Abstract：
BACKGROUND/AIMS:Human colonic epithelium produces large amounts of mucin. The aim of this study was to examine mucin biosynthesis in the human colon. METHODS:Human colonic mucin was isolated using CsCl density gradients, and polyclonal antiserum was raised. Biosynthesis of colonic mucins was studied by labeling colonic explants with 35S-labeled amino acids or [35S]sulfate and subsequent immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). RESULTS:The polyclonal antiserum specifically recognized colonic mucin, primarily reacting with peptide epitopes. Biosynthetic pulse/chase experiments showed a 35S-amino acid-labeled mucin precursor of about 600 kilodaltons, which was converted into a mature, glycosylated, and sulfated mucin and subsequently secreted into the medium. This mature mucin comigrated with isolated colonic mucin with an apparent molecular weight of 550 kilodaltons on SDS-PAGE, whereas gel filtration indicated that the molecular weight is actually much larger. Independent immunoprecipitation with an anti-Muc2 antiserum showed cross-reactivity with the 600-kilodalton precursor. CONCLUSIONS:These results show the biosynthesis of a secretory colonic mucin for the first time. This mucin is synthesized as a precursor protein of approximately 600 kilodaltons, which, after glycosylation, is secreted as a glycoprotein with an apparent molecular weight of 550 kilodaltons on SDS-PAGE. It is very likely that this mucin is Muc2.
journal_name
Gastroenterologyjournal_title
Gastroenterologyauthors
Tytgat KM,Büller HA,Opdam FJ,Kim YS,Einerhand AW,Dekker Jdoi
10.1016/0016-5085(94)90537-1subject
Has Abstractpub_date
1994-11-01 00:00:00pages
1352-63issue
5eissn
0016-5085issn
1528-0012pii
S0016508594003318journal_volume
107pub_type
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