Professor

Tel: 86-510-885197003

Email: xdgao@jiangnan.edu.cn

Web: http://klccb.jiangnan.edu.cn/info/1005/1017.htm 

2011 – Now  Jiangnan University,   CHINA.

2006 - 2011  Associate Professor (Ph.D   advisor). Hokkaido University, JAPAN.

2003 - 2006  Senior Research Scientist.   AIST JAPAN.

2002 - 2003  Assistant Professor. State   University of New York at Stony Brook, USA.

1998 - 2002  Research Scientist. State   University of New York at Stony Brook. USA.

1995 - 1998  Postdoctoral Fellow. AIST,   JAPAN.

1990 - 1994  Ph.D. The University of   Tokyo, JAPAN.

1988 - 1990  M.Sc. Yamanashi   University, JAPAN.

1984 - 1988  B.Sc Yamanashi   University, JAPAN.

Glycobiology

Glycosylation is an   essential modification that functions in a variety of biological roles   ranging from the stabilization of protein structure to the regulation of cell   surface properties. This biological process is highly conserved from yeast to   human.  The general interest of our research is to understand how and   why glycosylation is regulated and how carbohydrate modifications mediate   their biological roles in eukaryotic cell. Main research projects we are   currently working on are listed below:

(1)   Molecular biological study   on the synthesis pathway of the dolichyl-linked oligosaccharide (DLO) in   endoplasmic reticulum (ER).

Our   studies not only can provide a major interest on understanding the mechanism   of this important glycosylation in cell but also contribute to unravel new   subtype of inherited human disease, congenital disorders of glycosylation   (CDG).

DLO biosynthetic pathway in ER

-- the first step of N-glycosylation –

(2)   In vitro Chemo-enzymatic   synthesis of various human N-glycans.

Our   study will offer different types of N-glycans, providing useful   substrates and tools for scientific studies of glycosyltransferases,   glycoproteins or pharmaceutical and medical applications.

Various type of human N-glycans

(3)   Remodeling of cell strains   for producing pharmaceutical glycoproteins.

  Our studies are   aiming to construct glycol-engineered cell strains that can efficiently   produce proteins with various specialized human type of N-glycosylation   using for pharmaceutical treatment.

Corresponding   author:

1.       Jin ZC, Kitajima T,   Dong W, Huang YF, Ren WW, Guan F, Chiba Y, Gao X-D*. Fujita M*. (2018) Genetic disruption of multiple   α1,2-mannosidases generates mammalian cells producing recombinant proteins   with high-mannose-type N-glycans. J Biol Chem. 2018 Feb 23. pii:   jbc.M117.813030. doi: 10.1074/jbc.M117.813030.

2.       Kitajima T*. Xue W,   Liu YS, Wang CD, Liu SS, Fujita M, Gao X-D*. Construction of green fluorescence protein mutant to   monitor STT3B-dependent N-glycosylation. FEBS J. 2017 Dec 28. doi:   10.1111/febs.14375.

3.       Li S-T, Wang N, Xu X-X, Fujita M, Nakanishi   H, Kitajima T, Dean N^* and Gao X-D^*.  Alternative   routes for synthesis of N-linked glycans by the Alg2   mannosyltransferase. The FASEB J. 2017 Dec 22. pii: fj.201701267R.   doi: 10.1096/fj.

4.       Li S-T.,   Wang N., Xu S., Yin J, Nakanishi   H*. Dean N.   Gao X-D*. Quantitative   study of yeast Alg1 beta-1, 4 mannosyltransferase activity, a key enzyme involved   in protein N-glycosylation. BBA-general subjects, 2017   Jan; 1861(1 Pt A): 2934-2941. doi: 10.1016/j.bbagen.2016.09.023.

5.       Nakanishi H*. Li F. Han B. Arai S. Gao X-D*. Yeast cells as an assay system for in vivo O-GlcNAc   modification. BBA-general subjects, 2017 May;   1861(5 Pt A): 1159-1167. doi: 10.1016/j.bbagen.2017.03.002.

First author:

1.       Gao X-D. Moriyama S. Miura N.   Dean N. and Nishimura S-I. (2008) Interaction between the C-termini of Alg13   and Alg14 mediate formation of the active UDP-N-acetylglucosamine transferase   complex. J. Biol. Chem., 283: 32534-32541.

2.       Gao X-D. Tachikawa H. Sato T.   Jigami, Y. and Dean N. (2005) Alg14 recruits Alg13 to the cytoplasmic face of   the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine   transferase required for the second step of N-linked glycosylation. J.   Biol. Chem., 280: 36254 – 36262

3.       Gao X-D. Nishikawa A. and   Dean N. (2001). Identification of a conserved motif in the yeast GDP-mannose   transporter required for nucleotide sugar binding. J. Biol. Chem.,   276: 4424-4432.

4.       Gao X-D. and Dean N. (2000).   Distinct protein domains of the yeast Golgi GDP-mannose transporter mediate   oligomer assembly and export from the endoplasmic reticulum. J. Biol.   Chem., 275: 17718-17727.

5.       Gao X-D. Kaigorodov V. and   Jigami Y. (1999) YND1, a homologue of GDA1, encodes membrane-bound apyrase   required for Golgi N- and O-glycosylation in Saccharomyces cerevisiae. J.   Biol. Chem., 274: 21450 – 21456.