MARC Record from University of Toronto

LEADER: 02092nam 2200241 4500
001 AAIMR16064
005 20070119093938.5
008 070119s2006 onc|||||||||||||| ||eng d
020 $a9780494160640
039 $feh
100 1 $aLuong, Winnie.
245 10 $aBiochemcial studies of the regulation of the gating of CIC-2.
260 $c2006.
300 $a89 leaves.
500 $aSource: Masters Abstracts International, Volume: 44-06, page: 2802.
502 $aThesis (M.Sc.)--University of Toronto, 2006.
506 $aElectronic version licensed for access by U. of T. users.
520 $aOxidation reversibly activates CIC-2, and a four-cysteine cluster was identified as being potentially important for oxidant-dependent activation. I assessed the role of these cysteines in activation following mutagenesis. Unlike C256A, mutagenesis of these cysteines to serines did not alter cell surface expression. This mutant lacked activation by oxidation as assessed using an iodide efflux assay. Therefore, these cysteines are likely involved with oxidation-dependent gating.CIC-2 is a voltage-gated chloride channel that is important in neuronal chloride homeostasis. Mutations of CIC-2 in humans cause epilepsy. Channel opening is controlled by two gates.Zinc inhibits CIC-2 by closing the slow gate. Cysteine 256 has been implicated in metal binding because its mutation to alanine abolishes metal-evoked inhibition. However, I found using affinity chromatography that C256 was not required for metal binding. Rather, the mutation altered protein abundance at the cell surface. Therefore, loss of metal-sensitive inhibition likely reflects decreased cell surface expression.
590 $aROBARTS MICROTEXT copy on microfiche.$5CaOTU
653 $aChemistry, Biochemistry.
856 41 $uhttp://link.library.utoronto.ca/eir/EIRdetail.cfm?Resources__ID=441985&T=F$yConnect to resource
949 $atheses masters$wALPHANUM$c1$i6063686-1001$j2$lMICROTEXT$mMEDIA_COMM$rN$sY$tMICROFORM$u2/2/2007
949 $aOnline resource 441985$wASIS$c1$i6063686-2001$lONLINE$mE_RESOURCE$rY$sY$tE_RESOURCE$u2/2/2007