Staff View
Limiting oxidation in potassium channel kv2.1 using cysteine-alanine mutation

Descriptive

TitleInfo
Title
Limiting oxidation in potassium channel kv2.1 using cysteine-alanine mutation
Name (type = personal)
NamePart (type = family)
Royal
NamePart (type = given)
Remi
NamePart (type = date)
1989-
DisplayForm
Remi Royal
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Sesti
NamePart (type = given)
Federico
DisplayForm
Federico Sesti
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Jacinto
NamePart (type = given)
Estela
DisplayForm
Estela Jacinto
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Fan
NamePart (type = given)
Huizhou
DisplayForm
Huizhou Fan
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2013
DateOther (qualifier = exact); (type = degree)
2013-01
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
The Kv2.1 (KCNB1) channel is expressed in the cortex and hippocampus. Interaction between cysteine residues of the kv2.1 channel plays a role in the formation of disulfide bonds. Disulfide bond formation following oxidative stress suggests that cysteine interaction in voltage-gated K+ channel kv2.1 plays a key role in the oxidation of kv2.1. Previous research has shown that oxidation of potassium (K+) channels by reactive oxygen species (ROS) is a major factor in the loss of neuronal function [6]. The purpose of this study was to use cysteine-alanine mutations to prevent oxidation of K+ channel kv2.1. In this thesis, the anti-oxidant properties of the double mutant C73AC29A were investigated. The affects were observed using site-directed mutagenesis and the polymerase chain reaction (PCR). PCR was utilized to form a double mutant between C73A and C29A. SDS-Page and Western Blot analysis were used to analyze whether there was more or less oxidation in the double mutant C73AC29A compared to that of the kv2.1 control. The double mutant C73AC29A showed protective properties, showing less oxidation than the kv2.1 control when placed under oxidative stress. Findings suggest that C73AC29A could provide protection from oxidation-induced loss of function in the kv2.1 channel.
Subject (authority = RUETD)
Topic
Physiology and Integrative Biology
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_4503
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
vii, 33 p. : ill.
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Remi Royal
Subject (authority = ETD-LCSH)
Topic
Potassium channels
Subject (authority = ETD-LCSH)
Topic
Potassium--Oxidation
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000067828
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3NP234P
Genre (authority = ExL-Esploro)
ETD graduate
Back to the top

Rights

RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2013-01-09 14:53:21
AssociatedEntity
Name
Remi Royal
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
RightsEvent
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2013-01-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2013-08-02
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after August 2nd, 2013.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
Back to the top

Technical

RULTechMD (ID = TECHNICAL1)
ContentModel
ETD
OperatingSystem (VERSION = 5.1)
windows xp
Back to the top
Version 8.3.13
Rutgers University Libraries - Copyright ©2021