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J Biol Chem, Vol. 273, Issue 46, 30472-30481, November 13, 1998
-D-Galactosamine:Polypeptide
N-Acetylgalactosaminyltransferase That Complements Other
GalNAc-Transferases in Complete O-Glycosylation of the
MUC1 Tandem Repeat
,,,
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From the A fourth human UDP-GalNAc:polypeptide
N-acetylgalactosaminyltransferase, designated GalNAc-T4,
was cloned and expressed. The genomic organization of GalNAc-T4 is
distinct from GalNAc-T1, -T2, and -T3, which contain multiple coding
exons, in that the coding region is contained in a single exon.
GalNAc-T4 was placed at human chromosome 12q21.3-q22 by in
situ hybridization and linkage analysis. GalNAc-T4 expressed in
Sf9 cells or in a stably transfected Chinese hamster ovary cell
line exhibited a unique acceptor substrate specificity. GalNAc-T4
transferred GalNAc to two sites in the MUC1 tandem repeat sequence (Ser
in GVTSA and Thr in PDTR) using a 24-mer glycopeptide with GalNAc
residues attached at sites utilized by GalNAc-T1, -T2, and -T3
(TAPPAHGVTSAPDTRPAPGSTAPPA, GalNAc attachment sites underlined). Furthermore, GalNAc-T4 showed the best
kinetic properties with an O-glycosylation site in the
P-selectin glycoprotein ligand-1 molecule. Northern analysis of human
organs revealed a wide expression pattern. Immunohistology with a
monoclonal antibody showed the expected Golgi-like localization in
salivary glands. A single base polymorphism, G1516A (Val to Ile), was
identified (allele frequency 34%). The function of GalNAc-T4
complements other GalNAc-transferases in O-glycosylation of
MUC1 showing that glycosylation of MUC1 is a highly ordered process and
changes in the repertoire or topology of GalNAc-transferases will
result in altered pattern of O-glycan attachments.
Faculty of Health Sciences, School of
Dentistry, Copenhagen, Denmark, the § Department of
Molecular Biology, University of Odense, Denmark, the ¶ Imperial
Cancer Research Fund, London WC2A 3PX, United Kingdom, the
Eppley Institute for Research in Cancer and Allied Diseases,
University of Nebraska Medical Center, Omaha, Nebraska 68198, the
** University Hospital Nijmegen, Department of Human Genetics 6500HB
Nijmegen, The Netherlands, the Faculty of
Health Sciences, Genetics Institute, University of Copenhagen, 2200 N
Copenhagen, Denmark, and the §§ Regional Center
for Blood Transfusion, Aalborg Hospital, Aalborg, Denmark
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R. Steffensen, K. Carlier, J. Wiels, S. B. Levery, M. Stroud, B. Cedergren, B. Nilsson Sojka, E. P. Bennett, C. Jersild, and H. Clausen Cloning and Expression of the Histo-blood Group Pk UDP-galactose:Galbeta 1-4Glcbeta 1-Cer alpha 1,4-Galactosyltransferase. MOLECULAR GENETIC BASIS OF THE p PHENOTYPE J. Biol. Chem., May 26, 2000; 275(22): 16723 - 16729. [Abstract] [Full Text] [PDF]
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H. Hassan, C. A. Reis, E. P. Bennett, E. Mirgorodskaya, P. Roepstorff, M. A. Hollingsworth, J. Burchell, J. Taylor-Papadimitriou, and H. Clausen The Lectin Domain of UDP-N-acetyl-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T4 Directs Its Glycopeptide Specificities J. Biol. Chem., December 1, 2000; 275(49): 38197 - 38205. [Abstract] [Full Text] [PDF]
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