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(GLUT and SGLT): Expanded Families of Sugar Transport Proteins Downloaded from https://www.cambridge.org/core British Journal of Nutrition (2003), 89, 3–9 DOI: 10.1079/BJN2002763 q The Authors 2003 Horizons in Nutritional Science . IP address: Glucose transporters (GLUT and SGLT): expanded families of 170.106.35.229 sugar transport proteins , on I. Stuart Wood* and Paul Trayhurn 02 Oct 2021 at 12:31:40 Liverpool Centre for Nutritional Genomics, Neuroendocrine & Obesity Biology Unit, Department of Medicine, University of Liverpool, University Clinical Departments, Liverpool L69 3GA, UK The number of known glucose transporters has expanded considerably over the past 2 years. At , subject to the Cambridge Core terms of use, available at least three, and up to six, Naþ-dependent glucose transporters (SGLT1–SGLT6; gene name SLC5A) have been identified. Similarly, thirteen members of the family of facilitative sugar transporters (GLUT1–GLUT12 and HMIT; gene name SLC2A) are now recognised. These var- ious transporters exhibit different substrate specificities, kinetic properties and tissue expression profiles. The number of distinct gene products, together with the presence of several different transporters in certain tissues and cells (for example, GLUT1, GLUT4, GLUT5, GLUT8, GLUT12 and HMIT in white adipose tissue), indicates that glucose delivery into cells is a process of considerable complexity. Glucose transporter proteins: Diabetes mellitus: Adipose tissue: Muscle: Sugar transport Glucose is a key fuel in mammals and an important meta- Sodium-dependent glucose transporters https://www.cambridge.org/core/terms bolic substrate. It is obtained directly from the diet, princi- pally following the hydrolysis of ingested disaccharides The SGLT transport glucose (and galactose), with different and polysaccharides, and by synthesis from other substrates affinities, via a secondary active transport mechanism. The in organs such as the liver. Glucose derived from the diet is Na+-electrochemical gradient provided by the Na+ –K+ transferred from the lumen of the small intestine, and both ATPase pump is utilised to transport glucose into cells dietary glucose and glucose synthesised within the body against its concentration gradient. This form of glucose have to be transported from the circulation into target transport takes place across the lumenal membrane of cells. These processes involve the transfer of glucose cells lining the small intestine and the proximal tubules across plasma membranes and this occurs via integral of the kidneys. The first of this type of glucose transport transport proteins. These transporters comprise two protein to be cloned was the high-affinity transporter . structurally and functionally distinct groups, whose mem- from rabbit intestine, SGLT1 (Hediger et al. 1987). The https://doi.org/10.1079/BJN2002763 bers have been identified over the past two decades, human analogue soon followed by homology cloning namely: (i) the Naþ-dependent glucose co-transporters (Hediger et al. 1989). Amino acid comparisons of the (SGLT, members of a larger family of Na-dependent trans- human SGLT range from 57–71 % sequence identity porters, gene name SLC5A) (Wright, 2001); (ii) the facil- (GAP algorithm, GCG software package). SGLT1 has a itative Naþ-independent sugar transporters (GLUT family, limited tissue expression and is found essentially on the gene name SLC2A) (Mueckler, 1994; Joost & Thorens, apical membranes of small-intestinal absorptive cells 2001). (enterocytes) and renal proximal straight tubules (S3 cells). In the past 2 years the number of these glucose, and A second Na+ –glucose transporter, SGLT2, is of low other sugar, transporters identified has expanded consider- affinity and is predominantly expressed on the apical mem- ably, particularly the GLUT, with major implications for brane of renal convoluted proximal tubules (S1 and S2 the control of the delivery of glucose to mammalian cells) (Wells et al. 1992; Kanai et al. 1994). It is currently cells. These developments are summarised here. accepted that in the kidney, SGLT2 (low affinity, high Abbreviations: GLUT, glucose transporter; HMIT, H+-coupled myo-inositol transporter; SGLT, Naþ-dependent glucose transporter. * Corresponding author: Dr I. S. Wood, fax +44 151 706 5802, email [email protected] Downloaded from https://www.cambridge.org/core 4 I. S. Wood and P. Trayhurn capacity) transports the bulk of plasma glucose from the Project, has led to the identification of eight further mem- glomerular filtrate. Any remaining glucose is recovered bers of the GLUT family over the last 2 years (Joost & by SGLT1 (high affinity, low capacity) thus preventing Thorens, 2001). However, the pace at which these new glucose loss in the urine. However, controversy exists as genes were identified