ArticleAmerican journal of physiology. Renal physiology2013
Meprin A impairs epithelial barrier function, enhances monocyte migration, and cleaves the tight junction protein occludin.
Article in American journal of physiology. Renal physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 34 citations in OpenAlex.
- Meprin proteases in cutaneous homeostasis and psoriasis: pathophysiological mechanisms and therapeutic prospects.Frontiers in immunology · 2026Review
- Decellularization and Enzymatic Digestion Methods to Enhance ECM Protein Detection via MALDI-MS Imaging.Analytical chemistry · 2025Article
- Origin and Function of Monocytes in Inflammatory Bowel Disease.Journal of inflammation research · 2024Review
- Article
- Meprin β expression modulates the interleukin-6 mediated JAK2-STAT3 signaling pathway in ischemia/reperfusion-induced kidney injury.Physiological reports · 2022Article
- Proteases, Mucus, and Mucosal Immunity in Chronic Lung Disease.International journal of molecular sciences · 2021Review
- To be there when the picture is being painted.The Journal of biological chemistry · 2020Article
- Meprin-β activity modulates the β-catalytic subunit of protein kinase A in ischemia-reperfusion-induced acute kidney injury.American journal of physiology. Renal physiology · 2020Article
- LC-MS-based metabolomics analysis to identify meprin-β-associated changes in kidney tissue from mice with STZ-induced type 1 diabetes and diabetic kidney injury.American journal of physiology. Renal physiology · 2019Article
- Meprin β metalloproteases associated with differential metabolite profiles in the plasma and urine of mice with type 1 diabetes and diabetic nephropathy.BMC nephrology · 2019Article
- Review
- Proteases: History, discovery, and roles in health and disease.The Journal of biological chemistry · 2019Review
- Article
- Microscopic colitis-microbiome, barrier function and associated diseases.Annals of translational medicine · 2018Review
- Metalloproteinase meprin α regulates migration and invasion of human hepatocarcinoma cells and is a mediator of the oncoprotein Reptin.Oncotarget · 2017Article
- Meprin β contributes to collagen deposition in lung fibrosis.Scientific reports · 2017Article
- Proteolytic processing and inactivation of CCL2/MCP-1 by meprins.Biochemistry and biophysics reports · 2016Article
- Hypoxia Associated Proteolytic Processing of OS-9 by the Metalloproteinase Meprin β.International journal of nephrology · 2016Article
- The role of epithelial tight junctions involved in pathogen infections.Molecular biology reports · 2014Review
- ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Meprin metalloproteases are highly expressed at the luminal interface of the intestine and kidney and in certain leukocytes. Meprins cleave a variety of substrates in vitro, including extracellular matrix proteins, adherens junction proteins, and cytokines, and have been implicated in a number of inflammatory diseases. The linkage between results in vitro and pathogenesis, however, has not been elucidated. The present study aimed to determine whether meprins are determinative factors in disrupting the barrier function of the epithelium. Active meprin A or meprin B applied to Madin-Darby canine kidney (MDCK) cell monolayers increased permeability to fluorescein isothiocyanate-dextran and disrupted immunostaining of the tight junction protein occludin but not claudin-4. Meprin A, but not meprin B, cleaved occludin in MDCK monolayers. Experiments with recombinant occludin demonstrated that meprin A cleaves the protein between Gly(100) and Ser(101) on the first extracellular loop. In vivo experiments demonstrated that meprin A infused into the mouse bladder increased the epithelium permeability to sodium fluorescein. Furthermore, monocytes from meprin knockout mice on a C57BL/6 background were less able to migrate through an MDCK monolayer than monocytes from their wild-type counterparts. These results demonstrate the capability of meprin A to disrupt epithelial barriers and implicate occludin as one of the important targets of meprin A that may modulate inflammation.
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Registered trials
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.