ArticleThe Biochemical journal2002
C-terminal domain of rodent intestinal mucin Muc3 is proteolytically cleaved in the endoplasmic reticulum to generate extracellular and membrane components.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 38 citations in OpenAlex.
- Interphotoreceptor matrix proteoglycans IMPG1 and IMPG2 proteolyze in the SEA domain and reveal localization mutual dependency.Scientific reports · 2022Article
- Intake of a Mixture of Sake Cake and Rice Malt Increases Mucin Levels and Changes in Intestinal Microbiota in Mice.Nutrients · 2020Article
- Core 2 Mucin-Type O-Glycan Is Related to EPEC and EHEC O157:H7 Adherence to Human Colon Carcinoma HT-29 Epithelial Cells.Digestive diseases and sciences · 2015Article
- Core 2 mucin-type O-glycan inhibits EPEC or EHEC O157:H7 invasion into HT-29 epithelial cells.Gut pathogens · 2015Article
- Muc17 protects intestinal epithelial cells from enteroinvasive E. coli infection by promoting epithelial barrier integrity.American journal of physiology. Gastrointestinal and liver physiology · 2011Article
- Article
- Contribution of the conservative cleavage motif to posttranslational processing of the carboxyl terminal domain of rodent Muc3.Molecular and cellular biochemistry · 2008Article
- Evidence for a second peptide cleavage in the C-terminal domain of rodent intestinal mucin Muc3.The Biochemical journal · 2004Article
- SEA (sea-urchin sperm protein, enterokinase and agrin)-module cleavage, association of fragments and membrane targeting of rat intestinal mucin Muc3.The Biochemical journal · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although human MUC3 and rodent Muc3 are both membrane-associated intestinal mucins, the present study has explored the possibility that rodent Muc3 might exist in soluble as well as membrane forms. No evidence was obtained for the existence of soluble splice variants; however, experiments with heterologous cells transfected with cDNA encoding the 381-residue C-terminal domain of rodent Muc3 showed that a definitive proteolytic cleavage occurs during processing in the endoplasmic reticulum. The products consisted of a V5-tagged 30 kDa extracellular glycopeptide and a Myc-tagged 49 kDa membrane-associated glycopeptide. Throughout their cellular transport to the plasma membrane, the two fragments remained associated by non-covalent SDS-sensitive interactions. Site-specific mutagenesis pinpointed the need for glycine and serine residues in the cleavage sequence Leu-Ser-Lys-Gly-Ser-Ile-Val-Val, which is localized between the two epidermal-growth-factor-like motifs of the mucin. A similar cleavage sequence (Phe-Arg-Pro-Gly downward arrow Ser-Val-Val-Val, where downward arrow signifies the cleavage site) has been reported in human MUC1 and analogous sites are present in human MUC3, MUC12 and MUC17. Thus early proteolytic cleavage may be a conserved characteristic of many membrane-associated mucins, possibly as a prelude to later release of their large extracellular domains at cell surfaces.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.