Glycobiology, Vol 8, 731-740, Copyright © 1998 by Society for Glycobiology
IE VanderElst and A Datti
The distribution of the Golgi enzyme beta1, 6-N-
acetylglucosaminyltransferase (core 2 GlcNAc-T for short) has been
investigated in several tissue and cell systems by combining the potentials
of a polyclonal antibody and a novel, sensitive fluorescent enzyme assay.
In normal rat tissues, levels of the protein were found to vary and as a
general trend did not correlate with enzyme activities. Additionally, we
observed tissue-specific core 2 GlcNAc-T forms of various size: 75 kDa
(liver), 70 kDa (spleen), 60 kDA (heart), and 50 kDa (heart and lung).
These forms might arise from differential protein modifications;
alternatively, the smaller form may be a product of proteolytic cleavage,
given the presence of a catalytically inactive 50 kDa species in rat serum.
Chinese hamster ovary (CHO), MDAY-D2, PSA- 5E, and PYS-2 cell lines
consistently displayed a 70 kDa enzyme. When induced to retrodifferentiate
in the presence of butyrate + cholera toxin, CHO cells exhibited a 21-fold
increase in enzyme activity, while protein levels remained constant. A
similar trend was observed in the embryonal endoderm cell lines PSA-5E and
PYS-2, where an approximately 100-fold difference in core 2 GlcNAc-T
activity was found notwithstanding unchanged amounts of the protein and
identical mRNA levels, as evidenced by RT-PCR. In contrast, levels of core
2 GlcNAc-T activity in MDAY-D2 cells correlated well with protein
expression. Taken together, these observations demonstrate that core 2
GlcNAc-T expression may be subjected to multiple mechanisms of regulation
and suggest that in at least some instances (i.e., PSA-5E and PYS-2 cells)
expression may be regulated exclusively via posttranslational mechanism(s)
of control.
ORIGINAL ARTICLES
beta1,6 N-acetylglucosaminyltransferase (core 2 GlcNAc-T) expression in normal rat tissues and different cell lines: evidence for complex mechanisms of regulation
Department of Cell and Molecular Biology, Section of Biochemistry and Molecular Biology, University of Perugia, 06126 Perugia, Italy.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
S. Tan and P.-W. Cheng Mucin Biosynthesis: Identification of the cis-Regulatory Elements of Human C2GnT-M Gene Am. J. Respir. Cell Mol. Biol., June 1, 2007; 36(6): 737 - 745. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. M. Ben-Mahmud, G. E. Mann, A. Datti, A. Orlacchio, E. M. Kohner, and R. Chibber Tumor Necrosis Factor-{alpha} in Diabetic Plasma Increases the Activity of Core 2 GlcNAc-T and Adherence of Human Leukocytes to Retinal Endothelial Cells: Significance of Core 2 GlcNAc-T in Diabetic Retinopathy Diabetes, November 1, 2004; 53(11): 2968 - 2976. [Abstract] [Full Text] [PDF] |
||||
![]() |
T.-Y. Yen, B. A. Macher, S. Bryson, X. Chang, I. Tvaroska, R. Tse, S. Takeshita, A. M. Lew, and A. Datti Highly Conserved Cysteines of Mouse Core 2 {beta}1,6-N-Acetylglucosaminyltransferase I Form a Network of Disulfide Bonds and Include a Thiol That Affects Enzyme Activity J. Biol. Chem., November 14, 2003; 278(46): 45864 - 45881. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Chibber, B. M. Ben-Mahmud, G. E. Mann, J. J. Zhang, and E. M. Kohner Protein Kinase C {beta}2-Dependent Phosphorylation of Core 2 GlcNAc-T Promotes Leukocyte-Endothelial Cell Adhesion: A Mechanism Underlying Capillary Occlusion in Diabetic Retinopathy Diabetes, June 1, 2003; 52(6): 1519 - 1527. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. R. Falkenberg, K. Alvarez, C. Roman, and N. Fregien Multiple transcription initiation and alternative splicing in the 5' untranslated region of the core 2 {beta}1-6 N-acetylglucosaminyltransferase I gene Glycobiology, June 1, 2003; 13(6): 411 - 418. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Schwientek, J.-C. Yeh, S. B. Levery, B. Keck, G. Merkx, A. G. van Kessel, M. Fukuda, and H. Clausen Control of O-Glycan Branch Formation. MOLECULAR CLONING AND CHARACTERIZATION OF A NOVEL THYMUS-ASSOCIATED CORE 2 beta 1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE J. Biol. Chem., April 6, 2000; 275(15): 11106 - 11113. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. Schwientek, M. Nomoto, S. B. Levery, G. Merkx, A. G. van Kessel, E. P. Bennett, M. A. Hollingsworth, and H. Clausen Control of O-Glycan Branch Formation. MOLECULAR CLONING OF HUMAN cDNA ENCODING A NOVEL beta 1,6-N-ACETYLGLUCOSAMINYLTRANSFERASE FORMING CORE 2 AND CORE 4 J. Biol. Chem., February 19, 1999; 274(8): 4504 - 4512. [Abstract] [Full Text] [PDF] |
||||



