Mucins are the major macromolecular components of mucus. Each mucin has a unique and characteristic sequence of tandemly repeating amino acids rich in serine and/or threonine. The tandem repeat domain is the primary region for O -linked glycosylation of the molecule.

av A Herrmann · 2000 · Citerat av 2 — Among the latter, the oligomeric mucins are responsible for mucus formation. Mucins from rat small intestine occurred as an 'insoluble glycoprotein complex'. identified in colorectal carcinoma, including variations in blood group A, Lea, Leb, Department of Cell and Molecular Biology, Lund University; defense location

The mucin expands from the vesicle into this space at a very rapid rate. It is hypothesized that this rapid expansion is mediated by the exchange of sodium (and other monovalent cations) from the extracellular space with divalent calcium ions that are present in the vesicle in high concentration prior to exocytosis. All mucins are highly O-glycosylated by variable glycans depending on species, histoblood group and organ. This makes the intestinal main mucin MUC2 non-degradable by the host digestive system but A 'read' is counted each time someone views a publication summary (such as the title, abstract, and list of authors), clicks on a figure, or views or downloads the full-text.

Mucin biology group

Mucins are large, highly glycosylated molecules having typical mucin domains, where the oligosaccharides are linked via N-acetylgalactosamine to the amino acids threonine and serine. Mucins are forming the gel-like properties of mucus. The major mucin of the gastrointestinal tract is called MUC2 and is produced by the intestinal goblet cells. There are two main groups of mucins; the classical gel-forming polymeric mucins (MUC2, MUC5AC, MUC5B, and MUC6) and a more heterogeneous group of monomeric transmembrane mucins (MUC1, MUC3, MUC4, MUC12, MUC13, MUC15, MUC16, MUC17, MUC20, and MUC21). One research group attempting to identify the specifics regarding mucins is the Mucin Biology Group at the University of Gothenburg in Sweden. There are currently more than 20 human mucin genes that have been identified. The genes encoding mucin proteins are generally designated MUC (MUC1-MUC20) and have homologs in many species other than humans.

Brendan is a postdoctoral researcher in the Mucin Biology Group All mucins are highly O-glycosylated by variable glycans depending on species, histoblood group and organ. This makes the intestinal main mucin MUC2 non-degradable by the host digestive system but 2008-02-26 · Mucin-like protein 3.

Accepted in Biomacromolecules, doi.org/10.1021/acs.biomac.1c00073. 39. Käsdorf B, Weber F, Petrou G, Srivastava V, Crouzier T, Lieleg O (2017) Mucin-inspired lubrication on Nature Publishing Group, London, http://www.els.net/.

Department of Cell and 2 Resources Mucin Biology Group, University of Gothenburg Mucins, Methods and Protocols Methods in Molecular Biology v. 842 (Springer Protocols).

Nature Chemistry, Nature Publishing Group 2020, Vol. The mucin-selective protease StcE enables molecular and functional analysis of human cancer-associated ACS Chemical Biology, American Chemical Society (ACS) 2019, Vol.

The mucin expands from the vesicle into this space at a very rapid rate. Although reduced mucin production is often related to an alteration in the gut microbiota, the underlying mechanisms remain unclear. Nevertheless, changes in nutrient substrates or ecological niches of the endogenous bacteria are implicated.

Brendan Dolan currently works at the Department of Medical Biochemistry and Cell Biology, University of Gothenburg. Brendan is a postdoctoral researcher in the Mucin Biology Group Mucin is a mucoprotein found in mucous. It coats the epithelial surface. Gastric mucin protects the stomach from an attack of acids.
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Mucins are extracellular large highly glycosylated molecules having mucin domains. Usually one also demands that there is more than 50% of the mass that is due to glycans. Mucin domains (with glycans) or PTS domains (protein core only) are found also in other extracellular proteins, but are dominating in molecules that are usually called mucins.

Käsdorf B, Weber F, Petrou G, Srivastava V, Crouzier T, Lieleg O (2017) Mucin-inspired lubrication on Nature Publishing Group, London, http://www.els.net/. av M PiHl · Citerat av 4 — formation or eradicate biofilms from peritoneal dialysis catheters, thus reducing the number aerobes as a group are frequently encountered in peritonitis, for example the above 2006).