scholarly journals Expression, purification, and functional characterization of the insulin-responsive facilitative glucose transporter GLUT4

2015 ◽  
Vol 24 (12) ◽  
pp. 2008-2019 ◽  
Author(s):  
Thomas E. Kraft ◽  
Richard C. Hresko ◽  
Paul W. Hruz
Keyword(s):  
Glucose Transporter ◽  
Functional Characterization ◽  
Glucose Transporter Glut4 ◽  
Facilitative Glucose Transporter

Molecular and functional characterization and tissue localization of 2 glucose transporter homologues (TGTP1 and TGTP2) from the tapeworm Taenia solium

Parasitology ◽  
1998 ◽  
Vol 117 (6) ◽  
pp. 579-588 ◽  
Author(s):  
D. RODRÍGUEZ-CONTRERAS ◽  
P. J. SKELLY ◽  
A. LANDA ◽  
C. B. SHOEMAKER ◽  
J. P. LACLETTE
Keyword(s):  
Glucose Transporter ◽  
Cytochalasin B ◽  
Functional Characterization ◽  
Taenia Solium ◽  
Cdna Clones ◽  
Facilitated Diffusion ◽  
Porcine Cysticercosis ◽  
Isolation And Characterization ◽  
Hexose Uptake

Tapeworms absorb and consume large quantities of glucose through their syncytial tegument, storing the excess as glycogen. Although some studies on the metabolism of glucose in several tapeworms are available, the proteins that mediate its uptake and distribution in their tissue have not been identified. We describe the isolation and characterization of cDNA clones encoding 2 facilitated diffusion glucose transporters (TGTP1 and TGTP2) from Taenia solium, the causal agent of human and porcine cysticercosis. Radio-isotope labelled hexose uptake mediated by TGTP1 expressed in Xenopus oocytes is inhibited by the natural stereoisomers d-glucose and d-mannose but not by l-glucose. Transport by TGTP1 is sensitive to classical inhibitors of facilitated diffusion such as phloretin and cytochalasin B, and insensitive to ouabain. TGTP2 did not function in Xenopus oocytes. Localization studies using specific anti-TGTP1 and anti-TGTP2 antibodies show that TGTP1 is abundant in a number of structures underlying the tegument in adult parasites and larvae, whereas TGTP2 appears to be localized only on the tegumentary surface of the larvae and is not detected in adults.

Molecular and functional characterization of glucose transporter genes of the fox tapeworm Echinococcus multilocularis

2018 ◽  
Vol 225 ◽  
pp. 7-14 ◽  
Author(s):  
Takuya Kashiide ◽  
Shingo Kikuta ◽  
Misaki Yamaguchi ◽  
Takao Irie ◽  
Hirokazu Kouguchi ◽  
...  
Keyword(s):  
Echinococcus Multilocularis ◽  
Glucose Transporter ◽  
Functional Characterization

Molecular cloning and functional characterization of a glucose transporter (CsGLUT) in Clonorchis sinensis

2015 ◽  
Vol 115 (1) ◽  
pp. 347-354 ◽  
Author(s):  
Seong Kyu Ahn ◽  
Pyo Yun Cho ◽  
Byoung-Kuk Na ◽  
Sung-Jong Hong ◽  
Ho-Woo Nam ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Glucose Transporter ◽  
Clonorchis Sinensis ◽  
Functional Characterization

scholarly journals The deubiquitinating enzyme USP25 binds tankyrase and regulates trafficking of the facilitative glucose transporter GLUT4 in adipocytes

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Jessica B. A. Sadler ◽  
Christopher A. Lamb ◽  
Cassie R. Welburn ◽  
Iain S. Adamson ◽  
Dimitrios Kioumourtzoglou ◽  
...  
Keyword(s):  
Glucose Transporter ◽  
Deubiquitinating Enzyme ◽  
Glucose Transporter Glut4 ◽  
Facilitative Glucose Transporter

scholarly journals Hexose transport in Torulaspora delbrueckii: identification of Igt1, a new dual-affinity transporter

2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Andreia Pacheco ◽  
Lorena Donzella ◽  
Maria Jose Hernandez-Lopez ◽  
Maria Judite Almeida ◽  
Jose Antonio Prieto ◽  
...  
Keyword(s):  
Glucose Transporter ◽  
Functional Characterization ◽  
Sugar Transport ◽  
Sugar Metabolism ◽  
Torulaspora Delbrueckii ◽  
Sugar Transporters ◽  
Rate Limiting Step ◽  
Efficient Fermentation ◽  
Rate Limiting

ABSTRACT Torulaspora delbrueckii is a yeast species receiving increasing attention from the biotechnology industry, with particular relevance in the wine, beer and baking sectors. However, little is known about its sugar transporters and sugar transport capacity, frequently a rate-limiting step of sugar metabolism and efficient fermentation. Actually, only one glucose transporter, Lgt1, has been characterized so far. Here we report the identification and characterization of a second glucose transporter gene, IGT1, located in a cluster, upstream of LGT1 and downstream of two other putative hexose transporters. Functional characterization of IGT1 in a Saccharomyces cerevisiae hxt-null strain revealed that it encodes a transporter able to mediate uptake of glucose, fructose and mannose and established that its affinity, as measured by Km, could be modulated by glucose concentration in the medium. In fact, IGT1-transformed S. cerevisiae hxt-null cells, grown in 0.1% glucose displayed biphasic glucose uptake kinetics with an intermediate- (Km = 6.5 ± 2.0 mM) and a high-affinity (Km = 0.10 ± 0.01 mM) component, whereas cells grown in 2% glucose displayed monophasic kinetics with an intermediate-affinity (Km of 11.5 ± 1.5 mM). This work contributes to a better characterization of glucose transport in T. delbrueckii, with relevant implications for its exploitation in the food industry.

Functional characterization of an insulin-responsive glucose transporter (GLUT4) from fish adipose tissue

2004 ◽  
Vol 287 (2) ◽  
pp. E348-E357 ◽  
Author(s):  
Encarnación Capilla ◽  
Mònica Díaz ◽  
Amaya Albalat ◽  
Isabel Navarro ◽  
Jeffrey E. Pessin ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Plasma Membrane ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Intracellular Localization ◽  
Functional Characterization ◽  
Xenopus Laevis Oocytes ◽  
Native Form ◽  
Protein Motifs ◽  
Glucose Transporter Glut4

Glucose transport across the plasma membrane is mediated by a family of glucose transporter proteins (GLUTs), several of which have been identified in mammalian, avian, and, more recently, in fish species. Here, we report on the cloning of a salmon GLUT from adipose tissue with a high sequence homology to mammalian GLUT4 that has been named okGLUT4. Kinetic analysis of glucose transport following expression in Xenopus laevis oocytes demonstrated a 7.6 ± 1.4 mM Km for 2-deoxyglucose (2-DG) transport measured under zero- trans conditions and 14.4 ± 1.5 mM by equilibrium exchange of 3- O-methylglucose. Transport of 2-DG by okGLUT4-injected oocytes was stereospecific and was competed by d-glucose, d-mannose, and, to a lesser extent, d-galactose and d-fructose. In addition, 2-DG uptake was inhibited by cytochalasin B and ethylidene glucose. Moreover, insulin stimulated glucose uptake in Xenopus oocytes expressing okGLUT4 and in isolated trout adipocytes, which contain the native form of okGLUT4. Despite differences in protein motifs important for insulin-stimulated translocation of mammalian GLUT4, okGLUT4 was able to translocate to the plasma membrane from intracellular localization sites in response to insulin when expressed in 3T3-L1 adipocytes. These data demonstrate that okGLUT4 is a structural and functional fish homolog of mammalian GLUT4 but with a lower affinity for glucose, which could in part explain the lower ability of fish to clear a glucose load.

Functional characterization of mouse sodium/glucose transporter type 3b

2010 ◽  
Vol 299 (1) ◽  
pp. C58-C65 ◽  
Author(s):  
Oscar Aljure ◽  
Ana Díez-Sampedro
Keyword(s):  
Steady State ◽  
Human Genome ◽  
Conformational Changes ◽  
Glucose Transporter ◽  
Glucose Sensor ◽  
Functional Characterization ◽  
Sugar Transport ◽  
Tightly Coupled ◽  
Type 3

Despite belonging to a family of sugar cotransporters, human sodium/glucose transporter type 3 (hSGLT3) does not transport sugar, but it depolarizes the cell in the presence of extracellular sugar, and thus it has been suggested to work as a sugar sensor. In the human genome there is one SGLT3 gene, yet in mouse there are two. In this study we cloned one of them, mouse SGLT3b (mSGLT3b) and characterized the protein. We found that mSGLT3b has low affinity for sugars, as does hSGLT3, but surprisingly, mSGLT3b transports sugar, although the sugar transport is not as tightly coupled to cations as in SGLT1. Moreover, the sugar specificity of mSGLT3b has characteristics reminiscent of both SGLT1 and hSGLT3: mSGLT3b does not respond to galactose, similar to hSGLT3, but neither does it respond to 1-deoxynojirimycin, unlike hSGLT3 but similar to SGLT1. mSGLT3b has low apparent affinities for sugar and Na+ and, furthermore, displays pre-steady-state currents, which in SGLT1 report on conformational changes in the protein. Finally, phlorizin, the typical inhibitor of SGLT proteins, also inhibits mSGLT3b. In summary, although mSGLT3b has some characteristics that resemble SGLT1 and others that are similar to hSGLT3, its low sugar affinity and uncoupled sugar transport lead us to conclude that mSGLT3b likely functions as a physiological glucose sensor similar to hSGLT3.

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