Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus.

Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. Abstract Text:

N Asker,M A Axelsson,S O Olofsson,G C Hansson,

Pulse-chase experiments in the colon cell line LS 174T combined with subcellular fractionation by sucrose density gradient centrifugation showed that the initial dimerization of the MUC2 apomucin started directly after translocation of the apomucin into the rough endoplasmic reticulum as detected by calnexin reactivity. As the mono- and dimers were chased, O-glycosylated MUC2 mono- and dimers were precipitated using an O-glycosylation-insensitive antiserum against the N-terminal domain of the MUC2 mucin. These O-glycosylated species were precipitated from the fractions that comigrated with the galactosyltransferase activity during the subcellular fractionation, indicating that not only MUC2 dimers but also a significant amount of monomers are transferred into the Golgi apparatus. Inhibition of N-glycosylation with tunicamycin treatment slowed down the rate of dimerization and introduced further oligomerization of the MUC2 apomucin in the endoplasmic reticulum. Results of two-dimensional gel electrophoresis demonstrated that these oligomers (putative tri- and tetramers) were stabilized by disulfide bonds. The non-N-glycosylated species of the MUC2 mucin were retained in the endoplasmic reticulum because no O-glycosylated species were precipitated after inhibition by tunicamycin. This suggests that N-glycans of MUC2 are necessary for the correct folding and dimerization of the MUC2 mucin.

Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. Publishing Authors By Initials

N Asker,MA Axelsson,SO Olofsson,GC Hansson,

For similar investigative techniques: centrifugation: ultracentrifugation research abstracts see: investigative techniques: centrifugation: ultracentrifugation research

PUBMED ID PMID:

MEDLINE DATE:

Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 273

Page Numbers: 18857-63

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 24

MONTH: Jul

YEAR: 1998

Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. Keywords Mesh Terms:

KEYWORDS: Ultracentrifugation

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. Information

Substance Name: Tunicamycin

Registry Number: 11089-65-9

Grant and Affiliation Information for Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus.

AFFILIATION: Department of Medical Biochemistry, University of Göteborg, Medicinaregatan 9A, S-413 90 Gothenburg, Sweden.

Country: UNITED STATES

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biol Chem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus Related Publications

• A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway.
• An autocatalytic cleavage in the C terminus of the human MUC2 mucin occurs at the low pH of the late secretory pathway.
• Chemical changes in rubber allergens during vulcanization.
• Comparing two microarray platforms for identifying mutated genes in barley (Hordeum vulgare L.).
• Deglycosylation by gaseous hydrogen fluoride of mucus glycoproteins immobilized on nylon membranes and in microtiter wells.
• Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus.
• Effect of salt and surfactant concentration on the structure of polyacrylate gel/surfactant complexes.
• Entamoeba histolytica cysteine proteases cleave the MUC2 mucin in its C-terminal domain and dissolve the protective colonic mucus gel.
• Experimental and clinical studies in aetiologic role of bile reflux in acute pancreatitis.
• Flies' lives on a crab.
• For the safety and benefit of current and future patients.
• Functional classification and central nervous projections of olfactory receptor neurons housed in antennal trichoid sensilla of female yellow fever mosquitoes, Aedes aegypti.
• Human MUC5AC mucin dimerizes in the rough endoplasmic reticulum, similarly to the MUC2 mucin.
• Identification of transient glycosylation alterations of sialylated mucin oligosaccharides during infection by the rat intestinal parasite Nippostrongylus brasiliensis.
• Innate immunity, macrophage activation, and atherosclerosis.
• Internal repeat variability in mucin sequences.
• Molecular characterization of the large heavily glycosylated domain glycopeptide from the rat small intestinal Muc2 mucin.
• No evidence of RALGDS mutations in cutaneous melanoma.
• 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.
• PBSC harvests individually optimized by using pre-collection CD34(+) values and on-line flow cytometric analysis of the mononuclear cell enrichment.
• Plasma membrane and vesicular monoamine transporters in normal endometrium and early pregnancy decidua.
• Purification and characterization of sialyl-Le(a)-carrying mucins of human bile; evidence for the presence of MUC1 and MUC3 apoproteins.
• Sensitivity after bilateral prophylactic mastectomy and immediate reconstruction.
• The N terminus of the MUC2 mucin forms trimers that are held together within a trypsin-resistant core fragment.
• The glycosylation of rat intestinal Muc2 mucin varies between rat strains and the small and large intestine. A study of O-linked oligosaccharides by a mass spectrometric approach.
• The human MUC2 mucin apoprotein appears to dimerize before O-glycosylation and shares epitopes with the 'insoluble' mucin of rat small intestine.
• The recombinant C-terminus of the human MUC2 mucin forms dimers in Chinese-hamster ovary cells and heterodimers with full-length MUC2 in LS 174T cells.
• The salivary mucin MG1 (MUC5B) carries a repertoire of unique oligosaccharides that is large and diverse.
• The transcripts of the apomucin genes MUC2, MUC4, and MUC5AC are large and appear as distinct bands.
• Uncomplicated duplex kidney and DMSA scintigraphy in children with urinary tract infection.