Molecular Biology of Na
            <sup>+</sup>
            /Glucose Symport

Lever, Julia E.

doi:10.1002/cphy.cp060417

Cited by 3 publications

(2 citation statements)

References 35 publications

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“…Na+/D-glucose symport (cotransport) is a secondary active glucose transport mechanism restricted to the apical membranes of small intestine and kidney proximal tubule (Crane, 1977;Lever, 1991). The LLC-PK, cell line derived from pig kidney (Hull et al, 1976) is a useful model system for investigation of regulation of Na+/glucose symporter expression.…”

Section: G 1993 Wiley-liss Incmentioning

confidence: 99%

“…Our rcsults suggest that induction of symportcr expression by HMBA may be mediated in part by its effects on polyamine metabolism, and point to parallel roles of polyamines and cyclic AMP in regulating the expression of this physiologically important renal transport system. G 1993 Wiley-Liss, Inc Na+/D-glucose symport (cotransport) is a secondary active glucose transport mechanism restricted to the apical membranes of small intestine and kidney proximal tubule (Crane, 1977;Lever, 1991). The LLC-PK, cell line derived from pig kidney (Hull et al, 1976) is a useful model system for investigation of regulation of Na+/glucose symporter expression.…”

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Polyamine regulation of Na⁺/glucose symporter expression in LLC‐PK₁ cells

Hua

Lever

1993

Journal Cellular Physiology

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Addition of polyamines or their analogs to newly confluent LLC-PK1 cells resulted in down-regulation of Na(+)-dependent glucose transport (symport) activity. Polyamines prevented the induction of this symporter by the differentiation inducer hexamethylene bisacetamide (HMBA) but did not influence induction by the phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine (IBMX). Partial depletion of endogenous polyamines after addition of alpha-difluoromethylornithine (DFMO) resulted in a 4 to 5-fold increase in symporter expression. Symporter induction by either HMBA or DFMO was inhibited by the protein kinase inhibitor H-7 but H-7 did not affect symporter induction by IBMX. Changes in symporter activity were accompanied by changes in levels of the 75 kD symporter subunit detected by Western blot. Cultures exposed to HMBA exhibited reduced levels of ornithine decarboxylase activity. Our results suggest that induction of symporter expression by HMBA may be mediated in part by its effects on polyamine metabolism, and point to parallel roles of polyamines and cyclic AMP in regulating the expression of this physiologically important renal transport system.

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Section: G 1993 Wiley-liss Incmentioning

confidence: 99%

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confidence: 99%

Polyamine regulation of Na⁺/glucose symporter expression in LLC‐PK₁ cells

Hua

Lever

1993

Journal Cellular Physiology

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Release of glucagon-like peptide-1 (GLP-1) by carbohydrates in the perfused rat ileum

et al. 1997

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The effect of various carbohydrates on glucagon-like peptide-1 (GLP-1) release was studied in the in vivo perfused rat ileum. GLP-1 concentrations in the mesenteric venous effluent increased significantly after luminal perfusion with substrates of a sodium/glucose co-transporter (D-glucose, D-galactose, methyl-alpha D-glucoside, and 3-O-methyl-D-glucose). D-Fructose induced a sodium-independent release of GLP-1. Carbohydrates like 2-deoxy-D-glucose and N-acetyl-D-glucosamine, which are not substrates of a luminal sodium/glucose or fructose transporter, did not affect GLP-1 release. Since methyl-alpha D-glucoside is not a substrate of the basolateral glucose transport mechanism and 3-O-methyl-D-glucose is not metabolized within intestinal cells, it is concluded that intracellular metabolism of carbohydrates and intracellular removal are not essential to induce GLP-1 secretion in rats.

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Peptide regulation of intestinal glucose absorption.

Bird

Croom

Fan

et al. 1996

Journal of Animal Science

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Terminal hydrolysis of oligosaccharides at the small intestinal brush border yields monomeric glucose, most of which is then absorbed by the transepithelial route. This involves carrier-mediated processes requiring specialized functional proteins situated in the brush border (SGLT1) and basolateral (GLUT2) membranes. Glucose translocation at the enterocyte apical membrane is an active, Na(+)-dependent and saturable process, whereas exit from enterocytes is by facilitated diffusion and is energy-independent. Specific adaptation of glucose active transport occurs in response to changes in the proportion of glucose in the diet. The regulatory signals responsible for transport induction are imprecisely defined, although numerous protein hormones and gut regulatory proteins are implicated. Epidermal growth factor and peptide YY invoke up-regulation of jejunal active glucose transport in vivo. Recently, peptide YY has been shown to stimulate active glucose transport in mice without altering oxygen consumption of jejunal tissue. Several other peptides whose presence in tissues of the small bowel imply that they exert control over epithelial nutrient transport are considered, and the relevance of these physiological manipulations, with various regulatory peptides and hormones, to animal agriculture are discussed.

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Molecular Biology of Na ⁺ /Glucose Symport

Cited by 3 publications

References 35 publications

Polyamine regulation of Na⁺/glucose symporter expression in LLC‐PK₁ cells

Polyamine regulation of Na⁺/glucose symporter expression in LLC‐PK₁ cells

Release of glucagon-like peptide-1 (GLP-1) by carbohydrates in the perfused rat ileum

Peptide regulation of intestinal glucose absorption.

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Molecular Biology of Na + /Glucose Symport

Cited by 3 publications

References 35 publications

Polyamine regulation of Na+/glucose symporter expression in LLC‐PK1 cells

Polyamine regulation of Na+/glucose symporter expression in LLC‐PK1 cells

Release of glucagon-like peptide-1 (GLP-1) by carbohydrates in the perfused rat ileum

Peptide regulation of intestinal glucose absorption.

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Resources

About

Molecular Biology of Na ⁺ /Glucose Symport

Polyamine regulation of Na⁺/glucose symporter expression in LLC‐PK₁ cells

Polyamine regulation of Na⁺/glucose symporter expression in LLC‐PK₁ cells