GLUT5

Last updated
SLC2A5
GLUT5.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SLC2A5 , GLUT-5, GLUT5, solute carrier family 2 member 5
External IDs OMIM: 138230 MGI: 1928369 HomoloGene: 74459 GeneCards: SLC2A5
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001135585
NM_003039
NM_001328619
NM_001328620
NM_001328621

Contents

NM_019741

RefSeq (protein)

NP_001129057
NP_001315548
NP_001315549
NP_001315550
NP_003030

NP_062715

Location (UCSC) Chr 1: 9.04 – 9.09 Mb Chr 4: 150.2 – 150.23 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

GLUT5 is a fructose transporter expressed on the apical border of enterocytes in the small intestine. [5] GLUT5 allows for fructose to be transported from the intestinal lumen into the enterocyte by facilitated diffusion due to fructose's high concentration in the intestinal lumen. GLUT5 is also expressed in skeletal muscle, [6] testis, kidney, fat tissue (adipocytes), and brain. [7]

Fructose malabsorption or Dietary Fructose Intolerance is a dietary disability of the small intestine, where the amount of fructose carrier in enterocytes is deficient. [8]

In humans the GLUT5 protein is encoded by the SLC2A5 gene. [9]

Regulation

Fructose uptake rate by GLUT5 is significantly reduced by diabetes mellitus, hypertension, obesity, fructose malabsorption, and inflammation. However, age-related changes in fructose intake capability are not explained by the rate of expression of GLUT5. [10] [11] [12] The absorption of fructose in the simultaneous presence of glucose is improved, while sorbitol is inhibitory. [13] Fructose absorption by GLUT5 can be investigated using intestinal organoids. [14] [15]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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WP534.png go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to article
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Glycolysis and Gluconeogenesis edit
  1. The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

Related Research Articles

<span class="mw-page-title-main">Fructose</span> Simple ketonic monosaccharide found in many plants

Fructose, or fruit sugar, is a ketonic simple sugar found in many plants, where it is often bonded to glucose to form the disaccharide sucrose. It is one of the three dietary monosaccharides, along with glucose and galactose, that are absorbed by the gut directly into the blood of the portal vein during digestion. The liver then converts both fructose and galactose into glucose, so that dissolved glucose, known as blood sugar, is the only monosaccharide present in circulating blood.

<span class="mw-page-title-main">Enterocyte</span> Type of intestinal cell

Enterocytes, or intestinal absorptive cells, are simple columnar epithelial cells which line the inner surface of the small and large intestines. A glycocalyx surface coat contains digestive enzymes. Microvilli on the apical surface increase its surface area. This facilitates transport of numerous small molecules into the enterocyte from the intestinal lumen. These include broken down proteins, fats, and sugars, as well as water, electrolytes, vitamins, and bile salts. Enterocytes also have an endocrine role, secreting hormones such as leptin.

<span class="mw-page-title-main">Caco-2</span>

Caco-2 is an immortalized cell line of human colorectal adenocarcinoma cells. It is primarily used as a model of the intestinal epithelial barrier. In culture, Caco-2 cells spontaneously differentiate into a heterogeneous mixture of intestinal epithelial cells. It was developed in 1977 by Jorgen Fogh at the Sloan-Kettering Institute for Cancer Research.

<span class="mw-page-title-main">GLUT2</span> Transmembrane carrier protein

Glucose transporter 2 (GLUT2) also known as solute carrier family 2, member 2 (SLC2A2) is a transmembrane carrier protein that enables protein facilitated glucose movement across cell membranes. It is the principal transporter for transfer of glucose between liver and blood Unlike GLUT4, it does not rely on insulin for facilitated diffusion.

<span class="mw-page-title-main">Glucose transporter</span> Family of monosaccharide transport proteins

Glucose transporters are a wide group of membrane proteins that facilitate the transport of glucose across the plasma membrane, a process known as facilitated diffusion. Because glucose is a vital source of energy for all life, these transporters are present in all phyla. The GLUT or SLC2A family are a protein family that is found in most mammalian cells. 14 GLUTS are encoded by the human genome. GLUT is a type of uniporter transporter protein.

A hydrogen breath test is used as a diagnostic tool for small intestine bacterial overgrowth and carbohydrate malabsorption, such as lactose, fructose, and sorbitol malabsorption.

