title: Opsin exhibits cGMP-activated single-channel activity.
abstract: Low concentrations of cGMP evoked reversible single-channel currents in patches excised from liposomes that contained purified bovine opsin. Two elementary conductances, of 32 and 17 pS, were observed in the presence of 10-200 microM cGMP. Both individual channel openings (mean open times, approximately 1.6 ms for the 32-pS conductance and approximately 1.0 ms for the 17-pS conductance) and bursts of openings (mean burst duration, approximately 2-3 ms for the large events) were observed. The cGMP-activated channel activity could be observed in the presence or absence of Ca2+. These results raise the possibility that opsin or rhodopsin, an opsin/rhodopsin isoform, or an opsin/isoform multimer serves as a cGMP-modulated pore in the rod outer segment.
authors: Department of Ophthalmology and Visual Science, Yale University School of Medicine, New Haven, CT 06510.
authors: J W
authors: JW
authors: Clack
authors: P J
authors: PJ
authors: Stein
mesh_terms: D000818:Animals; D002417:Cattle; D006152:Cyclic GMP / Q000494:pharmacology*; D004553:Electric Conductivity; D005136:Eye Proteins / Q000494:pharmacology*; D007473:Ion Channels / Q000187:drug effects* / Q000502:physiology; D012374:Rod Cell Outer Segment / Q000187:drug effects / Q000502:physiology; D017299:Rod Opsins
chemical_list: D005136:Eye Proteins; D007473:Ion Channels; D017299:Rod Opsins; D006152:Cyclic GMP