Glucose transporters: physiological and pathological roles
- 620 Downloads
Glucose is a primary energy source for most cells and an important substrate for many biochemical reactions. As glucose is a need of each and every cell of the body, so are the glucose transporters. Consequently, all cells express these important proteins on their surface. In recent years developments in genetics have shed new light on the types and physiology of various glucose transporters, of which there are two main types—sodium–glucose linked transporters (SGLTs) and facilitated diffusion glucose transporters (GLUT)—which can be divided into many more subclasses. Transporters differ in terms of their substrate specificity, distribution and regulatory mechanisms. Glucose transporters have also received much attention as therapeutic targets for various diseases. In this review, we attempt to present a simplified view of this complex topic which may be of interest to researchers involved in biochemical and pharmacological research.
KeywordsSGLT GLUT Glucose transporters Anti-diabetic agents Anti-cancer agents
Compliance with Ethical Standards
Conflicts of interest
Archana M. Navale declares that she has no conflict of interest.
Archana N. Paranjape declares that she has no conflict of interest.
This article does not contain any studies with human participants or animals performed by any of the authors.
- Asano T, Katagiri H, Takata K, Lin JL, Ishihara H, Inukai K et al (1991) The role of N-glycosylation of GLUT1 for glucose transport activity. J Biol Chem 266:24632–24636Google Scholar
- Lazaridis KN, Pham L, Vroman B, De Groen PC, LaRusso NF (1997) Kinetic and molecular identification of sodium-dependent glucose transporter in normal rat cholangiocytes. Am J Physiol Gastrointest Liver Physiol 272:G1168–G1174Google Scholar
- Scheepers A, Schmidt S, Manolescu A, Cheeseman CI, Bell A, Zahn C et al (2005) Characterization of the human SLC2A11 (GLUT11) gene: alternative promoter usage, function, expression, and subcellular distribution of three isoforms, and lack of mouse orthologue. Mol Membr Biol 22:339–351CrossRefPubMedGoogle Scholar