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XING Shu
 Shu XING ,Ph.D.

Associate Professors, Shool of Life Sciences, Jilin University

email: xingshu@jlu.edu.cn

Tel:+86-0431-85155321

Fax:+86-0431-85155152

Life Science Building, Jilin University, Qianjin Street No.2699,Changchun,P. R. China,

Postal Code:130012
Scientific research field description
Tyrosine phosphorylation is a fundamental regulatory mechanism for numerous important aspects of human cellular physiology in health and disease. This process is controlled by coordinate action of protein tyrosine kinases (PTKs) and phosphatases (PTPs). Both families of the enzymes have highly diverse structures and functions. Their activities are tightly regulated under normal conditions, and deregulation of the enzymes produces human diseases including various cancers. One major research area in my lab is focused on myeloproliferative neoplasms (MPNs). We have identified an acquired mutation of tyrosine kinase JAK2 designated JAK2V617F in the majority of these patients. The mutation causes constitutive activation of JAK2 tyrosine kinase activity and downstream signaling components. We have further generated JAK2V617F transgenic mice which display MPN phenotypes. We thus obtain a unique mouse model to study the pathogenesis of MPNs and to develop therapeutic drugs to treat the diseases. Another major research area is to identify mutation of tyrosine kinases and phosphatases in all types of cancers. We will further characterize the biochemical properties and pathological functions of these mutant enzymes. Eventually, we will to find chemical inhibitors to target the enzymes for therapeutic purpose.
Representative papers
 

1.  Han H, Lu L, Wang Q, Zhu M, Yuan C, Xing S*, Fu X. Synthesis and evaluation of xovanadium (iv) complexes of Schiff-base condensates from 5-substituted-2-hydroxy benzaldehyde and 2-substituted-benzenamine as selective inhibitors of protein tyrosine phosphatase 1B. Dalton Trans. 2012 Aug 6; 41: 11116-24

2.  Lu L, Gao X, Zhu M, Wang S, Wu Q, Xing S*, Fu X, Liu Z, Guo M. Exploration of biguanido-oxovanadium complexes as potent and selective inhibitors of protein tyrosine phosphatases. Biometals. 2012 Jun; 25(3): 599-610. 

3.  Wang Q, Zhu M, Zhu R, Lu L, Yuan C, Xing S, Fu X, Mei Y, Hang Q. Exploration of α-aminophosphonate N-derivatives as novel, potent and selective inhibitors of protein tyrosine phosphatases. Eur J Med Chem. 2012 Mar; 49: 354-64.

4.  Yuan C, Zhu M, Wang Q, Lu L, Xing S, Fu X, Jiang Z, Zhang S, Li Z, Li Z, Zhu R, Ma L, Xu L. Potent and selective inhibition of T-cell protein tyrosine phosphatase (TCPTP) by a dinuclear copper(ii) complex. Chem Commun (Camb). 2012 Jan 4; 48(8):1153-5.

5.  Wang Q, Zhu M, Lu L, Yuan C, Xing S, Fu X. Potent inhibition of protein tyrosine phosphatases by quinquedentate binuclear copper complexes: synthesis, characterization and biological activities. Dalton Trans. 2011 Dec 28; 40(48): 12926-34.

6.  Li Y, Lu L, Zhu M, Wang Q, Yuan C, Xing S, Fu X, Mei Y. Potent inhibition of protein tyrosine phosphatases by copper complexes with multi-benzimidazole derivatives. Biometals. 2011 Dec; 24(6): 993-1004.

7.  Ma L, Lu L, Zhu M, Wang Q, Gao F, Yuan C, Wu Y, Xing S, Fu X, Mei Y, Gao X. Dinuclear copper complexes of organic claw: potent inhibition of protein tyrosine phosphatases. J Inorg Biochem. 2011 Sep; 105(9):1138-47.

8.  Ma L, Lu L, Zhu M, Wang Q, Li Y, Xing S, Fu X, Gao Z, Dong Y. Mononuclear copper(II) complexes with 3,5-substituted-4-salicylidene-amino-3,5-dimethyl-1,2,4-triazole: synthesis, structure and potent inhibition of protein tyrosine phosphatases. Dalton Trans. 2011 Jun 28; 40(24):6532-40. 

9.  Ma J, Li Z, Xing S, Ho WT, Fu X, Zhao ZJ. Tea contains potent inhibitors of tyrosine phosphatase PTP1B. Biochem Biophys Res Commun. 2011 Apr 1; 407(1): 98-102.

10.  Zhao W, Gao R, Lee J, Xing S, Ho WT, Fu X, Li S, Zhao ZJ. Relevance of JAK2V617F positivity to hematological diseases--survey of samples from a clinical genetics laboratory. J Hematol Oncol. 2011 Jan 14; 4: 4.

11.  Yuan C, Lu L, Wu Y, Liu Z, Guo M, Xing S, Fu X, Zhu M. Synthesis, characterization, and protein tyrosine phosphatases inhibition activities of oxovanadium(IV) complexes with Schiff base and polypyridyl derivatives. J Inorg Biochem. 2010 Sep; 104(9): 978-86.

12.  Lu L, Wang S, Zhu M, Liu Z, Guo M, Xing S, Fu X. Inhibition protein tyrosine phosphatases by an oxovanadium glutamate complex, Na(2)[VO(Glu) (2)(CH (3)OH)](Glu = glutamate). Biometals. 2010 Dec; 23(6):1139-47.

13.  Zhang X, Xing S, Wu X, Lin F, Fu X, Li W. Purification and characterization of protein tyrosine phosphatase MEG1 and preparation of anti-PTPMEG1 antibody. Chem Res Chinese U. 2010, 26(4): 591-95

14.  Xing S, Ho WT, Zhao W, Ma J, Wang S, Xu X, Li Q, Fu X, Xu M, Zhao ZJ. Transgenic expression of JAK2V617F causes myeloproliferative disorders in mice. Blood. 2008 May 15; 111(10): 5109-17.

15.  Zhao R, Xing S, Li Z, Fu X, Li Q, Krantz SB, Zhao ZJ. Identification of an acquired JAK2 mutation in polycythemia vera. J Biol Chem. 2005 Jun 17; 280(24): 22788-92.

16.  Wanming Zhao, Shu Xing, Rufei Gao, Aref Al-Kali, Wanting Tina Ho and Zhizhuang Joe Zhao. Generation and Characterization of Transgenic Mice Expressing MplW515L. Poster Session. The 51st ASH annual meeting, 2009, New Orleans, LA, USA.

17.  Shu Xing, Wanming Zhao, Wanting Tina Ho and Zhizhuang Joe Zhao. Transgenic Expression of Wild Type JAK2 Suppresses Myeloproliferative Disorder Phenotypes Induced by Mutant JAK2V617F in Mice. Oral Session. The 50th ASH annual meeting, 2008, San Francisco, CA, USA.

18.  Shu Xing and Zhizhuang Joe Zhao. Transgenic Expression of JAK2V617F Causes Myeloproliferative Disorders in Mice. Poster Session. The 49th ASH annual meeting, 2007, Atlanta, GA, USA.

 

College of Life Sciences, Jilin University,Changchun,China,130012

Tel:+86-431-81969061  Email: smxyld@jlu.edu.cn