Our Research: Faculty/Research Laboratories

Baohai Shao, PhD

Research Assistant Professor, Department of Medicine, Division of Metabolism, Endocrinology and Nutrition

Email Address: bhshao@u.washington.edu

Division of Metabolism, Endocrinology and Nutrition Website:  http://depts.washington.edu/metab/

Baohai Shao, PhD

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, 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, 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.

Shao B, Heinecke JW. Impact of HDL oxidation by the myeloperoxidase system on sterol efflux by the ABCA1 pathway. J Proteomics. 74: 2289-2299, 2011.

Shao B, Pennathur S, Heinecke JW. Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions. J Biol Chem. 287: 6375-6386, 2012.

Shao B. Site-specific oxidation of apolipoprotein A-I impairs cholesterol export by ABCA1, a key cardioprotective function of HDL. Biochim Biophys Acta. 1821: 490-501, 2012

  • Sui X, Wang Z, Shao B. Extraction Chromatograph Separation Spark Source Mass Spectrometric Analysis of 14 Rare Earth Impurities in High Purity Rare Earth Oxide. Anal Sci Technol 8:553-559, 1995.

    Shao B, Wang Z, Sui X. Development of Rare Earths Separation by Extraction Chromatography. Chinese J Anal Chem 25:597-603, 1997.

    Shao B, Yan J, Xu X, Fu X. Determination of Constituents in Hair Dyes by Reversed-phase High-performance Liquid Chromatography. Chinese Chem Lett 11:471-472, 2000.

    Shao B, Xu X, Yan J, Fu X: Quantitative Determination of Commercial Oxidation Hair Dyes by Reversed-phase HPLC. J Liq Chromatogr R T 24:241-249, 2001.

    Shao B, Xu X, Zou L, Cai X, Fu X. Enantioseparation of racemic naproxen esters on four cellulose derivative chiral columns and chiral recognition mechnism. Acta Chimica Sinica 59:1982-8, 2001.

    Xu X, Zou L, Hu M, Shao B. Enantiomeric separation of amino alcohols by ion-pair chromatography. Chinese J Anal Chem 29:1295-1298, 2001.

    Shao B, Xu X, Zou L, Fu X. Enantioseparation of Racemic Naproxen Esters on Cellulose Tris (4-Methylbenzoate) Chiral Stationary Phase. Chinese Chem Lett 13:151-152, 2002.

    Shao B, Xu X, Lu J, Fu X. Cellulose-based Chiral Stationary Phases for High-performace Liquid Chromatographic Enantioseparation. Chinese J Anal Chem 31:239-244, 2003.

    Shao B, Xu X, Lu J, Fu X. Enantioseparation of Three Kinds of Methoxyflavanone on Cellulose Derivative Chiral Columns and Chiral Recognition Mechanism. Acta Chim Sinica 61:440-444, 2003.

    Shao B, Xu X, Lu J, Zou L, Fu X. Influence of Mobile Phase Composition on the Enantioseparation of Methoxyflavanones with Self-prepared CDMPC Column. Chinese Chem Lett 14:401-403 2003.

    Shao B, Xu X, Lu J, Cai X, Zou L, Fu X. Comparison of enantioseparation and chiral recognition mechanism of racemic naproxen esters on (S, S)-whelk-O 1 and CDMPC chiral columns. Acta Chim Sinica 61:1635-1640, 2003.

    Shao B, Xu X, Wu Q, Lu J, Fu X: Comparative Enantioseparation of 2-Arylpropionic Acid Esters on Cellulose Derivative and (S,S)-Whelk-O 1 Columns. J Liq Chromatogr R T 28:63-80, 2005.

    Pennathur S, Bergt C, Shao B, Byun J, Kassim SY, Singh P, McDonald TO, Brunzell J, Chait A, Oram JF, O’Brien K, Geary RL, Heinecke JW: Human atherosclerotic intima and blood of patients with established coronary artery disease contain high density lipoprotein damaged by reactive nitrogen species. J. Biol. Chem. 279:42977-42983, 2004.

