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J Biol Chem, Vol. 273, Issue 30, 18864-18870, July 24, 1998
Department of Medical Biochemistry, University of Göteborg,
Medicinaregatan 9, 413 90 Gothenburg, Sweden
The MUC2 mucin is the major gel-forming mucin in
the small and large intestine. Due to its sequence similarities with
the von Willebrand factor, it has been suggested to dimerize in the endoplasmic reticulum and polymerize in the trans-Golgi network. Using
an O-glycosylation-sensitive MUC2 antiserum, a dimerization has been shown to occur in the endoplasmic reticulum of LS 174T cells
(Asker, N., Axelsson, M. A. B., Olofsson, S.-O., and Hansson, G. C. (1998) J. Biol. Chem. 273, 18857-18863).
Using an antiserum immunoprecipitating O-glycosylated MUC2
mucin, monomers and dimers were shown to occur in soluble form in the
lysate of LS 174T cells. The amount of O-glycosylated dimer
was small, and no larger species were found even after long chase
periods. However, most of the labeled MUC2 mucin was found in pelleted
debris of the cell lysate. This insoluble MUC2 mucin was recovered by
immunoprecipitation after reduction of disulfide bonds. Analysis by
agarose gel electrophoresis revealed two bands, of which the smaller
migrated as the O-glycosylated monomer and the larger
migrated as the O-glycosylated dimer of the cell lysis
supernatant. Mucins insoluble in 6 M guanidinium chloride
could also be obtained from LS 174T cells. Such mucins have earlier
been found in the small intestine (Carlstedt, I., Herrmann, A.,
Karlsson, H., Sheehan, J., Fransson, L.-Å., and Hansson, G. C. (1993) J. Biol. Chem. 268, 18771-18781). Reduction of
the mucins followed by purification by isopycnic density gradient ultracentrifugation and analysis by agarose gel electrophoresis revealed two bands reacting with an anti-MUC2 tandem repeat antibody after deglycosylation. These bands migrated identically to the bands
shown by metabolic labeling, and they could also be separated by rate
zonal ultracentrifugation. These results suggest that the MUC2 mucin is
forming nonreducible intermolecular bonds early in biosynthesis, but
after initial O-glycosylation.
O-Glycosylated MUC2 Monomer and Dimer from LS 174T
Cells Are Water-soluble, whereas Larger MUC2 Species Formed Early
during Biosynthesis Are Insoluble and Contain Nonreducible
Intermolecular Bonds
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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