NDLI: Regulation of Large Conductance $Ca^{2+}-activated$ $K^{+}$ (BK) Channel β1 Subunit Expression by Muscle RING Finger Protein 1 in Diabetic Vessels

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Regulation of Large Conductance $Ca^{2+}-activated$ $K^{+}$ (BK) Channel β1 Subunit Expression by Muscle RING Finger Protein 1 in Diabetic Vessels

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Regulation of Large Conductance $Ca^{2+}-activated$ $K^{+}$ (BK) Channel β1 Subunit Expression by Muscle RING Finger Protein 1 in Diabetic Vessels

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Huan Shen, Win-kuang Lu, Tong Lee, Hon-chi Yi, Fu Wang, Xiaoli Willis, Monte S. Chai, Qiang
Description	Author Affiliation: Yi F ( From the Department of Internal Medicine, Mayo Clinic, Rochester, Minnesota 55905.)
Abstract	The large conductance Ca(2+)-activated K(+) (BK) channel, expressed abundantly in vascular smooth muscle cells (SMCs), is a key determinant of vascular tone. BK channel activity is tightly regulated by its accessory ß1 subunit (BK-ß1). However, BK channel function is impaired in diabetic vessels by increased ubiquitin/proteasome-dependent BK-ß1 protein degradation. Muscle RING finger protein 1 (MuRF1), a muscle-specific ubiquitin ligase, is implicated in many cardiac and skeletal muscle diseases. However, the role of MuRF1 in the regulation of vascular BK channel and coronary function has not been examined. In this study, we hypothesized that MuRF1 participated in BK-ß1 proteolysis, leading to the down-regulation of BK channel activation and impaired coronary function in diabetes. Combining patch clamp and molecular biological approaches, we found that MuRF1 expression was enhanced, accompanied by reduced BK-ß1 expression, in high glucose-cultured human coronary SMCs and in diabetic vessels. Knockdown of MuRF1 by siRNA in cultured human SMCs attenuated BK-ß1 ubiquitination and increased BK-ß1 expression, whereas adenoviral expression of MuRF1 in mouse coronary arteries reduced BK-ß1 expression and diminished BK channel-mediated vasodilation. Physical interaction between the N terminus of BK-ß1 and the coiled-coil domain of MuRF1 was demonstrated by pulldown assay. Moreover, MuRF1 expression was regulated by NF-κB. Most importantly, pharmacological inhibition of proteasome and NF-κB activities preserved BK-ß1 expression and BK-channel-mediated coronary vasodilation in diabetic mice. Hence, our results provide the first evidence that the up-regulation of NF-κB-dependent MuRF1 expression is a novel mechanism that leads to BK channelopathy and vasculopathy in diabetes.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	15
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-04-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Diabetic Angiopathies Metabolism Gene Expression Regulation Large-Conductance Calcium-Activated Potassium Channel Beta Subunits Muscle Proteins Ubiquitin-Protein Ligases Animals Cells, Cultured Coronary Vessels Diabetes Mellitus, Experimental Electrophysiology HEK293 Cells Mice Mice, Inbred C57BL Microscopy, Video Muscle, Smooth, Vascular Cytology Mutation NF-kappa B Proteasome Endopeptidase Complex Protein Structure, Tertiary Up-Regulation Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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