Xuemin Xu, Ph.D., Professor

Mailing Address: Department of Pathobiology College of Veterinary Medicine The University of Tennessee 2407 River Drive Knoxville, TN 37996 Tel: (865) 974-8206 FAX: (865) 974-5616 Email: Web Sites: Cell Biology Laboratory Select One Cell Biology Laboratory Education Teaching Research Interests Professional Services Professional Societies Selected Publications RESEARCH PATHOLOGY

 

Education

• 1982 -- Department of Chemistry, Jilin University, Changchun (P.R. China) B.S. (Chemistry) awarded 3/82
• 1985 -- Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 227 (Japan) M.S. (Biochemistry) awarded 3/85
• 1989 -- Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama 227 (Japan) Ph.D. (Molecular Biology) awarded 3/89
• 1989 -- Graduate Fellow, Mitsubishi Kasei Corporation Research Center, Midori-ku Yokohama, 227 (Japan) 
  Graduate Fellow
• FELLOWSHIP: The Association for Overseas Technical Scholarship (AOTS) (4 April 1988 -- 31 March 1989) 

Teaching

• The graduate level core CEM course "Mechanisms of Disease"
• 2000-present Adviser of PhD student: Essam Laag, 
• 2002-present Adviser of PhD student: Guojun Zhao

Research Interests

• The molecular and cellular mechanism of Alzheimer’s disease and related neurodegeneration. 
• The mechanism of apoptotic cell death found in Neurodegenerative Disease, specifically, Alzheimer’s disease.
• Protein-protein interaction and its role in intracellular signal transduction. 
• I am currently conducting two research projects studying the pathological roles of 
  1. presenilins
  2. apolipoprotein E in Alzheimer’s disease

  The goal of my research is to determine the normal functions of these genes in neuron development including differentiation and survival, and the pathological role of these genes in Alzheimer’s disease using molecular and cellular approaches.

Professional Services

• Captive and free living wildlife medicine

Professional Societies

• American Association for the Advancement of Science
• Society for Neuroscience

Selected Publications

1. Guojun Zhao, Mei-Zhen Cui, Guozhang Mao, Jianxin Tan, Yunzhou Dong, Longsheng Sun, and Xuemin Xu (2005)
   γ-cleavage is dependent on ζ-cleavage during the proteolytic processing of amyloid precursor protein within its transmembrane domain. J. Biol. Chem., 2005. 280(45): p. 37689-37697.

2. Yunzhou Dong, Jianxin Tan, Mei-Zhen Cui, Guojun Zhao, Guozhang Mao, Neena Singh, and Xuemin Xu (2005)
   Calpain inhibitor MDL28170 modulates Aβ formation by inhibiting the formation of intermediate Aβ46 and protecting Aβ from degradation. The FASEB Journal, in press.

3. Guojun Zhao, Guozhang Mao, Jianxin Tan, Yunzhou Dong, Mei-Zhen Cui, Seong-Hun Kim, and Xuemin Xu.
   Identification of a New Presenilin-dependent ζ-Cleavage Site within the Transmembrane Domain of Amyloid Precursor Protein. J. Biol. Chem. 2004 279: 50647-50650. (Paper of the Week) (UTCVM Press Release)
   (American Society for Biochemistry and Molecular Biology Press Release)

4. Tan, M., Xu, X., Ohba, M. and Cui, M.-Z., (2004) Protein kinase C delta mediates Angiotensin II-induced protein kinase D phosphorylation in aortic smooth muscle cells. Artherioscler, Thromb Vasc Biol 24(12): 2271-2277.

5. Xuemin Xu, Wei Go, Goujun Zhao, Yong-chang Shi, and. Mei-Zhen Cui (2004). Presenilin-1-associated protein (PSAP) induced apoptosis involves FoF1-ATPase activity. Submitted. 

6. Cui, M.-Z. , Zhao, G., Winokur, A., Laag, E. Bydash J. R., Penn, M. S., Chisolm G. M., and Xu, X., (2003)
   Lysophosphatidic Acid Induction of Tissue Factor Expression in Aortic Smooth Muscle Cells. Artherioscler, Thromb Vasc Biol 23: 224-230. 

7. Tan, M., Xu, X., Ohba, M., Ogawa W. and Cui, M.-Z. (2002), Thrombin rapidly induces protein kinase D phosphorylation and protein kinase C delta mediates the activation J. Biol. Chem 278:  2824-2828. 

8. Yaping Gu, Susamma Verghese, Ravi Mishra, Xeumin Xu, Yongchang Shi, and Neena Singh. (2002). Mutant prion protein (PrP) mediated aggregation of normal PrP in the endoplasmic reticulum: Implications for prion propagation and neurotoxicity. J of Neurochemistry 83: 1-13. 

9. Xuemin Xu, Yong-chang Shi, Wei Gao, Guozhang Mao, Guojun Zhao, Sudesh Agrawal, Guy Chisolm, and Mei-Zhen Cui. (2002). The novel presenilin-1-associated protein (PSAP) is a pro-apoptotic mitochondrial protein. J Biol Chem 277:48913-48922. 