Sodium-dependent glucose cotransporters are a family of glucose transporter found in the intestinal mucosa (enterocytes) of the small intestine (SGLT1) and the proximal tubule of the nephron. They contribute to renal glucose reabsorption. In the kidneys, 100% of the filtered glucose in the glomerulus has to be reabsorbed along the nephron. If the plasma glucose concentration is too high (hyperglycemia), glucose passes into the urine (glucosuria) because SGLT are saturated with the filtered glucose.

<span class="mw-page-title-main">Hephaestin</span> Mammalian protein found in Homo sapiens

Hephaestin, also known as HEPH, is a protein which in humans is encoded by the HEPH gene.

Glucose transporter 3, also known as solute carrier family 2, facilitated glucose transporter member 3 (SLC2A3) is a protein that in humans is encoded by the SLC2A3 gene. GLUT3 facilitates the transport of glucose across the plasma membranes of mammalian cells. GLUT3 is most known for its specific expression in neurons and has originally been designated as the neuronal GLUT. GLUT3 has been studied in other cell types with specific glucose requirements, including sperm, preimplantation embryos, circulating white blood cells and carcinoma cell lines.

<span class="mw-page-title-main">Fructose-bisphosphate aldolase</span>

Fructose-bisphosphate aldolase, often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism.

<span class="mw-page-title-main">Natural resistance-associated macrophage protein 2</span>

Natural resistance-associated macrophage protein 2, also known as divalent metal transporter 1 (DMT1) and divalent cation transporter 1 (DCT1), is a protein that in humans is encoded by the SLC11A2 gene. DMT1 represents a large family of orthologous metal ion transporter proteins that are highly conserved from bacteria to humans.

<span class="mw-page-title-main">Glucose-galactose malabsorption</span> Medical condition

Glucose-galactose malabsorption is a rare condition in which the cells lining the intestine cannot take in the sugars glucose and galactose, which prevents proper digestion of these molecules and larger molecules made from them.

<span class="mw-page-title-main">Sodium/glucose cotransporter 1</span>

Sodium/glucose cotransporter 1 (SGLT1) also known as solute carrier family 5 member 1 is a protein in humans that is encoded by the SLC5A1 gene which encodes the production of the SGLT1 protein to line the absorptive cells in the small intestine and the epithelial cells of the kidney tubules of the nephron for the purpose of glucose uptake into cells. Recently, it has been seen to have functions that can be considered as promising therapeutic target to treat diabetes and obesity. Through the use of the sodium glucose cotransporter 1 protein, cells are able to obtain glucose which is further utilized to make and store energy for the cell.

<span class="mw-page-title-main">Peptide transporter 1</span> Mammalian protein found in Homo sapiens

Peptide transporter 1 also known as solute carrier family 15 member 1 (SLC15A1) is a protein that in humans is encoded by SLC15A1 gene. PepT 1 is a solute carrier for oligopeptides. It functions in renal oligopeptide reabsorption and in the intestines in a proton dependent way, hence acting like a cotransporter.

<span class="mw-page-title-main">Ileal sodium/bile acid cotransporter</span> Protein-coding gene in the species Homo sapiens

Ileal sodium/bile acid cotransporter, also known as apical sodium–bile acid transporter (ASBT) and ileal bile acid transporter (IBAT), is a bile acid:sodium symporter protein that in humans is encoded by the SLC10A2 gene.

<span class="mw-page-title-main">Inborn errors of carbohydrate metabolism</span> Medical condition

Inborn errors of carbohydrate metabolism are inborn error of metabolism that affect the catabolism and anabolism of carbohydrates.

Fructolysis refers to the metabolism of fructose from dietary sources. Though the metabolism of glucose through glycolysis uses many of the same enzymes and intermediate structures as those in fructolysis, the two sugars have very different metabolic fates in human metabolism. Unlike glucose, which is directly metabolized widely in the body, fructose is almost entirely metabolized in the liver in humans, where it is directed toward replenishment of liver glycogen and triglyceride synthesis. Under one percent of ingested fructose is directly converted to plasma triglyceride. 29% - 54% of fructose is converted in liver to glucose, and about a quarter of fructose is converted to lactate. 15% - 18% is converted to glycogen. Glucose and lactate are then used normally as energy to fuel cells all over the body.

<span class="mw-page-title-main">Plasma membrane monoamine transporter</span>

The plasma membrane monoamine transporter (PMAT) is a low-affinity monoamine transporter protein which in humans is encoded by the SLC29A4 gene. It is known alternatively as the human equilibrative nucleoside transporter-4 (hENT4). It was discovered in 2004 and has been identified as a potential alternate target for treating various conditions.

