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Mucus Detachment by Host Metalloprotease Meprin beta Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB

Artikel i vetenskaplig tidskrift
Författare R. Wichert
Anna Ermund
S. Schmidt
M. Schweinlin
M. Ksiazek
P. Arnold
K. Knittler
F. Wilkens
B. Potempa
B. Rabe
M. Stirnberg
R. Lucius
J. W. Bartsch
S. Nikolaus
M. Falk-Paulsen
P. Rosenstiel
M. Metzger
S. Rose-John
J. Potempa
Gunnar C. Hansson
P. J. Dempsey
C. Becker-Pauly
Publicerad i Cell Reports
Volym 21
Nummer/häfte 8
Sidor 2090-2103
ISSN 2211-1247
Publiceringsår 2017
Publicerad vid Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 2090-2103
Språk en
Länkar dx.doi.org/10.1016/j.celrep.2017.10...
Ämnesord aminobenzoic acid hydrolase, inflammatory-bowel-disease, functional cftr, channel, cystic-fibrosis mucus, cell-cell adhesion, porphyromonas-gingivalis, targeted disruption, epithelial-cells, small-intestine, alpha-subunit
Ämneskategorier Cellbiologi

Sammanfattning

The host metalloprotease meprin beta is required for mucin 2 (MUC2) cleavage, which drives intestinal mucus detachment and prevents bacterial over-growth. To gain access to the cleavage site in MUC2, meprin b must be proteolytically shed from epithelial cells. Hence, regulation of meprin b shedding and activation is important for physiological and pathophysiological conditions. Here, we demonstrate that meprin b activation and shedding are mutually exclusive events. Employing ex vivo small intestinal organoid and cell culture experiments, we found that ADAM-mediated shedding is restricted to the inactive pro-form of meprin beta and is completely inhibited upon its conversion to the active form at the cell surface. This strict regulation of meprin beta activity can be overridden by pathogens, as demonstrated for the bacterial protease Arg-gingipain (RgpB). This secreted cysteine protease potently converts membrane-bound meprin beta into its active form, impairing meprin beta shedding and its function as a mucus-detaching protease.

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