Showing papers by "Margaret P. Price published in 1998"
TL;DR: Although PPK did not form channels on its own, it associated with and reduced the current generated by a related human brain Na+ channel, suggesting that it may be a channel subunit involved in mechanosensation.
Abstract: Drosophila melanogaster has proven to be a good model for understanding the physiology of ion channels. We identified two novel Drosophila DEG/ ENaC proteins, Pickpocket (PPK) and Ripped Pocket (RPK). Both appear to be ion channel subunits. Expression of RPK generated multimeric Na+ channels that were dominantly activated by a mutation associated with neurodegeneration. Amiloride and gadolinium, which block mechanosensation in vivo, inhibited RPK channels. Although PPK did not form channels on its own, it associated with and reduced the current generated by a related human brain Na+ channel. RPK transcripts were abundant in early stage embryos, suggesting a role in development. In contrast, PPK was found in sensory dendrites of a subset of peripheral neurons in late stage embryos and early larvae. In insects, such multiple dendritic neurons play key roles in touch sensation and proprioception and their morphology resembles human mechanosensory free nerve endings. These results suggest that PPK may be a channel subunit involved in mechanosensation.
262 citations
TL;DR: The finding of the gamma subunit of ENaC localized to the site of mechanotransduction in baroreceptor nerve terminals innervating the aortic arch and carotid sinus suggests that ENac subunits may be components of the barorecept mechanotranducer and pave the way to a better definition of mechanisms responsible for blood pressure regulation and hypertension.
199 citations
TL;DR: Data indicate that protons induce a reversible conformational change that activates BNC1 thereby exposing residue 430 to the extracellular solution and once Cys-430 is modified with a large chemical group, the channel is prevented from relaxing back to the inactive state.
74 citations