ArticlePflugers Archiv : European journal of physiology2007
PI3-kinase-dependent electrogenic intestinal transport of glucose and amino acids.
Article in Pflugers Archiv : European journal of physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Biology of Peptide Transporter 2 in Mammals: New Insights into Its Function, Structure and Regulation.Cells · 2022Review
- CaFrontiers in pharmacology · 2022Article
- RNA sequencing reveals widespread transcriptome changes in a renal carcinoma cell line.Oncotarget · 2018Article
- Sodium-glucose cotransport.Current opinion in nephrology and hypertension · 2015Review
- SPAK-sensitive regulation of glucose transporter SGLT1.The Journal of membrane biology · 2014Article
- Serum- and glucocorticoid-regulated kinase 2 determines drug-activated pregnane X receptor to induce gluconeogenesis in human liver cells.The Journal of pharmacology and experimental therapeutics · 2014Article
- Loss of enteral nutrition in a mouse model results in intestinal epithelial barrier dysfunction.Annals of the New York Academy of Sciences · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intestinal glucose and amino acid transport is stimulated by the serum- and glucocorticoid-inducible kinase isoforms SGK1, SGK2, and SGK3 and protein kinase B which are, in turn, stimulated following activation of the phosphoinositol-3 kinase (PI3 kinase). The present study has been performed to explore whether pharmacological inhibition of the PI3 kinase affects electrogenic jejunal transport of glucose and amino acids. In Ussing chamber experiments, glucose (20 mM), phenylalanine (20 mM), glutamine (20 mM), cysteine (20 mM), and proline (20 mM) generated lumen negative currents (I (glc), I (phe), I (gln), I (cys), and I (pro)), respectively, which gradually declined following application of the PI3 kinase inhibitor Wortmannin (1 muM). Within 40 min, Wortmannin treatment significantly decreased I (glc) by 39 +/- 10% (n = 5), I (phe) by 70 +/- 7% (n = 4), I (gln) by 69 +/- 8% (n = 4), I (cys) by 67 +/- 8% (n = 6), and I (prol) by 79 +/- 12% (n = 3). A similar decline of I (glc) was observed following application of the PI3 kinase inhibitor LY294002 (50 microM). Exposure to the inhibitors did not significantly alter transepithelial potential difference and resistance in the absence of substrates for electrogenic transport. The observations suggest that the electrogenic transport of glucose and several amino acids requires the continued activity of PI3 kinase.
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