Use of cultured epithelia to study transport and its regulation.
Epithelial cells from a variety of species and organs form polarized epithelia in culture. When epithelia are grown on a porous surface, such as a millipore filter, transport can be studied using adaptations of standard techniques. In the few years in which cultured epithelia have been studied by transport physiologists, most work has been focused on identification and description of the differentiated transport exhibited by cultured epithelia. Epithelia formed by a continuous line of cells derived from pig kidney (LLC-PK1) exhibit sodium-coupled glucose transport similar to that of the proximal tubule and have vasopressin-sensitive adenylate cyclase that has been studied in great detail. Also of interest are epithelia formed by continuous lines of cells derived from amphibian kidney (A6) and from amphibian urinary bladder (TBM). Each line forms epithelia that have high electrical resistance and amiloride-sensitive sodium transport. Transport is stimulated by aldosterone and by cAMP or hormones that raise cell cAMP levels. In LLC-PK1 and in A6 epithelia, transport and the response to hormones can be manipulated by manipulating the culture conditions. Cultured epithelia have also been used to explore the cell biology of epithelia. Most interesting in this regard are studies of the development and maintenance of epithelial cell polarity. This approach should be especially valuable.
D000450:Aldosterone / Q000502:physiology; D000818:Animals; D001692:Biological Transport; D002460:Cell Line; D002950:Citrate (si)-Synthase; D046508:Culture Techniques; D004847:Epithelial Cells; D004848:Epithelium / Q000502:physiology*; D007365:Intercellular Junctions / Q000502:physiology; D007668:Kidney / Q000502:physiology; D008564:Membrane Potentials; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism; D001743:Urinary Bladder / Q000502:physiology; D014882:Water-Electrolyte Balance
D000450:Aldosterone; D002950:Citrate (si)-Synthase; D000254:Sodium-Potassium-Exchanging ATPase