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Last update 23 Jan 2025

GLUT5

Last update 23 Jan 2025

Basic Info

Synonyms

Fructose transporter, Glucose transporter type 5, small intestine, GLUT-5

+ [5]

Introduction

Functions as a fructose transporter that has only low activity with other monosaccharides (PubMed:8333543, PubMed:16186102, PubMed:28083649, PubMed:17710649, PubMed:29548810). Can mediate the uptake of 2-deoxyglucose, but with low efficiency (PubMed:1695905). Essential for fructose uptake in the small intestine (By similarity). Plays a role in the regulation of salt uptake and blood pressure in response to dietary fructose (By similarity). Required for the development of high blood pressure in response to high dietary fructose intake (By similarity).

Drugs associated with GLUT5

S-700

Target

GLUT5

Mechanism

GLUT5 blockers

Active Org.

SCOHIA PHARMA, Inc.Startup

Originator Org.

SCOHIA PHARMA, Inc.Startup

Active Indication

Metabolic Diseases

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with GLUT5

100 Translational Medicine associated with GLUT5

0 Patents (Medical) associated with GLUT5

693

Literatures (Medical) associated with GLUT5

01 Jan 2025·Poultry Science

Transcriptome analysis of jejunal mucosal tissue in breeder hens exposed to acute heat stress

Article

Author: Okrathok, Supattra ; Khempaka, Sutisa ; Zhu, Yongcai ; Kubota, Satoshi ; Pasri, Phocharapon ; Yang, Shenglin ; Rakngam, Sitthipong ; Pukkung, Chayanan

Heat stress (HS) severely compromises intestinal barrier function in poultry, resulting in significant production losses. This study aimed to explore the molecular response of the small intestine to acute HS in breeder hens. Fifty 28-week-old breeder hens were raised individually in a cage and randomly assigned to control and heat-treated groups (25 hens each). Control group hens were maintained at thermoneutral conditions (23°C) and heat-treated group hens were subjected to acute HS (36°C for a 6-h). The heart rate and cloacal temperature were measured in all hens. The jejunal mucosa tissues were collected from 12 randomly selected hens per group for transcriptomic analysis. The acute HS induced significant physiological alterations, with a marked increase in the heart rate and cloacal temperature in hens (P = 0.001). Transcriptome analysis revealed 138 genes with altered expression patterns under acute HS conditions. Of these, 75 genes including heat shock proteins (HSPs) showed upregulated expression, while 63 genes including a key bile acid transport molecule (SLC10A2) exhibited downregulated expression. Functional analysis through gene ontology classification, pathway mapping via the Kyoto encyclopedia of genes and genomes, and protein interaction networks identified several important regulatory genes in thermal response (HSPA8 and HSPA2), energy homeostasis and fat metabolism (PDK4, PPARA, and CD36), glucose transport (SLC2A5), and cholesterol synthesis pathway (SQLE, CYP51A1, and HSD17B7). The findings suggest that acute HS might affect energy utilization, fat metabolism, and glucose transport mechanisms in the jejunal mucosa of breeder hens. The upregulation of HSPs appears to serve as a protective mechanism, potentially preserving intestinal nutrient processing capacity under acute HS. These findings provide foundational knowledge for further investigation into the molecular mechanisms governing HS responses in avian intestinal function and may inform strategies for maintaining gut health in commercial poultry operations exposed to environmental challenges.

31 Dec 2024·Animal Cells and Systems

Role of Carbohydrate response element-binding protein in mediating dexamethasone-induced glucose transporter 5 expression in Caco-2BBE cells and during the developmental phase in mice

Article

Author: Kim, Jaewan ; Oh, Ah-Reum ; Lee, Ho-Jae ; Hwang, Soonjae ; Park, Sangbin ; Cha, Ji-Young

Glucose transporter 5 (GLUT5), the main fructose transporter in mammals, is primarily responsible for absorbing dietary fructose in the small intestine. The expression of this intestinal gene significantly increases in response to developmental and dietary cues that reach the glucocorticoid receptor and carbohydrate response element-binding protein (ChREBP), respectively. Our study demonstrates that ChREBP is involved in the dexamethasone (Dex)-induced expression of GLUT5 in Caco-2BBE cells and the small intestine of both wild-type and ChREBP-knockout mice. Dex, a glucocorticoid, demonstrated an increase in GLUT5 mRNA levels in a dose- and time-dependent manner. While the overexpression of ChREBP moderately increased GLUT5 expression, its synergistic increase in the presence of Dex was noteworthy, whereas the suppression of ChREBP significantly reduced Dex-induced GLUT5 expression. Dex did not increase ChREBP protein levels but facilitated its nuclear translocation, thereby increasing the activity of the GLUT5 promoter. In vivo experiments conducted on 14-day-old mice pups treated with Dex for three days revealed that only wild-type mice (not ChREBP-knockout mice) exhibited Dex-mediated Glut5 gene induction, which further supports the role of ChREBP in regulating GLUT5 expression. Collectively, our results provide insights into the molecular mechanisms involved in the regulation of GLUT5 expression in response to developmental and dietary signals mediated by glucocorticoids and ChREBP. General significance: The transcription factor ChREBP is important for Dex-mediated Glut5 gene expression in the small intestine.

01 Dec 2024·Biochemical and Biophysical Research Communications

Cryo-EM structure of the human glucose transporter GLUT7

Article

Author: Kim, Subin ; Jin, Mi Sun ; Lee, Sang Soo

GLUT7 is a Class II glucose transporter predominantly expressed at the apical membrane of enterocytes in the small intestine. Here, we report the cryo-EM structure of nanodisc-reconstituted human GLUT7 in the apo state at 3.3 Å resolution. Our atomic model reveals a typical major facilitator superfamily fold, with the substrate-binding site open to the extracellular side of the membrane. Despite the nearly identical conformation to its closest family member, rat GLUT5, our structure unveils distinct features of the substrate-binding cavity that may influence substrate specificity and binding mode. A homology model of the inward-open human GLUT7 indicates that similar to other members of the GLUT family, it may undergo a global rocker-switch-like reorientation of the transmembrane bundles to facilitate substrate translocation across the membrane. Our work enhances the current structural understanding of the GLUT family, and lays a foundation for rational design of regulators of GLUTs and other sugar transporters.

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GLUT5

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