ArticleAmerican journal of physiology. Renal physiology2011
Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusion.
Article in American journal of physiology. Renal physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 33 citations in OpenAlex.
- Meprin β activity modulates cellular proliferation via trans-signaling IL-6-mediated AKT/ERK pathway in IR-induced kidney injury.BMC nephrology · 2025Article
- Meprin β regulates osteopontin-signaling in ischemia/reperfusion-induced kidney injury.BMC nephrology · 2025Article
- Meprin β expression modulates the interleukin-6 mediated JAK2-STAT3 signaling pathway in ischemia/reperfusion-induced kidney injury.Physiological reports · 2022Article
- 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
- An inducible intestinal epithelial cell-specific NHE3 knockout mouse model mimicking congenital sodium diarrhea.Clinical science (London, England : 1979) · 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
- Proteases: History, discovery, and roles in health and disease.The Journal of biological chemistry · 2019Review
- Review
- Undiagnosed Kidney Injury in Uninsured and Underinsured Diabetic African American Men and Putative Role of Meprin Metalloproteases in Diabetic Nephropathy.International journal of nephrology · 2018Article
- Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes.Journal of diabetes research · 2017Article
- Proteolytic processing and inactivation of CCL2/MCP-1 by meprins.Biochemistry and biophysics reports · 2016Article
- Both the anti- and pro-apoptotic functions of villin regulate cell turnover and intestinal homeostasis.Scientific reports · 2016Article
- Hypoxia Associated Proteolytic Processing of OS-9 by the Metalloproteinase Meprin β.International journal of nephrology · 2016Article
- Basement membrane protein nidogen-1 is a target of meprin β in cisplatin nephrotoxicity.Toxicology letters · 2015Article
- Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.American journal of physiology. Renal physiology · 2015Article
- Meprin metalloproteases inactivate interleukin 6.The Journal of biological chemistry · 2014Article
- Medaka villin 1-like protein (VILL) is associated with the formation of microvilli induced by decreasing salinities in the absorptive ionocytes.Frontiers in zoology · 2014Article
- Meprin A impairs epithelial barrier function, enhances monocyte migration, and cleaves the tight junction protein occludin.American journal of physiology. Renal physiology · 2013Article
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4 authors at 2 institutions in 1 country.
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Abstract
Meprins, metalloproteinases abundantly expressed in the brush-border membranes (BBMs) of rodent proximal kidney tubules, have been implicated in the pathology of renal injury induced by ischemia-reperfusion (IR). Disruption of the meprin β gene and actinonin, a meprin inhibitor, both decrease kidney injury resulting from IR. To date, the in vivo kidney substrates for meprins are unknown. The studies herein implicate villin and actin as meprin substrates. Villin and actin bind to the cytoplasmic tail of meprin β, and both meprin A and B are capable of degrading villin and actin present in kidney proteins as well as purified recombinant forms of these proteins. The products resulting from degradation of villin and actin were unique to each meprin isoform. The meprin B cleavage site in villin was Glu(744)-Val(745). Recombinant forms of rat meprin B and homomeric mouse meprin A had K(m) values for villin and actin of ∼1 μM (0.6-1.2 μM). The k(cat) values varied substantially (0.6-128 s(-1)), resulting in different efficiencies for cleavage, with meprin B having the highest k(cat)/K(m) values (128 M(-1)·s(-1) × 10(6)). Following IR, meprins and villin redistributed from the BBM to the cytosol. A 37-kDa actin fragment was detected in protein fractions from wild-type, but not in comparable preparations from meprin knockout mice. The levels of the 37-kDa actin fragment were significantly higher in kidneys subjected to IR. The data establish that meprins interact with and cleave villin and actin, and these cytoskeletal proteins are substrates for meprins.
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