Biosynthesis of mucin derived from a 60-kDa precursor protein in the human stomach
| Autor: | Amalia Slomiany, Bronislaw L. Slomiany, Yasutake Yamamoto, Shuichi Sano, Kazuichi Okazaki |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Protein subunit
Cyclopentanes Biology chemistry.chemical_compound Biosynthesis Culture Techniques Extracellular Humans Secretion Monensin Protein Precursors Protein Synthesis Inhibitors Brefeldin A Gastric Mucins Tunicamycin Mucin Gastroenterology Antibodies Monoclonal Precipitin Tests Molecular biology Molecular Weight Biochemistry chemistry Gastric Mucosa Intracellular |
| Zdroj: | Journal of Gastroenterology. 29:685-694 |
| ISSN: | 1435-5922 0944-1174 |
| DOI: | 10.1007/bf02349272 |
| Popis: | We studied the biosynthesis of mucin in the human stomach using an anti-mucin core peptide monoclonal antibody, 3G12. Human stomach mucosa was labeled with [35S]methionine, and chased for 3 h. An approximately 60-kDa subunit of human gastric mucin precursor protein was detected in the intracellular product. Under nonreducing conditions, dimer, trimer, and tetramer mucin precursor protein (120, 180, 240 kDa) were detected. Treatment with tunicamycin or endo-beta-N-acetylglucosaminidase H had no effect on the 60-kDa subunit and its oligomers. Extracellular products contained only the high molecular weight mucin, and the secretion was not affected by tunicamycin. By treatment with monensin or brefeldin A, the mature mucin was not secreted extracellularly. These findings suggested that a 60-kDa subunit of the mucin precursor protein was biosynthesized into mature mucin after oligomerization to tetramers, and that neither the oligomerization nor the intracellular transport of the mucin in the human stomach was associated with N-glycosylation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink