ReviewThe Biochemical journal2013
The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.
Review in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 128 citations in OpenAlex.
- Serum meprin α levels for the detection of systemic inflammatory response syndrome.Molecular medicine (Cambridge, Mass.) · 2026Article
- The Role of Meprins on the Brain Extracellular Matrix and Perineuronal Nets.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Meprin-β levels are increased in the brain and the cerebrospinal fluid of Alzheimer's disease patients.Alzheimer's research & therapy · 2026Article
- Meprin proteases in cutaneous homeostasis and psoriasis: pathophysiological mechanisms and therapeutic prospects.Frontiers in immunology · 2026Review
- Crossing the barrier or how regulation of ovastacin controls fertilization and translates into clinical phenotypes.iScience · 2025Review
- Exploring cadmium-binding proteins in Japanese scallops Mizuhopecten yessoensis: isolation and characterization.Environmental science and pollution research international · 2025Article
- A novel mouse model for N-terminal truncated Aβ2-x generation through meprin β overexpression in astrocytes.Cellular and molecular life sciences : CMLS · 2024Article
- Review
- Synthesis and structure-activity relationships of pyrazole-based inhibitors of meprin α and β.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Review
- Identifying causal serum protein-cardiometabolic trait relationships using whole genome sequencing.Human molecular genetics · 2023Article
- Proteolytic processing of galectin-3 by meprin metalloproteases is crucial for host-microbiome homeostasis.Science advances · 2023Article
- Initial detachment of the mouse oocyte from the zona pellucida is mediated by metallopeptidase activity†.Biology of reproduction · 2023Article
- Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor.Nature communications · 2022Article
- The structure, biosynthesis, and biological roles of fetuin-A: A review.Frontiers in cell and developmental biology · 2022Review
- A preliminary study of possible fibrotic role of meprin metalloproteases in scleroderma patients.Archives of rheumatology · 2021Article
- Multi-Antigen Imaging Reveals Inflammatory DC, ADAM17 and Neprilysin as Effectors in Keloid Formation.International journal of molecular sciences · 2021Article
- Structure and Dynamics of Meprin β in Complex with a Hydroxamate-Based Inhibitor.International journal of molecular sciences · 2021Article
- Discovery and Optimization of Selective Inhibitors of Meprin α (Part I).Pharmaceuticals (Basel, Switzerland) · 2021Article
- Discovery and Optimization of Selective Inhibitors of Meprin α (Part II).Pharmaceuticals (Basel, Switzerland) · 2021Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The metalloproteases meprin α and meprin β exhibit structural and functional features that are unique among all extracellular proteases. Although meprins were discovered more than 30 years ago, their precise substrates and physiological roles have been elusive. Both enzymes were originally found to be highly expressed in kidney and intestine, which focused research on these particular tissues and associated pathologies. Only recently it has become evident that meprins exhibit a much broader expression pattern, implicating functions in angiogenesis, cancer, inflammation, fibrosis and neurodegenerative diseases. Different animal models, as well as proteomics approaches for the identification of protease substrates, have helped to reveal more precise molecular signalling events mediated by meprin activity, such as activation and release of pro-inflammatory cytokines. APP (amyloid precursor protein) is cleaved by meprin β in vivo, reminiscent of the β-secretase BACE1 (β-site APP-cleaving enzyme 1). The subsequent release of Aβ (amyloid β) peptides is thought to be the major cause of the neurodegenerative Alzheimer's disease. On the other hand, ADAM10 (a disintegrin and metalloprotease domain 10), which is the constitutive α-secretase, was shown to be activated by meprin β, which is itself shed from the cell surface by ADAM10. In skin, both meprins are overexpressed in fibrotic tumours, characterized by massive accumulation of fibrillar collagens. Indeed, procollagen III is processed to its mature form by meprin α and meprin β, an essential step in collagen fibril assembly. The recently solved crystal structure of meprin β and the unique cleavage specificity of these proteases identified by proteomics will help to generate specific inhibitors that could be used as therapeutics to target meprins under certain pathological conditions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.