Kuruma A, Hirayama Y, Hartzell H C
Department of Cell Biology, Emory University School of Medicine, Atlanta, Georgia 30322-3030, USA.
Am J Physiol Cell Physiol. 2000 Nov;279(5):C1401-13. doi: 10.1152/ajpcell.2000.279.5.C1401.
Heterologous expression of a variety of membrane proteins in Xenopus oocytes sometimes results in the appearance of a hyperpolarization-activated inward current. The nature of this current remains incompletely understood. Some investigators have suggested that this current is a Cl current, whereas others have identified it as a nonselective cation current. The purpose of this investigation was to characterize this current in more detail. The hyperpolarization-activated inward current (I(IN)) present in native oocytes was composed of a current carried at least partly by Ca and Mg under physiological ionic conditions plus a Ca-activated Cl current. The Ca-activated Cl current was blocked by chelation of cytosolic Ca with 1,2-bis(2-aminophenoxy)ethane-N,N,N', N'-tetraacetic acid. When Cl currents were blocked, the cation current could be carried by Ca, Mg, or Co, but not appreciably by Ba, Mn, or Cd. I(IN) was stimulated by intracellular acidification. The properties of I(IN) were quite different from those of the store-operated Ca current. Heterologous expression of transient receptor potential-like gene product (TRPL), one of the members of the transient receptor potential family of putative store-operated Ca channels, apparently resulted in alteration of the voltage sensitivity of the endogenous I(IN).
