Wei Deng, M.D., Ph.D.
199 Ren'ai Rd. Suzhou, Jiangsu 215123, P.R.China
Cyrus Tang Hematology Center, Soochow University
Phone: 86-512-65880877-3601
Fax: 86-512-65880929
Email:dengwei0328@suda.edu.cn
Education:
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Lanzhou University, Lanzhou, Gansu
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BS
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09/1997
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07/2001
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Chemistry
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Peking University, Beijing, Beijing
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PhD
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09/2002
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07/2008
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Physical chemistry
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University of Houston, Houston, Texas
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Postdoctoral Fellow
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11/2008
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07/2009
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Chemistry
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University of Texas Health & Science Center at Houston, Houston, Texas
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Postdoctoral Fellow
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07/2009
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07/2011
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Biochemistry
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Emory University, Atlanta, Georgia
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Postdoctoral Fellow
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07/2011
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07/2015
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Biochemistry
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Research:
1. Membrane receptor of platelets are important for a variety of essential functions of platelets. Study these membrane proteins will allow us to understand and further manipulate the regulation of platelet activation. Our lab carries multidisciplinary researches on the structure and interaction of several important platelet membrane receptors including GPIb, GPVI, ADAM17/10, thrombin receptors and ADP receptors. We are seeking to explore the mechanism underling these receptor-related signaling transductions and develop novel therapeutic strategy for those related diseases.
2. The relationship between blood component, endothelial cells and shear flow is important in understanding many diseases related to blood. In blood circulation, many signaling events are closely regulated by the interactions of circulating proteins and membrane receptors on vascular surface, in which shear stress induced by blood flow plays somehow critical role. Von Willebrand disease is the most common bleeding disorder around the world. The related protein, called Von Willebrand Factor (VWF), is a large multimeric glycoprotein in circulation. VWF critically mediates hemostasis, thrombosis and thrombo-inflammation by sensing and responding to shear flow. We are seeking to investigate the structure and function of VWF so that we can find a proper diagnosis and treatment to a large majority of VWD patients. Our study, inspired by the idea that VWF has its A1 domain protected under low shear stress and exposed to interaction at high shear stress condition, mainly focuses on understanding the mechanism of this autoinhibitory regulation, which in turn, will enable us to create new tools to diagnose various VWD.
Representative Publications:
1. Deng W, Xu Y, Chen W, Paul DS, Syed AK, Dragovich MA, Liang X, Zakas P, Berndt MC, Di Paola J, Ware J, Lanza F, Doering CB, Bergmeier W, Zhang XF, Li R. Platelet clearance via shear-induced unfolding of a membrane mechanoreceptor. Nat Communs. 2016; 7:12863. PubMed PMID: 27670775; PubMed Central PMCID: PMC5052631.
2. Deng W, Cho S, Su PC, Berger BW, Li R. Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10. Proc Natl Acad Sci U S A. 2014; 111(45):15987-92. PubMed PMID: 25349418; PubMed Central PMCID: PMC4234582.
3. Zhang W, Deng W, Zhou L, Xu Y, Yang W, Liang X, Wang Y, Kulman JD, Zhang XF, Li R. Identification of a juxtamembrane mechanosensitive domain in the platelet mechanosensor glycoprotein Ib-IX complex. Blood. 2015; 125(3):562-9. PubMed PMID: 25359992; PubMed Central PMCID: PMC4296016.
4. Deng W, Wang Y, Druzak SA, Healey JF, Syed AK, Lollar P, Li R. A discontinuous autoinhibitory module masks the A1 domain of von Willebrand factor. J Thromb Haemost. 2017; 15(9):1867-1877. PMID: 28692141; PMCID: PMC5585049.
5. Batsuli G, Deng W, Healey JF, Parker ET, Baldwin WH, Cox C, Nguyen B, Kahle J, Königs C, Li R, Lollar P, Meeks SL. High-affinity, noninhibitory pathogenic C1 domain antibodies are present in patients with hemophilia A and inhibitors. Blood. 2016; 128(16):2055-2067. PMID: 27381905; PubMed Central PMCID: PMC5073184.