Till sidans topp

Sidansvarig: Webbredaktion
Sidan uppdaterades: 2012-09-11 15:12

Tipsa en vän
Utskriftsversion

Proteomic analyses of the… - Göteborgs universitet Till startsida
Webbkarta
Till innehåll Läs mer om hur kakor används på gu.se

Proteomic analyses of the two mucus layers of the colon barrier reveal that their main component, the Muc2 mucin, is strongly bound to the Fcgbp protein.

Artikel i vetenskaplig tidskrift
Författare Malin E V Johansson
Kristina A Thomsson
Gunnar C. Hansson
Publicerad i Journal of proteome research
Volym 8
Nummer/häfte 7
Sidor 3549-57
ISSN 1535-3893
Publiceringsår 2009
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 3549-57
Språk en
Länkar dx.doi.org/10.1021/pr9002504
Ämnesord Animals, Cell Adhesion Molecules, metabolism, Chromatography, Liquid, methods, Colon, metabolism, Disulfides, chemistry, Humans, Intestine, Large, metabolism, Mass Spectrometry, methods, Mice, Mice, Inbred C57BL, Mucin-2, metabolism, Mucins, chemistry, Mucus, metabolism, Proteomics, methods, von Willebrand Factor, chemistry
Ämneskategorier Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci)

Sammanfattning

The colon epithelium is protected from the luminal microbes as recently revealed by an inner firmly attached mucus layer impervious to bacteria and an outer loose mucus layer that is the habitat of bacteria. For an additional understanding of these layers, we analyzed the protein composition of these two mucus layers from the mouse colon. Proteomics using nano-LC-MS and MS/MS revealed more than 1000 protein entries. As the mucus layers contain detached cells, a majority of the proteins had an intracellular origin. However, at least 44 entries were described as secreted proteins and predicted to be mucus constituents together with extracellular/plasma and bacterial proteins, the latter largely in the loose mucus layer. A major protein was the Muc2 mucin that by its net-like disulfide-bonded polymer structure builds the mucus. When guanidinium chloride insoluble Muc2 units were analyzed, N-terminal parts of the Fc-gamma binding protein (Fcgbp) was found to be covalently attached in mouse and human colon, whereas its C-terminus was lost by reducing the disulfide bonds. In conclusion, the Fcgbp protein is probably cleaved at GD/PH and covalently attached to Muc2 via one or several of its von Willebrand D domains.

Sidansvarig: Webbredaktion|Sidan uppdaterades: 2012-09-11
Dela:

På Göteborgs universitet använder vi kakor (cookies) för att webbplatsen ska fungera på ett bra sätt för dig. Genom att surfa vidare godkänner du att vi använder kakor.  Vad är kakor?