    Shao B, O’Brien KD, McDonald TO, Fu X, Oram JF, Uchida K, Heinecke JW. Acrolein Modifies Apolipoprotein A-I in the Human Artery Wall. Ann N Y Acad Sci 1043:396-403, 2005.

    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, Belaaouaj A, Verlinde CL, Fu X, Heinecke JW: Methionine Sulfoxide and Proteolytic Cleavage Contribute to the Inactivation of Cathepsin G by Hypochlorous Acid: An Oxidative Mechanism for Regulation of Serine Proteinases by Myeloperoxidase. J Biol Chem 280:29311-29321, 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 280:36386-36396, 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, Vaisar T, Oram JF, Heinecke JW. Pathways for Oxidation of High Density Lipoprotein in Human Cardiovascular Disease. Curr Opin Mol Ther 8:198-205, 2006.

    Shao B, Oda MN, Oram JF, Heinecke JW.Myeloperoxidase: an inflammatory enzyme for generating dysfunctional high density lipoprotein. Curr Opin Cardiol 21:322-328, 2006.

    Vaisar T, Shao B, Green PS, Oda MN, Oram JF, Heinecke JW. Myeloperoxidase and inflammatory proteins: Pathways for generating dysfunctional high-density lipoprotein in humans. Curr Atheroscler Rep 9:417-44, 2007.

    Wang Y, Rosen H, Madtes DK, Shao B, Martin TR, Heinecke JW, Fu X. Myeloperoxidase inactivates TIMP-1 by oxidizing its N-terminal cysteine residue: An oxidative mechanism for regulating proteolysis during inflammation. J Biol Chem 282:31826-31834, 2007.

    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.

    Cavigiolio G, Shao B, Geier EG, Ren G, Heinecke JW, Oda MN. The interplay between size, morphology, stability, and functionality of high-density lipoprotein subclasses. Biochemistry. 47:4770-4779, 2008.

    Wang XS, Shao B, Oda MN, Heinecke JW, Mahler S, Stocker R. A sensitive and specific ELISA detects methionine sulfoxide-containing apolipoprotein A-I in HDL. J Lipid Res 50:586-594, 2009.

    Shao B, Heinecke JW. HDL, lipid peroxidation, and atherosclerosis. J Lipid Res 50:599-601, 2009.

    Shao B, Oda MN, Oram JF, Heinecke JW. Myeloperoxidase: an oxidative pathway for generating dysfunctional high-density lipoprotein. 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.

    Crouch EC, Hirche TO, Shao B, Boxio R, Wartelle J, Benabid R, McDonald B, Heinecke J, Matalon S, Belaaouaj A. Myeloperoxidase-dependent inactivation of surfactant protein D in vitro and in vivo. J Biol Chem 285:16757-16770, 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 reactiv. carbonyls, blocks cholesterol efflux by the ABCA1 pathway. J Biol Chem 285:18473-18484, 2010.

    Cavigiolio G, Geier EG, Shao B, Heinecke JW, Oda MN. Exchange of apolipoprotein A-I between lipid-associated and lipid-free states: a potential target for oxidative generation of dysfunctional high density lipoproteins. J Biol Chem 285:18847-18857, 2010.

    Shao B, Heinecke JW. Impact of HDL oxidation by the myeloperoxidase system on sterol efflux by the ABCA1 pathway. J Proteomics. 74: 2289-2299, 2011.

    Shao B, Pennathur S, Heinecke JW. Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions. J Biol Chem. 287: 6375-6386, 2012.

    Shao B. Site-specific oxidation of apolipoprotein A-I impairs cholesterol export by ABCA1, a key cardioprotective function of HDL. Biochim Biophys Acta. 1821: 490-501, 2012

 

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

Outside the Diabetes and Obesity Center of Excellence
Jonathan Himmelfarb, MD, University of Washington
Ian de Boer, MD, MS, University of Washington
Gail Jarvik, MD, PhD, University of Washington
Michael Oda, PhD, Children’s Hospital Oakland Research Institute
Subramaniam Pennathur, MD, University of Michigan