Glucose transmembrane transport

Kobori M, Shinmoto H, Tsushida T, Shinohara K (1997) Phloretin-induced apoptosis in B16 melanoma 4A5 cells by inhibition of glucose transmembrane transport. Cancer Lett 119 207... 

Many transmembrane transporter proteins, termed secondary transporters, use the discharge of an ionic gradient to power the uphill translocation of a solute molecule across membranes. Couphng solute movement to ion transport enables these secondary transporters to concentrate solutes by a factor of 10 with a solute flux 10 faster than by simple diffusion. We have already encountered the co-transport of leucine and Na+ by LeuT, but there are many other examples. Sugars and amino acids can be transported into cells by Na+-dependent symports. Dietary glucose is concentrated in the epithelial cells of the small intestine by a Na -dependent symport, and is then... 

FIGURE 10.5 A model for the arrangement of the glucose transport protein in the erythrocyte membrane. Hydropathy analysis is consistent with 12 transmembrane helical segments. 

The insulin receptor is a transmembrane receptor tyrosine kinase located in the plasma membrane of insulin-sensitive cells (e.g., adipocytes, myocytes, hepatocytes). It mediates the effect of insulin on specific cellular responses (e.g., glucose transport, glycogen synthesis, lipid synthesis, protein synthesis). 

Figure 46-5. Variations in the way in which proteins are inserted into membranes. This schematic representation, which illustrates a number of possible orientations, shows the segments of the proteins within the membrane as a-helicesand the other segments as lines. The LDL receptor, which crosses the membrane once and has its amino terminal on the exterior, is called a type I transmembrane protein. The asialoglycoprotein receptor, which also crosses the membrane once but has its carboxyl terminal on the exterior, is called a type II transmembrane protein. The various transporters indicated (eg, glucose) cross the membrane a number of times and are called type III transmembrane proteins they are also referred to as polytopic membrane proteins. (N, amino terminal C, carboxyl terminal.) (Adapted, with permission, from Wickner WT, Lodish HF Multiple mechanisms of protein insertion into and across membranes. Science 1985 230 400. Copyright 1985 by the American Association for the Advancement of Science.)...

SLC2 (solute carrier) superfamily consists of 12 glucose transporters (GLUT1-12) and one H+-myo-inositol cotransporter (HMIT or GLUT13). They all have 12 transmembrane segments with the N- and C-termini both on the cytoplasmic aspect and a specific N-linked oligosaccharide side-chain on either the first or fourth extracellular loop. 

That is, the cotransporter can pump glucose inward until its concentration within the epithelial cell is about 9,000 times that in the intestine. As glucose is pumped from the intestine into the epithelial cell at the apical surface, it is simultaneously moved from the cell into the blood by passive transport through a glucose transporter (GLUT2) in the basal surface (Fig. 11-44). The crucial role of Na+ in symport and antiport systems such as these requires the continued outward pumping of Na+ to maintain the transmembrane Na+ gradient. 

---