EDUCATION AND TRAINING

Chemistry, Ph.D. Zhejiang University,  Hangzhou,  PR China

OFFICE ADDRESS

University of Washington School of Medicine
1959 NE Pacific Street
UW Mailbox 356426
Seattle, WA 98195-6426


CURRENT RESEARCH INTERESTS

Our laboratory uses a wide variety of mass spectrometric and proteomic approaches to investigate the role of oxidative pathways in the regulation of matrix metalloproteinases (MMPs) and tissue inhibitor of metalloproteinases (TIMPs). We also are interested in exploring protein expression by activated neutrophils and macrophages, two key cellular components of the innate immune system. Our long-term goal is to explore the role of activated phagocytes and MMPs in the pathogenesis of inflammatory diseases.

REPRESENTATIVE PUBLICATIONS

Fu X, Kassim SY, Parks WC, Heinecke JW:  Hypochlorous acid oxigenates the cysteine switch domain of pro-matrilysin (MMP-7): A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase.  J Biol Chem 276:41279-41287, 2001.

Fu X, Kassim SY, Parks WC, Heinecke JW:  Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin):  An oxidative mechanism for restraining proteolytic activity during inflammation. J Biol Chem 278:28403-28409, 2003.

Fu X, Kao J, Bergt C, Kassim SY, Huq NP, d’Avignon A, Parks WC,  Mecham RP, Heinecke JW:  Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: Specific structural motifs control protein oxidation. J Biol Chem 279:6209-6212, 2004.

Kassim SY, Fu X, Liles WC, Shapiro SD, Parks WC, Heinecke JW:  NADPH oxidase restrains the matrix metalloproteinase activity of macrophages.  J Biol Chem 280: 30201-30205, 2005.

Fu X, Wang Y, Kao J, Irwin A,d’Avignon A, Mecham RP, Parks WC, Heinecke JW: Specific sequence motifs direct the oxygenation and chlorination of tryptophan by myeloperoxidase.  Biochemistry 45:3961-3971, 2006.