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(Received for publication, July 8, 1997, and in revised form, August 18, 1997)
,
,
,
From the The large glycosylated domains obtained from the
rat intestinal mucin Muc2 were isolated from the large and small
intestine of the inbred rat strains GOT-W and GOT-BW. The expression of the rat Muc2 in the large intestine was confirmed
immunochemically and by Northern blotting. Released oligosaccharides
were structurally characterized by gas chromatography-mass spectrometry
(neutral and sialylated species) or by tandem mass spectrometry
(sulfated species), and a total of 63 structures was assigned. The
large intestinal oligosaccharides were found to be identical between the strains, while the small intestinal glycosylation differed. Until
now, detailed structural analysis of oligosaccharides isolated from a
single mucin core or mucin domain with different origin have not been
performed, and the information of different mucin glycoforms has been
limited to immunochemistry. Blood group A-determinants (GalNAc
Department of Medical Biochemistry,
Göteborg University, Medicinaregatan 9A, 413 90 Gothenburg,
Sweden and the ¶ Department of Cell and Molecular Biology, Section
for Molecular Pathogenesis, Lund University, P. O. Box 94, 221 00 Lund, Sweden
1-3(Fuc
1-2)Gal
1-, and structures related to the blood group Sda/Cad-related epitope
NeuAc/NeuGc
1-3(GalNAc
1-4)Gal
1-, were found in GOT-BW small
intestine, and also in both large intestines. Blood group
H-determinants and NeuAc/NeuGc
1-3Gal
1- were found in all
samples. Core 1 (Gal
1-3GalNAc
1-), core 2 (Gal
1-3(GlcNAc
1-6)GalNAc
1-), core 3 (GlcNAc
1-3GalNAc
1-), and core 4 (GlcNAc
1-3(GlcNAc
1-6)GalNAc
1- were also found in all the
samples. The large intestine were enriched in sulfated oligosaccharides
and the small intestine contained higher amounts of sialylated species.
Sulfation were found exclusively on C-6 of GlcNAc.
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