities of the sulfate transport systems for DIDS correlated with different substrate specificities. The luminal transport system accepted a smaller range of anions than the contraluminal system and did not operate as a Na+-independent anion exchanger. After treatment of basolateral membrane vesicles with 50 microM DIDS at pH 8.4 for 30 min, an irreversible inhibition of sulfate uptake was observed. With brush border membranes, only a small irreversible inhibition was obtained. Lack of inhibition after treatment of basolateral membranes with DIDS at pH 6.4 indicated that DIDS reacted with deprotonated amino groups of the transport protein. Sulfate was protected from the irreversible inhibition by DIDS. Sodium-driven uptake of L-glutamate and methylsuccinate into basolateral membrane vesicles was not irreversibly inhibited by DIDS, indicating a specific action of DIDS on the contraluminal sulfate transport system. Irreversible and substrate-protectable inhibition of sulfate transport render DIDS suitable for future affinity labeling studies on the sulfate transport system in basolateral membranes.

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Language(s): eng - English
 Dates: 1984-12-111985-08-161986-02-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1152/ajprenal.1986.250.2.F226
PMID: 3946600
 Degree: -

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Title: American Journal of Physiology-Renal Physiology
  Other : Am. J. Physiol. Renal Physiol.
Source Genre: Journal
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Publ. Info: Bethesda, Md. : American Physiological Society.
Pages: - Volume / Issue: 250 (2 Pt 2) Sequence Number: - Start / End Page: F226 - F234 Identifier: ISSN: 0363-6127
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000238890