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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2 Pt 1
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pubmed:dateCreated |
1999-3-30
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pubmed:abstractText |
Na+-glucose cotransporter (SGLT1) expression and the role of actin in epidermal growth factor (EGF)-induced alterations in glucose transport and brush-border surface area were examined in New Zealand White rabbit jejunal loops. In separate experiments, EGF or EGF concurrent with cytochalasin D, an inhibitor of actin polymerization, was administered to the experimental loop and compared with its vehicle control. SGLT1 expression was measured by Western blot in brush-border membrane vesicles (BBMV) after 5-min and 1-h exposure. Glucose kinetics were determined by a rapid filtration technique, and brush-border surface area was examined by electron microscopy after 1-h exposure. The effect of cytochalasin D alone on BBMV glucose kinetics and brush-border surface area was also assessed. EGF resulted in a significant increase in BBMV SGLT1 expression (P < 0.05), glucose maximal uptake (Vmax; P < 0.001), and absorptive brush-border surface area (P < 0.001). These effects were abolished with concurrent cytochalasin D treatment. Cytochalasin D alone had no effect on glucose transport or brush-border surface area. The findings suggest that EGF acutely upregulates jejunal brush-border surface area and the Vmax for jejunal glucose uptake via the recruitment and insertion of SGLT1 from an internal pool into the brush border by a mechanism that is dependent on actin polymerization.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin D,
http://linkedlifedata.com/resource/pubmed/chemical/Drug Combinations,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Glucose Transporter 1
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0002-9513
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
G463-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9950820-Actins,
pubmed-meshheading:9950820-Animals,
pubmed-meshheading:9950820-Blotting, Western,
pubmed-meshheading:9950820-Cytochalasin D,
pubmed-meshheading:9950820-Drug Combinations,
pubmed-meshheading:9950820-Epidermal Growth Factor,
pubmed-meshheading:9950820-Glucose,
pubmed-meshheading:9950820-Jejunum,
pubmed-meshheading:9950820-Kinetics,
pubmed-meshheading:9950820-Membrane Glycoproteins,
pubmed-meshheading:9950820-Microscopy, Electron,
pubmed-meshheading:9950820-Microvilli,
pubmed-meshheading:9950820-Monosaccharide Transport Proteins,
pubmed-meshheading:9950820-Rabbits,
pubmed-meshheading:9950820-Sodium-Glucose Transporter 1
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pubmed:year |
1999
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pubmed:articleTitle |
Role of actin in EGF-induced alterations in enterocyte SGLT1 expression.
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pubmed:affiliation |
Gastrointestinal Research Group, Health Sciences Centre, University of Calgary, Calgary, Alberta, Canada T2N 4N1.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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