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dc.contributor.authorChappell, Richard L.  Concept link
dc.contributor.authorQian, Haohua  Concept link
dc.contributor.authorZakevicius, Jane  Concept link
dc.contributor.authorRipps, Harris  Concept link
dc.date.accessioned2006-02-13T19:43:16Z
dc.date.available2006-02-13T19:43:16Z
dc.date.issued2004-12
dc.identifier.citationBiological Bulletin 207 (2004): 188-190en
dc.identifier.urihttp://hdl.handle.net/1912/561
dc.descriptionAuthor Posting. © Marine Biological Laboratory, 2004. This article is posted here by permission of Marine Biological Laboratory for personal use, not for redistribution. The definitive version was published in Biological Bulletin 207 (2004): 188-190.
dc.description.abstractZinc has been shown to modulate hemichannel currents of connexins Cx35 and Cx38 in Xenopus oocytes. In both cases the effects were biphasic; i.e., low concentrations of zinc enhanced, whereas higher concentrations decreased, the magnitudes of the voltage-activated hemichannel currents. The present study was designed to determine the effects of zinc on hemichannels formed by Cx26, a connexin reportedly expressed on dendrites of carp horizontal cells and implicated in a mechanism for photoreceptor feedback. In addition, we examined whether histidine, a zinc chelator, would block the action of zinc on Cx26 hemichannel currents, or would exert a direct effect on those currents.en
dc.description.sponsorshipThis work was supported in part by Fight for Sight, PSC/CUNY Grant 66257-0035, and NCRR/NIH RCMI Award RR-03037 (RLC); NIH Grants EY-06516 (HR), EY-14557 (HR), EY-12028 (HQ); and a Senior Research Investigator Award from Research to Prevent Blindness (HR).en
dc.format.extent318018 bytes
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen
dc.publisherMarine Biological Laboratoryen
dc.relation.urihttps://doi.org/10.2307/1543206
dc.titleHistidine suppresses zinc modulation of connexin hemichannelsen
dc.typeArticleen
dc.identifier.doi10.2307/1543206


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