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World J Cardiol. Aug 26, 2013; 5(8): 305-312
Published online Aug 26, 2013. doi: 10.4330/wjc.v5.i8.305
Published online Aug 26, 2013. doi: 10.4330/wjc.v5.i8.305
Blood cellular mutant LXR-α protein stability governs initiation of coronary heart disease
Mansi Arora, Deepak Kaul, Yash Paul Sharma, Department of Experimental Medicine, Biotechnology and Cardiology, Post Graduate Institute of Medical Education and Research, Chandigarh 160012, India
Author contributions: Kaul D designed the study; Arora M executed the study; Sharma YP provided the blood samples.
Supported by Indian Council of Medical Research, New Delhi, India
Correspondence to: Deepak Kaul, PhD, Professor and Head, Departments of Experimental Medicine, Biotechnology and Cardiology, Post Graduate Institute of Medical Education and Research, Pin-133001, Chandigarh 160012, India. dkaul-24@hotmail.com
Telephone: +91-172-2755228 Fax: +91-172-2744401
Received: March 3, 2013
Revised: June 3, 2013
Accepted: July 18, 2013
Published online: August 26, 2013
Processing time: 182 Days and 17.3 Hours
Revised: June 3, 2013
Accepted: July 18, 2013
Published online: August 26, 2013
Processing time: 182 Days and 17.3 Hours
Core Tip
Core tip: The present study proposes that the stability of mutant liver X receptor-α (LXR-α) protein in blood mononuclear cells of human coronary heart disease (CHD) subjects is governed by its ubiquitination dependent degradation by [breast and ovarian cancer susceptibility 1 (BRCA1)-associated RING domain1 (BARD1)]/BRCA1 E3 ubiquitin ligase complex. Additionally, BARD1/BRCA1 expression shows an increasing trend with respect to severity of coronary occlusion. This degradation is rescued to some extent by the ability of Vitamin D3 to bind mutant LXR-α protein thus providing warranted evidence that dietary supplementation of Vitamin D3 in such subjects may be exploited therapeutically.