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- W2612252555 endingPage "2104" @default.
- W2612252555 startingPage "2096" @default.
- W2612252555 abstract "The zinc-endopeptidases meprin α and meprin β 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 α and meprin β 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 α and meprin β 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." @default.
- W2612252555 created "2017-05-19" @default.
- W2612252555 creator A5011610563 @default.
- W2612252555 creator A5073470059 @default.
- W2612252555 creator A5073944069 @default.
- W2612252555 date "2017-11-01" @default.
- W2612252555 modified "2023-10-03" @default.
- W2612252555 title "Meprin metalloproteases: Molecular regulation and function in inflammation and fibrosis" @default.
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- W2612252555 doi "https://doi.org/10.1016/j.bbamcr.2017.05.011" @default.
- W2612252555 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28502593" @default.
- W2612252555 hasPublicationYear "2017" @default.
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