Haem or Heme carrier protein 1 (HCP1) was originally identified as mediating heme-Fe transport although it later emerged that it was the SLC46A1 folate transporter.

<span class="mw-page-title-main">Proton-coupled folate transporter</span> Mammalian protein found in Homo sapiens

The proton-coupled folate transporter is a protein that in humans is encoded by the SLC46A1 gene. The major physiological roles of PCFTs are in mediating the intestinal absorption of folate, and its delivery to the central nervous system.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000142583 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028976 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Uldry M, Thorens B (February 2004). "The SLC2 family of facilitated hexose and polyol transporters" (PDF). Pflügers Archiv: European Journal of Physiology. 447 (5): 480–9. doi:10.1007/s00424-003-1085-0. PMID   12750891. S2CID   25539725.
  6. Hundal HS, Darakhshan F, Kristiansen S, Blakemore SJ, Richter EA (1998). "GLUT5 Expression and Fructose Transport in Human Skeletal Muscle". Skeletal Muscle Metabolism in Exercise and Diabetes. Advances in Experimental Medicine and Biology. Vol. 441. pp. 35–45. doi:10.1007/978-1-4899-1928-1_4. ISBN   978-1-4899-1930-4. PMID   9781312.
  7. Douard V, Ferraris RP (August 2008). "Regulation of the fructose transporter GLUT5 in health and disease". American Journal of Physiology. Endocrinology and Metabolism. 295 (2): E227–37. doi:10.1152/ajpendo.90245.2008. PMC   2652499 . PMID   18398011.
  8. Barone S, Fussell SL, Singh AK, Lucas F, Xu J, Kim C, Wu X, Yu Y, Amlal H, Seidler U, Zuo J, Soleimani M (February 2009). "Slc2a5 (Glut5) Is Essential for the Absorption of Fructose in the Intestine and Generation of Fructose-induced Hypertension". The Journal of Biological Chemistry. 284 (8): 5056–66. doi: 10.1074/jbc.M808128200 . PMC   2643499 . PMID   19091748.
  9. White PS, Jensen SJ, Rajalingam V, Stairs D, Sulman EP, Maris JM, Biegel JA, Wooster R, Brodeur GM (1998). "Physical mapping of the CA6, ENO1, and SLC2A5 (GLUT5) genes and reassignment of SLC2A5 to 1p36.2". Cytogenetics and Cell Genetics. 81 (1): 60–4. doi:10.1159/000014989. PMID   9691177. S2CID   46770845.
  10. Douard V, Ferraris RP (August 2008). "Regulation of the fructose transporter GLUT5 in health and disease". Am. J. Physiol. Endocrinol. Metab. 295 (2): E227–37. doi:10.1152/ajpendo.90245.2008. PMC   2652499 . PMID   18398011.
  11. Litherland GJ, Hajduch E, Gould GW, Hundal HS (June 2004). "Fructose transport and metabolism in adipose tissue of Zucker rats: diminished GLUT5 activity during obesity and insulin resistance" (PDF). Mol. Cell. Biochem. 261 (1–2): 23–33. doi:10.1023/b:mcbi.0000028734.77867.d2. PMID   15362482. S2CID   13029991. Archived from the original (PDF) on September 9, 2012.
  12. Drozdowski LA, Woudstra TD, Wild GE, Clandinin MT, Thomson AB (October 2004). "Age-associated changes in intestinal fructose uptake are not explained by alterations in the abundance of GLUT5 or GLUT2". J. Nutr. Biochem. 15 (10): 630–7. doi:10.1016/j.jnutbio.2004.06.003. PMID   15542355.
  13. Heinrich Kasper: Ernährungsmedizin und Diätetik. 11. Auflage, Elsevier, Urban&Fischer-Verlag, 2009, ISBN   9783437420122, S. 208
  14. Zietek T, Giesbertz P, Ewers M, Reichart F, Weinmüller M, Demir IE, et al. (2020). "Organoids to Study Intestinal Nutrient Transport, Drug Uptake and Metabolism – Update to the Human Model and Expansion of Applications". Frontiers in Bioengineering and Biotechnology. 8: 577656. doi: 10.3389/fbioe.2020.577656 . ISSN   2296-4185. PMC   7516017 . PMID   33015026.
  15. Zietek T, Rath E, Haller D, Daniel H (November 2015). "Intestinal organoids for assessing nutrient transport, sensing and incretin secretion". Scientific Reports. 5 (1): 16831. doi: 10.1038/srep16831 . PMC   4652176 . PMID   26582215.