Secondary active transport

Counter-transport

An example of this system (also called antiport) begins with the sugar transporter described above. There are equal concentrations of glucose on both sides of the cell. A high concentration of galactose is then added outside the cell. Galactose competes with glucose for binding sites on the transport protein, so that mostly galactose—and a little glucose—enter the cell. The transporter itself, undergoing a conformational change, presents its binding sites for sugar at the inner face of the membrane. Here, at least transiently, glucose is in excess of galactose; it binds to the transporter and leaves the cell as the transporter switches back to its original conformation. Thus, glucose is pumped out of the cell against its gradient in exchange for the galactose riding into the cell down its own gradient.

Many counter-transport systems operate across the cell membranes of the body. A well-studied system (present in red blood cells, nerve cells, and muscle cells) pumps one calcium ion out of the cell in exchange for two or three sodium ions. This system helps maintain the low calcium concentration required for effective cellular activity. A different system, present in kidney cells, counter-transports hydrogen ions and sodium ions in a one-for-one ratio. This is important in stabilizing acidity by transporting hydrogen ions out of the body as needed.

Co-transport

In co-transport (sometimes called symport) two species of substrate, generally an ion and another molecule or ion, must bind simultaneously to the transporter before its conformational change can take place. As the driving substrate is transported down its concentration gradient, it drags with it the driven substrate, which is forced to move up its concentration gradient. The transporter must be able to undergo a conformational change when not bound to either substrate, so as to complete the cycle and return the binding sites to the side from which driving and driven substrates both move.

Sodium ions are usually the driving substrates in the co-transport systems of animal cells, which maintain high concentrations of these ions through primary active transport. The driven substrates include a variety of sugars, amino acids, and other ions. During the absorption of nutrients, for example, sugars and amino acids are removed from the intestine by co-transport with sodium ions. After passing across the glomerular filter in the kidney, these substrates are returned to the body by the same system. Plant and bacterial cells usually use hydrogen ions as the driving substrate; sugars and amino acids are the most common driven substrates. When the bacterium Escherichia coli must metabolize lactose, it co-transports hydrogen ions with lactose (which can reach a concentration 1,000 times higher than that outside the cell).

The sodium-potassium pump

Human red blood cells contain a high concentration of potassium and a low concentration of sodium, yet the plasma bathing the cells is high in sodium and low in potassium. When whole blood is stored cold under laboratory conditions, the cells lose potassium and gain sodium until the concentrations across the membrane for both ions are at equilibrium. When the cells are restored to body temperature and given appropriate nutrition, they extrude sodium and take up potassium, transporting both ions against their respective gradients until the previous high concentrations are reached. This ion pumping is linked directly to the hydrolysis of adenosine triphosphate (ATP), the cell’s repository of metabolic energy (see above Coupled chemical reactions). For every molecule of ATP split, three ions of sodium are pumped out of the cell and two of potassium are pumped in.

An enzyme called sodium-potassium-activated ATPase has been shown to be the sodium-potassium pump, the protein that transports the ions across the cell membrane while splitting ATP. Widely distributed in the animal kingdom and always associated with the cell membrane, this ATPase is found at high concentration in cells that pump large amounts of sodium (e.g., in mammalian kidneys, in salt-secreting glands of marine birds, and in the electric organs of eels). The enzyme, an intrinsic protein, exists in two major conformations whose interconversion is driven by the splitting of ATP or by changes in the transmembrane flows of sodium and potassium. When only sodium is present in the cell, the inorganic phosphate split from ATP during hydrolysis is transferred to the enzyme. Release of the chemically bound phosphate from the enzyme is catalyzed by potassium. Thus, the complete action of ATP splitting has been demonstrated to require both sodium (to catalyze the transfer of the phosphate to the enzyme) and potassium (to catalyze the release of the phosphate and free the enzyme for a further cycle of ATP splitting). Apparently, only after sodium has catalyzed the transferal of the phosphate to the enzyme can it be transported from the cell. Similarly, only after potassium has released the phosphate from the enzyme can it be transported into the cell. This overall reaction, completing the cycle of conformational changes in the enzyme, involves a strict coupling of the splitting of ATP with the pumping of sodium and potassium. It is this coupling that creates primary active transport.

The sodium-potassium pump extrudes one net positive charge during each cycle of ATP splitting. This flow of current induces an electric potential across the membrane that adds to the potentials brought about by the diffusion of ions through gated channels. The pump’s contribution to the overall potential is important in certain specialized nerve cells.