Baohai Shao, PhD
Title:
Research Assistant Professor, Department of Medicine, Division of Metabolism, Endocrinology and Nutrition
Email Address:
Background:
Baohai Shao received his PhD from the Zhejiang University, China in 2002. After completing postdoctoral training in the laboratory of Dr. Jay Heinecke, he joined the Diabetes and Obesity Center of Excellence as a Research Assistant Professor in the Department of Medicine at the University of Washington.
Focus:
HDL – the good form of cholesterol – removes cholesterol from macrophages, which plays a key role in protecting humans from atherosclerosis. However, not all forms of HDL are cardioprotective. Dr. Shao’s research focuses on the impact of oxidative modifications and diabetes on the anti-atherogenic effects of HDL. One major area of interest is myeloperoxidase, a heme enzyme secreted by macrophages. Dr. Shao is also interested in modification of HDL by glucose and reactive carbonyls that can covalently attach to amino acids and damage proteins. His research group uses cell biology together with tandem mass spectrometry to pinpoint specific amino acid residues in HDL that are damaged by reactive intermediates. Another major effort is directed towards developing sensitive mass spectrometric assays to identify novel HDL oxidation products in translational studies. Dr. Shao’s long term goal is to understand the role of oxidative reactions in the pathogenesis of atherosclerosis, diabetes and other inflammatory diseases in humans.
Representative Publications:
Shao B, Bergt C, Fu X, Green P, Voss JC, Oda MN, Oram JF, Heinecke JW. Tyrosine 192 in Apolipoprotein A-I is the Major Site of Nitration and Chlorination by Myeloperoxidase, but only Chlorination Markedly Impairs ABCA1-dependent Cholesterol Transport. J Biol Chem 280:5983-5993, 2005.
Shao B, Fu X, McDonald TO, Green PS, Uchida K, O'Brien KD, Oram JF, Heinecke JW. Acrolein impairs ABCA1-dependent cholesterol export from cells through site-specific modification of apolipoprotein A-I. J Biol Chem 280:36386-26396, 2005.
Shao B, Oda MN, Bergt C, Fu X, Green PS, Brot N, Oram JF, Heinecke JW. Myeloperoxidase Impairs ABCA1-dependent Cholesterol Efflux through Methionine Oxidation and Site-specific Tyrosine Chlorination of Apolipoprotein A-I. J Biol Chem 281:9001-9004, 2006.
Shao B, Oda MN, Oram JF, Heinecke JW. Myeloperoxidase: An Inflammatory Enzyme for Generating Dysfunctional HDL. Curr Opin Cardiol 21:322-328, 2006.
Shao B, Heinecke JW: Using MS/MS to Quantify Site-specific Chlorination and Nitration of Proteins: Model System Studies with High Density Lipoprotein Oxidized by Myeloperoxidase. Methods Enzymol. 440:33-63, 2008.
Shao B, Cavigiolio G, Brot N, Oda MN, Heinecke JW. Methionine oxidation impairs reverse cholesterol transport by apolipoprotein A-I. Proc Natl Acad Sci U S A 105:12224-12229, 2008.
Shao B, Oda MN, Oram JF, Heinecke JW: Myeloperoxidase. An oxidative pathway for generating dysfunctional HDL. Chem Res Toxicol 23:447-454, 2010.
Shao B, Tang C, Heinecke JW, Oram JF: Oxidation of apolipoprotein A-I by myeloperoxidase impairs the initial interactions with ABCA1 required for signaling and cholesterol export. J Lipid Res 51:1849-1858, 2010.
Shao B, Pennathur S, Pagani I, Oda MN, Witztum JL, Oram JF, Heinecke JW. Modifying apolipoprotein A-I by malondialdehyde, but not by an array of other reactive carbonyls, blocks cholesterol efflux by the ABCA1 pathway. J Biol Chem 285:18473-18484, 2010.
Current Collaborations:
Within the Diabetes and Obesity Center of Excellence and its Affiliated Members
Jay Heinecke, MD
Chongren Tang, PhD
Renee LeBoeuf, PhD
Karin Bornfeldt, PhD
Tomas Vaisar, PhD
Andy Hoofnagle, MD, PhD
Lev Becker, PhD
Outside the Diabetes and Obesity Center of Excellence
Gail Jarvik, MD, PhD, University of Washington
Michael Oda, PhD, Children’s Hospital Oakland Research Institute
Subramaniam Pennathur, MD, University of Michigan
Sean Davidson, PhD, University of Cincinnati
Christine C. Winterbourn, PhD, University of Otago, New Zealand