title: Sodium absorption, volume control and potassium channels: in tribute to a great biologist.
abstract: It is well established, for all Na-absorbing epithelia, that an increase in the rate of transcellular Na+ absorption is accompanied by an increase in the conductance of the basolateral membrane to K+. For the case of small intestinal epithelial cells from the salamander Necturus maculosus, where the rate of transcellular Na+ absorption can be increased manyfold by the addition of sugars or amino acids to the luminal bathing solution, it appears that this parallelism between Na-K pump rate and basolateral membrane K+ conductance is closely related to volume regulation by the enterocyte. Recent studies have disclosed the presence of stretch-activated K+ channels, in a highly enriched basolateral membrane fraction isolated from these epithelial cells, whose activity is increased by an increase in vesicle volume and inhibited by a decrease in vesicle volume or ATP. The activity of this channel also appears to be regulated by the degree of organization of the cortical actin cytoskeleton; activity is increased by depolymerization of the actin cytoskeleton and decreased by repolymerization of that structure. We postulate that the inhibitory effect of ATP is related to its role in promoting the polymerization of G-actin to form F-actin. We propose that enterocyte swelling that results from the intracellular accumulation of sugars or amino acids in osmotically active forms brings about disorganization of the cortical actin cytoskeleton and activates these channels and is, at least in part, responsible for the "pump-leak parallelism" in this amphibian.
authors.affiliation: Department of Integrative Biology and Pharmacology, University of Texas Medical School, P.O. Box 20708, Houston, TX 77225, USA. stanley.g.schultz@uth.tmc.edu
authors.forename: S G
authors.initials: SG
authors.lastname: Schultz
authors.forename: W P
authors.initials: WP
authors.lastname: Dubinsky
mesh_terms: D000042:Absorption / Q000502:physiology; D000409:Alanine / Q000737:chemistry; D000818:Animals; D001001:Anura; D017097:Electric Impedance; D020895:Enterocytes / Q000166:cytology* / Q000378:metabolism; D023421:Models, Animal; D009338:Necturus maculosus; D011188:Potassium / Q000378:metabolism*; D015221:Potassium Channels / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism / Q000493:pharmacokinetics*; D000254:Sodium-Potassium-Exchanging ATPase / Q000502:physiology*; D014981:Xenopus
chemical_list: D015221:Potassium Channels; D012964:Sodium; D000254:Sodium-Potassium-Exchanging ATPase; D000409:Alanine; D011188:Potassium