Linked Life Data

8163506

Source:http://linkedlifedata.com/resource/pubmed/id/8163506

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1994-5-26
pubmed:databankReference
pubmed:abstractText
We report the primary structure, functional characterization, and tissue distribution of the high affinity Na+/glucose cotransporter SGLT1 from rat kidney. Rat SGLT1 (665 amino acid residues) is 86-87% identical to SGLT1 from rabbit, pig, and human. High stringency Northern analysis demonstrated that SGLT1 is strongly expressed in small intestine and at lower levels in kidney, liver, and lung. In situ hybridization performed on kidney sections revealed that SGLT1 is predominantly present in S3 segments of the proximal tubule. In small intestine, SGLT1 message was located in cells of the lower two-thirds of intestinal villi. Expression of rat SGLT1 in Xenopus oocytes resulted in a large Na(+)-dependent uptake of [14C]-alpha-methyl-D-glucopyranoside (alpha MeGlc). Overall, the transport characteristics were similar to those of rabbit SGLT1. High affinity Na+/glucose cotransport in membrane vesicles was previously shown to be coupled to the cotransport of two Na+ ions (Turner, R. J., and Moran, A. (1982) J. Membr. Biol. 70, 37-45). Previous kinetic analysis of rat and rabbit SGLT1, however, demonstrated between second and first order dependence of sugar uptake on extracellular Na+ concentration, suggesting the existence of Na(+)-binding sites with different affinities. Here, we directly compared the initial rates of the alpha MeGlc uptake with alpha MeGlc-induced inward currents as an indicator of the Na+ flux. This analysis clearly revealed a Na+ to glucose coupling ratio of 2:1. In summary, our data provide important insights into the function and tissue distribution of the high affinity Na+/glucose cotransporter SGLT1 and clarify its role in the reabsorption mechanism of D-glucose in the kidney.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12032-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8163506-Amino Acid Sequence, pubmed-meshheading:8163506-Animals, pubmed-meshheading:8163506-Blotting, Northern, pubmed-meshheading:8163506-Carrier Proteins, pubmed-meshheading:8163506-Cattle, pubmed-meshheading:8163506-Female, pubmed-meshheading:8163506-Gene Expression, pubmed-meshheading:8163506-Gene Library, pubmed-meshheading:8163506-Humans, pubmed-meshheading:8163506-Kidney Cortex, pubmed-meshheading:8163506-Kidney Tubules, pubmed-meshheading:8163506-Kinetics, pubmed-meshheading:8163506-Male, pubmed-meshheading:8163506-Membrane Glycoproteins, pubmed-meshheading:8163506-Membrane Proteins, pubmed-meshheading:8163506-Methylglucosides, pubmed-meshheading:8163506-Models, Structural, pubmed-meshheading:8163506-Molecular Sequence Data, pubmed-meshheading:8163506-Monosaccharide Transport Proteins, pubmed-meshheading:8163506-Oocytes, pubmed-meshheading:8163506-Phlorhizin, pubmed-meshheading:8163506-Protein Structure, Secondary, pubmed-meshheading:8163506-Rabbits, pubmed-meshheading:8163506-Rats, pubmed-meshheading:8163506-Rats, Sprague-Dawley, pubmed-meshheading:8163506-Sequence Homology, Amino Acid, pubmed-meshheading:8163506-Sodium-Glucose Transporter 1, pubmed-meshheading:8163506-Swine, pubmed-meshheading:8163506-Xenopus
pubmed:year
1994
pubmed:articleTitle
The high affinity Na+/glucose cotransporter. Re-evaluation of function and distribution of expression.
pubmed:affiliation
Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't