Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization.

Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization. Abstract Text:

S L Bell,I A Khatri,G Xu,J F Forstner,

We have investigated the possibility that the intestinal mucin rat Muc2 forms dimers during biosynthesis via intermolecular disulphide bridging of its C-terminal domains. Since the cysteine alignment of RMuc2 (and other secretory mucins) is similar to that of human von Willebrand factor, a similar C-tail to C-tail dimerization may occur in mucins. The C-terminal domain of RMuc2 (534 amino acids) was expressed in COS-1 cells, and the products monitored by SDS/PAGE and western blotting with three antibodies to different regions of the C-terminal domain. In cells, the expressed domain was glycosylated and formed disulphide-dependent dimers centred at approximately 150 kDa. The domain dimer, but not its precursor monomer, was secreted into the culture medium. The dimers in the media however, appeared to be 12-15-kDa heavier (i.e. had a slower mobility) than in cell lysates. Initial N-glycosylation, dimerization and secretion were inhibited by addition of tunicamycin to incubations, whereas benzyl-alpha-GalNAc did not interfere with these processes. However benzyl-alpha-GalNAc resulted in a decrease in the apparent size of secreted dimers, such that they now had the same mobility on gels as dimers normally seen in cell lysates (i.e. 150 kDa). A similar change in dimer size was observed after incubating untreated media samples with N-acetylneuraminidase. This suggests that benzyl-alpha-GalNAc caused inhibition of sialylation of cell dimers just before they were secreted. In summary, the C-terminal domain of RMuc2 can form disulphide-dependent dimers, and N-glycosylation is required for dimerization and subsequent secretion. A late sialylation event appears to precede the secretion of mucin domain dimers.

Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization. Publishing Authors By Initials

SL Bell,IA Khatri,G Xu,JF Forstner,

For similar investigative techniques: genetic techniques: gene transfer techniques: transfection research abstracts see: investigative techniques: genetic techniques: gene transfer techniques: transfection research

PUBMED ID PMID:

MEDLINE DATE:

Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization. Journal Published:

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

Journal: European journal of biochemistry / FEBS

VOLUME: 253

Page Numbers: 123-31

Journal Abbreviation: Eur. J. Biochem.

ISSN: 0014-2956

DAY: 1

MONTH: Apr

YEAR: 1998

Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 107600

Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization. Keywords Mesh Terms:

KEYWORDS: Transfection

MESH TERMS: genetics

Chemical & Substance for Abstract: Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization. Information

Substance Name: Neuraminidase

Registry Number: EC 3.2.1.18

Grant and Affiliation Information for Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization.

AFFILIATION: Research Institute, The Hospital for Sick Children, Department of Biochemistry, University of Toronto, Ontario, Canada.

Country: GERMANY

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: Eur J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization Related Publications

• C-terminal domain of rodent intestinal mucin Muc3 is proteolytically cleaved in the endoplasmic reticulum to generate extracellular and membrane components.
• Characteristics of rodent intestinal mucin Muc3 and alterations in a mouse model of human cystic fibrosis.
• Detection of Salmonellae in Different Turtle Species within a Headwater Spring Ecosystem.
• Evidence for a second peptide cleavage in the C-terminal domain of rodent intestinal mucin Muc3.
• Evidence that a peptide corresponding to the rat Muc2 C-terminus undergoes disulphide-mediated dimerization.
• Interaction of heparin with synthetic peptides corresponding to the C-terminal domain of intestinal mucins.
• N-linked oligosaccharides play a role in disulphide-dependent dimerization of intestinal mucin Muc2.
• Radiological staging of ovarian cancer: imaging findings and contribution of CT and MRI.
• Regulated and unregulated pathways for MUC2 mucin secretion in human colonic LS180 adenocarcinoma cells are distinct.
• Role of the cystine-knot motif at the C-terminus of rat mucin protein Muc2 in dimer formation and secretion.
• SEA (sea-urchin sperm protein, enterokinase and agrin)-module cleavage, association of fragments and membrane targeting of rat intestinal mucin Muc3.
• Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage.
• Synthesis and secretion of mucin by the human colonic tumour cell line LS180.
• The carboxyl-terminal sequence of rat intestinal mucin RMuc3 contains a putative transmembrane region and two EGF-like motifs.
• The cationic C-terminus of rat Muc2 facilitates dimer formation post translationally and is subsequently removed by furin.
• [Studies on the serum protein changes and antibody formation in the rabbit following administration of antigens of the pig ascarid (Ascaris suum)]