Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1864, Issue 11, Pages 2096-2104Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2017.05.011
Keywords
Meprin metalloproteases; Inflammation; Fibrosis; Shedding; Interleukin-6 receptor; CD99
Categories
Funding
- Deutsche Forschungsgemeinschaft (DFG) [SFB 877]
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The zinc-endopeptidases meprin a and meprin beta are extracellular proteases involved in connective tissue homeostasis, intestinal barrier function and immunological processes. Meprins are unique among other extracellular proteases with regard to cleavage specificity and structure. Meprin alpha and meprin beta have a strong preference for negatively charged amino acids around the scissile bond, reflected by cleavage sites identified in procollagen I, the amyloid precursor protein (APP) and the interleukin-6 receptor (IL-6R). In this review we report on recent findings that summarize the complex molecular regulation of meprins, particular folding, activation and shedding. Dysregulation of meprin alpha and meprin beta is often associated with pathological conditions such as neurodegeneration, inflammatory bowel disease and fibrosis. Based on mouse models and patient data we suggest meprins as possible key regulators in the onset and progression of fibrotic disorders, leading to severe diseases such as pulmonary hypertension. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.
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