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  Cloning of a membrane-associated protein which modifies activity and properties of the Na+-D-glucose cotransporter

Veyhl, M., Spangenberg, J., Püschel, B., Poppe, R., Dekel, C., Fritzsch, G., et al. (1993). Cloning of a membrane-associated protein which modifies activity and properties of the Na+-D-glucose cotransporter. Journal of Biological Chemistry, 268(33), 25041-25053. doi:10.1016/S0021-9258(19)74569-4.

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Veyhl, Maike1, Author           
Spangenberg, Jörg1, Author           
Püschel, Bernd1, Author           
Poppe, Robert1, Author           
Dekel, Carmela1, Author           
Fritzsch, Günter2, Author           
Haase, Winfried1, Author           
Koepsell, Hermann1, Author           
1Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              


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 Abstract: An expression library from porcine kidney cortex was screened with a monoclonal antibody (R4A6) which stimulates high-affinity phlorizin binding in kidney and intestine but does not react with the membrane protein (SGLT1) which mediates Na+-coupled transport of D-glucose (Hediger, M.A., Coady, M.J., Ikeda, T.S., and Wright, E.M. (1987) Nature 330, 379-381). A cDNA (RS1) was obtained which codes for a hydrophilic Mr 66,832 polypeptide and contains a predicted hydrophobic alpha-helix at the COOH terminus. After expression in Xenopus oocytes RS1 protein was found associated with the plasma membrane. RS1-homologous mRNAs were detected in renal outer cortex and outer medulla, small intestine, liver, and LLCPK1 cells, but not in skeletal muscle, heart muscle, Madin-Darby canine kidney (MDCK) cells, renal inner medulla, and Xenopus oocytes. After nondenaturing gel electrophoresis of renal brush-border membranes comigration of RS1- and SGLT1-homologous proteins as a high molecular weight complex was demonstrated. RS1 altered the expression of Na+-glucose cotransport by SGLT1 in Xenopus oocytes. There was no effect on the expression of the nonhomologous transporters for Na+-gamma-aminobutyric acid cotransport and for Na+-independent glucose transport. However, RS1 also changed the expression of the SGLT1-homologous Na+-myo-inositol cotransporter from MDCK cells. The Vmax of methyl-alpha-D-glucopyranoside (AMG) transport expressed after injection of a small amount of SGLT1-cRNA was increased 40-fold when a stoichiometric amount of RS1-cRNA was coinjected. In addition the voltage and glucose dependence of expressed AMG uptake and the concentration dependence of transport inhibition by phlorizin were changed when stoichiometric amounts of RS1-cRNA were coinjected with SGLT1-cRNA. Thus with SGLT1 one apparent transport site (K0.5 about 100 microM) and one apparent phlorizin inhibition site (Ki about 5 microM) was observed whereas with SGLT1 plus RS1 two apparent transport sites (K0.5(1) about 20 microM, K0.5(2) about 1 mM) and two apparent phlorizin inhibition sites (Ki(1) about 0.3 microM, Ki(2) about 30 microM) were found as has been described in brush-border membrane vesicles of kidney and intestine (see e.g. Koepsell, H., Fritzsch, G., Korn, K., and Madrala, A. (1990) J. Membr. Biol. 114, 113-132). The data suggest that the Na+-D-glucose cotransporter and possibly also other SGLT1-type Na+-cotransporters contain RS1-type regulatory subunits.


Language(s): eng - English
 Dates: 1993-07-021993-03-232021-01-041993-11-25
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0021-9258(19)74569-4
PMID: 8227068
 Degree: -



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Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 268 (33) Sequence Number: - Start / End Page: 25041 - 25053 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826