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The metalloprotease "Meprin": Structure and function in the human intestine.

Applicant Sterchi Erwin Ernst
Number 100772
Funding scheme Project funding (Div. I-III)
Research institution Institut für Biochemie und Molekulare Medizin Universität Bern
Institution of higher education University of Berne - BE
Main discipline Biochemistry
Start/End 01.04.2003 - 31.03.2008
Approved amount 260'059.00
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All Disciplines (3)

Molecular Biology
Cellular Biology, Cytology

Keywords (13)

meprin; astacin; Mmetzincin; metalloprotease; Intestine; epithelial cells; brush border membrane; extracellular matrix; adherens junctions; cell migration; colon cancer; inflammatory bowel disease; coeliac disease

Lay Summary (English)

Lay summary
Meprin is a metalloprotease which is dependent on a zinc atom in the catalytic site. Metzincins are a superfamily of such zinc-dependent metallproteases that includes several different families including MMPs (matrix metalloproteases), ADAMs (A disintegrin and metalloprotease) and astacins. Meprin belongs tothe last of these families, the astacin family, and as such is related to other proteases such as procollagen C-peptidase.Meprin consists of two homologous subunits alpha and beta that form homo- and heterooligomeric structures. The major site of expression for meprin are barrier epithelia such as those found in intestine, the proximal tubules and the podocytes in the kidney, the lactating mammary gland and the placenta. Meprin subunits may be membrane-bound or they may be secreted from the site of synthesis and they can degrade proteins involved in cell-cell, and cell-matrix interactions. In doing so, they may be involved in wound healing, but also in cell detachment and migration. It is thought that meprin plays an important part in colorectal cancer and in inflammatory bowel disease.
Direct link to Lay Summary Last update: 21.02.2013

Responsible applicant and co-applicants


Associated projects

Number Title Start Funding scheme
125212 Meprins, membrane-bound and secreted Astacinmetalloproteinases: Function in intestinal Epithelium 01.05.2009 Project funding (Div. I-III)