| pubmed-article:10852908 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0042637 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0017742 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0037473 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0017725 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10852908 | lifeskim:mentions | umls-concept:C0598850 | lld:lifeskim |
| pubmed-article:10852908 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:10852908 | pubmed:dateCreated | 2000-9-25 | lld:pubmed |
| pubmed-article:10852908 | pubmed:abstractText | The Vibrio parahaemolyticus sodium/glucose transporter (vSGLT) is a bacterial member of the SGLT gene family. Wild-type and mutant vSGLT proteins were expressed in Escherichia coli, and transport activity was measured in intact cells and plasma membrane vesicles. Two cysteine-less vSGLT proteins exhibited sugar transport rates comparable with that of the wild-type protein. Six residues in two regions of vSGLT known to be of functional importance in SGLT1 were replaced individually with cysteine in the cysteine-less protein. Characterization of these single cysteine-substituted vSGLTs showed that two residues (Gly-151 and Gln-428) are essential for transport function, whereas the other four residues (Leu-147, Leu-149, Ala-423, and Gln-425) are not. 2-Aminoethylmethanethiosulfonate (MTSEA) blocked Na(+)/glucose transport by only the transporter bearing a cysteine at position 425 (Q425C). MTSEA inhibition was reversed by dithiothreitol and blocked by the presence of both Na(+) and d-glucose, indicating that conformational changes of the vSGLT protein are involved in Na(+)/glucose transport. A split version of vSGLT was generated by co-expression of the N-terminal (N(7)) and C-terminal (C(7)) halves of the transporter. The split vSGLT maintained Na(+)-dependent glucose transport activity. Chemical cross-linking of split vSGLT, with a cysteine in each N(7) and C(7) fragment, suggested that hydrophilic loops between helices 4 and 5 and between helices 10 and 11 are within 8 A of each other. We conclude that the mechanism of Na(+)/glucose transport by vSGLT is similar to mammalian SGLTs and that further studies on vSGLT will provide novel insight to the structure and function of this class of cotransporters. | lld:pubmed |
| pubmed-article:10852908 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10852908 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10852908 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10852908 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10852908 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10852908 | pubmed:author | pubmed-author:WrightE MEM | lld:pubmed |
| pubmed-article:10852908 | pubmed:author | pubmed-author:TuriGG | lld:pubmed |
| pubmed-article:10852908 | pubmed:author | pubmed-author:XieZZ | lld:pubmed |
| pubmed-article:10852908 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10852908 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:10852908 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10852908 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10852908 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10852908 | pubmed:pagination | 25959-64 | lld:pubmed |
| pubmed-article:10852908 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:meshHeading | pubmed-meshheading:10852908... | lld:pubmed |
| pubmed-article:10852908 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10852908 | pubmed:articleTitle | Characterization of the Vibrio parahaemolyticus Na+/Glucose cotransporter. A bacterial member of the sodium/glucose transporter (SGLT) family. | lld:pubmed |
| pubmed-article:10852908 | pubmed:affiliation | Department of Physiology, UCLA School of Medicine, Los Angeles, California 90095-1751, USA. | lld:pubmed |
| pubmed-article:10852908 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10852908 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10852908 | lld:pubmed |