10. Xu, X., Y. Shi, X. Wu, P. Gambetti, D. Sui, and M. Z. Cui. (1999). Identification of a Novel PSD-95/Dlg/ZO-1 (PDZ)-like Protein Interacting with the C Terminus of Presenilin-1. J Biol Chem 274:32543-32546.

11. Smine, A., Xu, X., Nishiyama, K., Katada, T., Gambetti, P., Yadav, S. P., Wu, X., Shi, Y. C., Yasuhara, S., Homburger, V., and Okamoto, T. Regulation of brain G-protein go by Alzheimer's disease gene presenilin- 1 (1998) J Biol Chem 273(26), 16281-16288

12. Xu, X., Wang, Y., Barry, D.C., Chanock, S.J., and Bokoch, G.M. (1997) Guanine nucleotide binding properties of Rac2 mutant proteins and analysis of responsiveness to guanine nucleotide dissociation stimulator. Biochemistry, 36: 626-632.

13. Chuang, T.-H*., Xu, X*., Kaartinen, V., Heisterkamp, N., Groffen, J., and Bokoch, G.M. (1995) Abr and Bcr are multifunctional Regulators of the Rho GTP-binding Protein Family. Proc Natl Acad Sci USA. 92: 10282-10286.

14. Chuang, T.-H., Xu, X., Quilliam, L.A., and Bokoch, G.M. (1994) SmgGDS Stabilizes Nucleotide-Bound and -Free Forms of the Rac1 GTP-binding Protein and Stimulates GTP/GDP Exchange Through a Substituted Enzyme Mechanism. Biochem. J.  303: 761-767.

15. Xu, X., Barry, D.C., Settleman, J., Schwartz, M.A and Bokoch, G.M. (1994) Differing Structural Requirements for GTPase-activating Protein Responsiveness and NADPH Oxidase Activation by Rac. J. Biol. Chem. 269: 23569-23574.

16. Heyworth, P.G., Knaus, U.G., Xu, X., Uhlinger, D.J., Conroy, L., Bokoch, G.M., and Curnutte, J.T. (1993) Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophile NADPH oxidase. MBC 4:261-269.

17. Chuang, T.-H., Xu, X., Knaus, U.G., Hart, M., and Bokoch, G.M. (1993) GDP dissociation inhibitor (GDI) prevents intrinsic and GAP-stimulated GTP hydrolysis by the Rac1 and Rac2 GTP-binding proteins. J. Biol. Chem. 268:775-778.

18. Xu, X., and Yagi, T. (1993) DNA sequencing of the seven remaining structural genes of the gene duster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry 32:968-981.

19. Yagi, T., and Xu, X. (1992) The energy-transducing NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Biochimica et Biopysica Acta. 1101:181-183.

20. Xu, X., and Yagi, T. (1992) Gene cluster of energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: Characterization of four structural gene products. Biochemistry 31:6925-6932.

21. Yagi, T., Xu, X., and Matsuno-Yagi, A. (1991) Gene cluster of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Biol. Chem. Hoppe Seyler 372:555-555. Xu, X., and Yagi, T. (1992) Structural features of the 66 kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Arch. Biochem. Biophys. 296:40-48.

22. Xu, X., and Yagi, T. (1991) Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: Sequence similarity to 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I. Biochemistry 30:8678-8684.

23. Xu, X., and Yagi, T. (1991) The NADH-binding subunit of energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: Gene cloning and deduced primary structure. Biochemistry, 30:6422-6428.

24. Xu, X., and Yagi, T. (1991) Identification of the NADH-binding subunit of energy-transducing NADH-quinone oxidoreductase (NADH-1) of Thermus Thermophilus HB-8. Biochem. Biophys. Res. Commun. 174:667-672.

25. Xu, X., Koyama, N., Cui, M., Yamagishi, A., Nosoh, Y., and Oshima, T. (1991) Molecular cloning and nucleotide sequence of NADH dehydrogenase gene from alkalophilic Bacillus. J. Biochem. 109:678-683.

26. Xu, X., Koyama, N., Sekiguchi, T., Nosho, Y., Kanaya, S., Ohashi, S., and Tsuda, K. (1989) Tryptic digestion of NADH dehydrogenase from alkalophilic Bacillus. J. Biochem. 105:626-632.

27. Xu, X., Koyama, N., Sekiguchi, T., Nosho, Y., Kanaya, S., Ohashi, S., and Tsuda, K. (1986) In: Contemporary Themes in Biochemistry (Kon, O.L., ed) pp. 52-53, Cambridge University Press, Cambridge.

28. Xu, X., Hisae, K., Koyama,N., and Nosoh, Y. (1985) Loss of liposome binding of NADH dehydrogenase from alkalophilic Bacillus on subtilisin digestion. FEBS Lett. 181:313-317.

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