Histidine suppresses zinc modulation of connexin hemichannels


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dc.contributor.author Chappell, Richard L.
dc.contributor.author Qian, Haohua
dc.contributor.author Zakevicius, Jane
dc.contributor.author Ripps, Harris
dc.date.accessioned 2006-02-13T19:43:16Z
dc.date.available 2006-02-13T19:43:16Z
dc.date.issued 2004-12
dc.identifier.citation Biological Bulletin 207 (2004): 188-190 en
dc.identifier.uri http://hdl.handle.net/1912/561
dc.description Author 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.abstract Zinc 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.sponsorship This 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.extent 318018 bytes
dc.format.mimetype application/pdf
dc.language.iso en_US en
dc.publisher Marine Biological Laboratory en
dc.relation.uri http://www.biolbull.org/cgi/content/short/205/2/209
dc.title Histidine suppresses zinc modulation of connexin hemichannels en
dc.type Article en

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