The glucose transporter families SGLT and GLUT: molecular basis of normal and aberrant function
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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Insulin stimulates translocation of GLUTs from intracellular pools to the cell membrane, amplifying glucose uptake from blood into fat and skeletal muscle cells.
“a process that is amplified by the translocation of GLUTs from intracellular pools to the cell membrane following insulin stimulation ( 26, 27 ).”
From Dynamic modulation of glucose utilisation by glucocorticoid rhythms in health and disease (2020) · cites this paper as [26]
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“The SGLT2 protein co-transports sodium and glucose across the brushborder membrane of the proximal renal tubule into the tubular epithelial cells, a process driven by the sodium gradient between the tubule and the cell, thereby facilitating secondary active transport of glucose.([13,14,21,22]) Glucose is then passivel…”
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“Currently, sugar transporters are mainly classified into three superfamilies: the major facilitator superfamily (MFS), such as glucose transporters (GLUTs) (8, 9); the sodium solute symporter family (SSF), such as sodium-glucose cotransporters (SGLTs) (10); and Sugar Will Eventually be Exported Transporter (SWEET) pro…”
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“The secondary active SGLT transporters are utilized to transport glucose against its concentration gradient, whereas sodium ion transport is driven by the Naþ electrochemical gradient (Wright, 2001; Wood and Trayhurn, 2003; Scheepers et al., 2004).”
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“Sodium-dependent glucose transporter 1 (SGLT1) is the main mediator of apical glucose uptake, whereas at the basolateral membrane the glucose transporter GLUT2 facilitates diffusive transport of intracellular glucose into the bloodstream”
BackgroundStructural basis for the facilitative diffusion mechanism by SemiSWEET transporter
Lee, Y., Nishizawa, T., Yamashita, K., Ishitani, R., & Nureki, O. (2015) · Nature Communications · doi:10.1038/ncomms7112 · Cited by 87 · see citing works
Modeling Kinetics of Subcellular Disposition of Chemicals
Baláž, Š. (2009) · Chemical Reviews · doi:10.1021/cr030440j · Cited by 82 · see citing works
Overlapped Metabolic and Therapeutic Links between Alzheimer and Diabetes
Ahmad, W. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8352-z · Cited by 80 · see citing works
“GLUT 1 expressed on BBB endothelial cells and cortical membranes, GLUT 3 expressed on neurons while GLUT 4 and GLUT 8 expressed in intracellular compartments of neurons [10, 142, 143].”
BackgroundGrimm, M. F., Koziolek, M., Saleh, M., et al. (2018) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.7b00919 · Cited by 81 · see citing works
Mueckler, M. M., & Makepeace, C. M. (2009) · Biochemistry · doi:10.1021/bi900521n · Cited by 80 · see citing works
“At least five of the 14 mammalian GLUT proteins are glucose transporters that are expressed and regulated in a cell-specific fashion and that play distinct roles in cellular and organismal glucose homeostasis (5,6).”
BackgroundPlant mineral transport systems and the potential for crop improvement
Yadav, B., Jogawat, A., Lal, S. K., Lakra, N., Mehta, S., Shabek, N., & Narayan, O. P. (2021) · Planta · doi:10.1007/s00425-020-03551-7 · Cited by 79 · see citing works
New advances in brain-targeting nano-drug delivery systems for Alzheimer's disease
Ouyang, Q., Meng, Y., Zhou, W., Tong, J., Cheng, Z., & Zhu, Q. (2021) · Journal of drug targeting · doi:10.1080/1061186x.2021.1927055 · Cited by 79 · see citing works
Hyperinsulinemia: A unifying theory of chronic disease?
Crofts, C. A. P. (2015) · Diabesity · doi:10.15562/diabesity.2015.19 · Cited by 75 · see citing works
Endocrinopathies and Male Infertility
Sengupta, P., Dutta, S., Karkada, I. R., & Chinni, S. V. (2021) · Life · doi:10.3390/life12010010 · Cited by 75 · see citing works
“A total of 14 members make up the GLUT family, which can be split into three groups based on the sequence similarities between them [115].”
BackgroundPolyphenols: Potential Future Arsenals in the Treatment of Diabetes
Solayman, M., Ali, Y., Alam, F., Islam, M. A., Alam, N., Khalil, M. I., & Gan, S. H. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666151125001111 · Cited by 73 · see citing works
Glucose transporters are expressed in taste receptor cells
Merigo, F., Benati, D., Cristofoletti, M., Osculati, F., & Sbarbati, A. (2011) · Journal of Anatomy · doi:10.1111/j.1469-7580.2011.01385.x · Cited by 68 · see citing works
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“To date, 14 members of GLUTs have been reported in the human tissue (23).”
Disorders of Carbohydrate Metabolism
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Enzymatic features of the glucose metabolism in tumor cells
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Clinical and Genetic Overview of Paroxysmal Movement Disorders and Episodic Ataxias
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Effects of Estrogen in the Brain: Is it a Neuroprotective Agent in Alzheimers Disease?
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Oncogene Pathway Activation in Mammary Tumors Dictates FDG-PET Uptake
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“There are 14 GLUT genes in humans, 11 of which encode proteins possessing glucose transport activity (14).”
Sex differences in growth performance are related to cecal microbiota in chicken
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Sweet Taste Is Complex: Signaling Cascades and Circuits Involved in Sweet Sensation
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Histopathologic Changes in the Cochlea Associated With Diabetes Mellitus—A Review
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Diabetes mellitus and male infertility
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“The GLUT family consists of 14 members and can be divided into three groups based on their sequence similarities[51].”
BackgroundBrain glucose and ketone utilization in brain aging and neurodegenerative diseases
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D-galactose induces necroptotic cell death in neuroblastoma cell lines
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“2011 Wiley Periodicals, Inc. KEY WORDS: D-GALACTOSE; NEUROBLASTOMA; NECROPTOSIS; APOPTOSIS D -Galactose (D-gal) is a kind of hexose and can be transportedinto cells via glucose transporters (Gluts) and then converted to glucose through enzymatic reactions [Scheepers et al., 2004].”
BackgroundCurrent knowledge on boar sperm metabolism: Comparison with other mammalian species
Rodríguez-Gil, J. E., & Bonet, S. (2015) · Theriogenology · doi:10.1016/j.theriogenology.2015.05.005 · Cited by 61 · see citing works
“These proteins differentiate themselves by subtle structural changes that, in turn, lead to great differences in the affinity for separate sugars and tissue specificity [17,18].”
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Essential role of glucose transporter GLUT3 for post-implantation embryonic development
Schmidt, S., Hommel, A., Gawlik, V., Augustin, R., Junicke, N., Florian, S., Richter, M., Walther, D. J., Montag, D., Joost, H., et al. (2008) · Journal of Endocrinology · doi:10.1677/joe-08-0262 · Cited by 59 · see citing works
“The glucose transporter family comprises 14 members, GLUT1–12, GLUT14 and HMIT1 (HC/myo-inositol symporter; Joost & Thorens 2001, Scheepers et al. 2004).”
BackgroundSelf-citation
- 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
- 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
- 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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