and classified by independent to whether SGLT2 is the major renal glucose transporter groups initially caused confusion in their terminology. A . IP address: (Hediger et al. 1995; Wright, 2001). consensus has since been reached (Joost et al. 2002) in A pig renal amino acid co-transporter (SAAT1) has been which the thirteen members have been named GLUT1– + reclassified as a low-affinity glucose co-transporter (Mack- 12 and HMIT (H -coupled myo-inositol transporter). It is 170.106.35.229 enzie et al. 1994) and finally renamed pSGLT3. However, considered that all members of the family have now been current studies with the human analogue of SGLT3 (EMBL identified (Joost & Thorens, 2001). accession number, AJ133127) suggest that its function may The facilitative sugar transporters are predicted to have require a re-evaluation (EM Wright, personal communi- twelve membrane-spanning regions with intracellular , on cation). Signals have been detected for SGLT3 in the located amino- and carboxyl-termini. Amino acid sequence 02 Oct 2021 at 12:31:40 small intestine of pigs by northern blot analysis (Kong comparisons of the human GLUT family members range et al. 1993) and in human subjects by reverse transcription from 28 to 65 % identity (GAP algorithm, GCG software polymerase chain reaction (IS Wood, unpublished data). package) measured against GLUT1. Sequence comparisons These findings conflict with collective data indicating of all members reveal the presence of ‘sugar transporter that SGLT1 is the only Na+ –glucose co-transporter signatures’ (Joost & Thorens, 2001) and these consist of expressed in the small intestine. numerous conserved glycine and tryptophan residues, , subject to the Cambridge Core terms of use, available at Mutations of human SGLT1 result in the potentially fatal which are regarded as being essential for general facilita- neonatal condition of glucose galactose malabsorption tive transporter function. Structural and functional charac- (Turk et al. 1991). The severe diarrhoea associated with teristics of the individual GLUT members are at varying glucose-galactose malabsorption is corrected by replacing degrees of completion. Based on a dendrogram (Fig. 1) dietary glucose with fructose. The magnitude of this dis- from a multiple sequence alignment of the extended order, by the mutation of a single gene, would indicate GLUT family, three subclasses (I–III) are apparent, that alternative lumenal glucose transport does not occur which also share common sequence motifs (Joost & Tho- to any significant extent. The relevance of SGLT3 intesti- rens, 2001); see Table 1. nal expression needs to be addressed and suggests that care should be taken when transposing structure–function relationships to similar proteins across species. Further- Class I facilitative transporters more, the importance of establishing protein localisation in heterologous tissue types rather than relying on mRNA The class I facilitative transporters contain GLUT1–4, and expression alone cannot be overlooked. these have been comprehensively characterised in terms of Over recent years, data collected from homology cloning structure, function and tissue distribution. GLUT1 is https://www.cambridge.org/core/terms and the Human Genome Project has indicated the presence expressed particularly in the brain (including the blood– of additional members of the SGLT-like transporters, brain barrier) and erthyrocytes. Moderate levels of which are currently under investigation (Wright, 2001). expression are also observed in adipose tissue, muscle Additional members, SGLT4–6, have been assigned but and the liver. GLUT2 is expressed primarily in pancreatic await complete functional and structural characterisation b-cells, the liver and the kidneys. In the b-cells, GLUT2 is (EM Wright, personal communication). thought to play a role in the glucose-sensing mechanism, while in the liver it is expressed on the sinusoidal mem- brane of hepatocytes and allows for the bi-directional Facilitative glucose transporters transport of glucose under hormonal control. GLUT2 is . The facilitative transporters (GLUT) utilise the diffusion also found on the basolateral surface of proximal renal https://doi.org/10.1079/BJN2002763 gradient of glucose (and other sugars) across plasma mem- tubules and enterocytes, where it forms part of the transcel- branes and exhibit different substrate specificities, kinetic lular pathway for glucose and fructose transport. GLUT3 properties and tissue expression profiles. The first transpor- has a high affinity for glucose and this is consistent with ter to be isolated, GLUT1, was cloned from a HepG2 cell its presence in tissues where the demand for glucose as a line (Mueckler et al. 1985). Identification of other mem- fuel is considerable, in particular the brain. bers of the
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