Cited by 476Metabolism, Diabetes, and CancerIon Transport and Channel RegulationDiabetes Treatment and Management

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The glucose transporter families SGLT and GLUT: molecular basis of normal and aberrant function

Scheepers, A, Joost, HG, Schurmann, A·2004·Journal of Parenteral and Enteral Nutrition

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Abstract

Glucose enters eucaryotic cells via 2 different types of membrane associated carrier proteins, the Na+‐coupled glucose transporters (SGLT) and glucose transporter facilitators (GLUT). Three members of the SGLT family function as sugar transporters (SGLT1 and SGLT2) or sensors (SGLT3). The human GLUT family consists of 14 members, of which 11 have been shown to catalyze sugar transport. The individual isotypes exhibit different substrate specificity, kinetic characteristics, and expression profiles, thereby allowing a tissue‐specific adaptation of glucose uptake through regulation of their gene expression. Furthermore, some transporters (eg, GLUT4 and GLUT8) are regulated by their subcellular distribution. In addition to catalyzing glucose entry into cells, some isotypes (eg, GLUT2) seem to be involved in the mechanisms of glucosensing of pancreatic beta‐cells, neuronal, or other cells, thereby playing a major role in the hormonal and neural control. Targeted disruption in mice has helped to elucidate the physiologic function of some isotypes (GLUT1, GLUT2, GLUT4). Furthermore, several congenital defects of sugar metabolism are caused by aberrant transporter genes (eg, the glucose‐galactose malabsorption syndrome, SGLT1; the glucose transporter 1 deficiency syndrome; and the Fanconi‐Bickel syndrome, GLUT2). In addition, a malfunction of glucose transporter expression or regulation (GLUT4) appears to contribute to the insulin resistance syndrome.

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Small Intestinal Digestive Functions and Feed Efficiency Differ in Different Pig Breeds
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“Specifically, SGLT1 is a high-affinity and low-capacity sodium–glucose symporter and is expressed mainly in the small intestine [44].”
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“Both genes code class II sugar transport facilitators, which belong to the membrane transporter superfamily.(22,23) Although the substrates for Slc2a11b and Slc2a15b remain unknown and which step is participated by those genes to form xanthophore is now unresolved, the homologs of those genes in X tropicalis would inv…”
Background
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“As it is well known, glucose is an essential source of cellular energy and it acts as an important substrate for protein and lipid synthesis (Scheepers et al. 2004).”
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“It is estimated that 90% of renal glucose reabsorption is facilitated by SGLT2 residing on the surface of the epithelial cells lining the S1 segment of the proximal tubule; the remaining 10% is likely mediated by SGLT1 localized on the more distal S3 segment of the proximal tubule [15–20].”
Background
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The apical sorting signal for human GLUT9b resides in the N-terminus
Bibee, K., Augustin, R., Gazit, V. A., et al. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1564-3 · Cited by 7
“In the case of GLUT11, while there is some overlap among tissues with expression, each splice variants has at least one tissue where it is predominant [6].”
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“Renal reabsorption of glucose mainly involves the SGLT-2 transporter, located in the apical membrane of renal tubule epithelial cells, which co-transports one glucose molecule with every Na ? ion ( Scheepers et al. 2004; Wright et al.”
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Convenient synthesis of [3R-(3α,4β,5α,6β)]-2-[7-chloro-1-(4-ethylbenzyl)-5-methyl-1H-indol-3-yl]-6-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol
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“They could be considered as true positive candidates, because microarray analysis of cell lines ectopically expressing PPAR family members [22] had shown that many of the established PPAR target genes are equally receptive to all 3 receptors although preferential targets do exist for each isotype (27 for PPARG, 33 for…”
BackgroundInfluential
Investigational Agents Targeting SGLT1 and SGLT2 in the Treatment of Type 2 Diabetes Mellitus
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Authors: Scheepers, A., Joost, H., & Schurmann, A.
Affiliations: German Institute of Human Nutrition (DE)
Venue: Journal of Parenteral and Enteral Nutrition
Publisher: Wiley
Published: 2004-09
Volume: 28
Issue: 5
Pages: 364-371
ISSN: 0148-6071 (ISSN-L)
1941-2444
DOI: 10.1177/0148607104028005364
OpenAlex: W1993812967
Cited by: 476
References: 0
Citations by year: 2026: 7 · 2025: 17 · 2024: 16 · 2023: 16 · 2022: 27 · 2021: 26 · 2020: 27 · 2019: 24 · 2018: 29 · 2017: 22 · 2016: 23 · 2015: 29 · 2014: 34 · 2013: 28 · 2012: 28
FWCI: 3.76
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Parenteral and Enteral Nutrition (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
Keywords: glucose transporters, GLUT family, SGLT1, SGLT2, GLUT1, GLUT2, GLUT4, GLUT8, glucose transport, sugar transporters, glucose detection, pancreatic beta cells, GLUT1 deficiency syndrome, Fanconi-Bickel syndrome, insulin resistance, gene expression regulation
MeSH terms: Animals, Biological Transport, Active, Gene Expression Regulation, Glucose, Humans, Monosaccharide Transport Proteins, Signal Transduction, Protein Isoforms, Mice

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The glucose transporter families SGLT and GLUT: molecular basis of normal and aberrant function

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