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A Study on the Interaction of Cardiac Potassium Channels

Author: SunZuo
Tutor: DingJiuPing
School: Huazhong University of Science and Technology
Course: Biophysics
Keywords: Potassium channel KCNQ1 KCNE1 ER retention
CLC: Q46
Type: Master's thesis
Year: 2007
Downloads: 92
Quote: 0
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Abstract


Contains a variety of ion channels, including sodium ion channel , a potassium ion channel , a calcium ion channel and a chloride ion channel in the heart , wherein compared to the other ion channels , potassium channels , not only the number of channels and the type of complex . Potassium channels with congenital long QT syndrome cardiac potassium channel become a hot research topic . The potassium channel , KCNQ1 belongs to voltage-gated potassium channels , first discovered in a chromosomal loci inherited LQT syndrome , and associated with the inherited LQT syndrome . KCNE1 gene encoding the potassium channel protein, is an important regulator of the KCNQ channel subunits . KCNQ1 and KCNE1 normal combination of KCNQ channel function was normal guarantee . Sites and the role of the form of this interaction is still inconclusive. The study showed that more than 50% of LQTS KCNQ1 or KCNE1 gene mutation , the reason why these mutations lead to channel the changing nature of the real reason is still an unsolved mystery . The task of this project is to KCNQ1 and KCNE1 preliminary studies with these questions . Experiments by building KCNQ1 and KCNE1 plasmid and on the plasmid for the corresponding mutations , respectively expressed in HEK-293 and CHO cells . Immunofluorescence imaging and fluorescent protein imaging optical observation and analysis , and application of changes in the electrophysiological characteristics of the detected current . The results show that on the KCNQ1 RXR this may be , X is a hydrophobic weakening will lead to KCNQ1 expression level of the membrane also weakens the structure of the ER retention signal . KCNE1 different results expressed in HEK-293 and CHO cells alone also laid a foundation for further study of KCNQ1 and KCNE1 binding sites and mode of action .

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CLC: > Biological Sciences > Physiology > Circulation physiology
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