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Facilitated Diffusion and Carrier Proteins

Facilitated diffusion, like passive diffusion, involves the movement of molecules in the direction determined by their relative concentrations inside and outside of the cell. No external source of energy is provided, so molecules travel across the membrane in the direction determined by their concentration gradients and, in the case of charged molecules, by the electric potential across the membrane. However, facilitated diffusion differs from passive diffusion in that the transported molecules do not dissolve in the phospholipid bilayer. Instead, their passage is mediated by proteins that enable the transported molecules to cross the membrane without directly interacting with its hydrophobic interior. Facilitated diffusion therefore allows polar and charged molecules, such as carbohydrates, amino acids, nucleosides, and ions, to cross the plasma membrane.

Two classes of proteins that mediate facilitated diffusion are generally distinguished: carrier proteins and channel proteins. Carrier proteins bind specific molecules to be transported on one side of the membrane. They then undergo conformational changes that allow the molecule to pass through the membrane and be released on the other side. In contrast, channel proteins (see the next section) form open pores through the membrane, allowing the free diffusion of any molecule of the appropriate size and charge.

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Carrier proteins are responsible for the facilitated diffusion of sugars, amino acids, and nucleosides across the plasma membranes of most cells. The uptake of glucose, which serves as a primary source of metabolic energy, is one of the most important transport functions of the plasma membrane, and the glucose transporter provides a well-studied example of a carrier protein. The glucose transporter was initially identified as a 55-kd protein in human red blood cells, in which it represents approximately 5% of total membrane protein. Subsequent isolation and sequence analysis of a cDNA clone revealed that the glucose transporter has 12 α-helical transmembrane segments—a structure typical of many carrier proteins (Figure 12.16). These transmembrane α helices contain predominantly hydrophobic amino acids, but several also contain polar amino acid residues that are thought to form the glucose-binding site in the interior of the protein.

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As with many membrane proteins, the three-dimensional structure of the glucose transporter is not known, so the molecular mechanism of glucose transport remains an open question. However, kinetic studies indicate that the glucose transporter functions by alternating between two conformational states (Figure 12.17). In the first conformation, a glucose-binding site faces the outside of the cell. The binding of glucose to this exterior site induces a conformational change in the transporter, such that the glucose-binding site now faces the interior of the cell. Glucose can then be released into the cytosol, followed by the return of the transporter to its original conformation.

Most cells, including erythrocytes, are exposed to extracellular glucose concentrations that are higher than those inside the cell, so facilitated diffusion results in the net inward transport of glucose. Once glucose is taken up by these cells it is rapidly metabolized, so intracellular glucose concentrations remain low and glucose continues to be transported into the cell from the extracellular fluids. Because the conformational changes of the glucose transporter are reversible, however, glucose can be transported in the opposite direction simply by reversing the steps in Figure 12.17. Such reverse flow occurs, for example, in liver cells, in which glucose is synthesized and released into the circulation.

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