A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains.

A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains. Research Abstract Details 

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A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains. Abstract Text:

Azad Kumar,Navneet K Tyagi,Enrique Arevalo,Keith W Miller,Rolf K H Kinne,

In order to obtain further information about the structure and function of human sodium/D-glucose cotransporter 1 (hSGLT1), the recombinant protein was subjected, either after reconstitution into liposomes or in its free form, to proteolysis followed by nanoscale microcapillary liquid chromatography electrospray ionization tandem mass spectrometry (LC-MS/MS). The peptides released from SGLT1 proteoliposomes by trypsin bead digestion represented the early N-terminal, loop 7, and loop 9, supporting topology models that place these domains on the extracellular side of the protein. Trypsin bead digestion generated, however, also a number of peptides derived from loop 13 whose topology with regard to the membrane is hitherto a point of debate. Sequence coverage was provided from amino acids 559 to 644, suggesting that loop 13 is almost completely accessible at the extravesicular face of the proteoliposomes. These results support the notion that major parts of loop 13, essential for the interaction with transport inhibitors in vivo, are located extracellularly in intact cells. In-gel trypsin, chymotrypsin, and in particular trypsin/chymotrypsin digestion of recombinant SGLT1 in combination with LC-MS/MS provide extensive sequence coverage of the protein, including domains involved in sugar and inhibitor binding and potential phosphorylation sites. These studies demonstrate that proteomic analysis combined with mass spectrometry is a useful tool to characterize regions of SGLT1 that are important for its function and regulation.

A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains. Publishing Authors By Initials

A Kumar,NK Tyagi,E Arevalo,KW Miller,RK Kinne,

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A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains. Journal Published:

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

Journal: Biochimica et biophysica acta

VOLUME: 1774

Page Numbers: 968-74

Journal Abbreviation: Biochim. Biophys. Acta

ISSN: 0006-3002

DAY: 29

MONTH: 05

YEAR: 2007

A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 217513

A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains. Keywords Mesh Terms:

KEYWORDS: Spectrometry, Mass, Electrospray Ionizat

MESH TERMS: genetics

Chemical & Substance for Abstract: A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains. Information

Substance Name: Sodium-Glucose Transporter 1

Registry Number: 0

Grant and Affiliation Information for A proteomic study of sodium/D-glucose cotransporter 1 (SGLT1): topology of loop 13 and coverage of other functionally important domains.

AFFILIATION: Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, Dortmund 44227, Germany.

Country: Netherlands

AGENCY: United States NIGMS

GRANT: GM 58448

ACRONYM: GM

MEDLINETA: Biochim Biophys Acta

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