An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin
about
Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprinTargeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profilesMeprins, membrane-bound and secreted astacin metalloproteinasesADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactionsThe astacin family of metalloendopeptidasesHeterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitroActivation of human meprin-alpha in a cell culture model of colorectal cancer is triggered by the plasminogen-activating systemSecretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunitsThe cleavage of protein kinase A by the kinase-splitting membranal proteinase is reproduced by meprin betaProbing the active sites and mechanisms of rat metalloproteases meprin A and BCompartmentalised expression of meprin in small intestinal mucosa: enhanced expression in lamina propria in coeliac disease.The evolution of the vertebrate metzincins; insights from Ciona intestinalis and Danio rerio.ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A.The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family.Enhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer.Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.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-reperfusionActinonin, a meprin A inhibitor, protects the renal microcirculation during sepsisCopper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis.The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.Meprin A metalloproteinase and its role in acute kidney injury.Purification and cloning of carp nephrosin, a secreted zinc endopeptidase of the astacin family.Meprin A and meprin alpha generate biologically functional IL-1beta from pro-IL-1betaDisruption of the meprin alpha and beta genes in mice alters homeostasis of monocytes and natural killer cells.Isoform switching of type IV collagen is developmentally arrested in X-linked Alport syndrome leading to increased susceptibility of renal basement membranes to endoproteolysis.Pharmacological targets in the renal peritubular microenvironment: implications for therapy for sepsis-induced acute kidney injury.Extracellular matrix and the kidney.A novel 2D-based approach to the discovery of candidate substrates for the metalloendopeptidase meprin.Human N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin): genomic structure of the alpha and beta subunits.N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase beta (human meprinbeta). A 13-amino-acid sequence is required for proteolyticprocessing and subsequent secretion.Activation mechanism of meprins, members of the astacin metalloendopeptidase family.Cysteine mutations in the MAM domain result in monomeric meprin and alter stability and activity of the proteinase.Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes.Proteolytic processing of the alpha-subunit of rat endopeptidase-24.18 by furin.Proteolytic processing and inactivation of CCL2/MCP-1 by meprins.Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors.Basement membrane protein nidogen-1 is a target of meprin β in cisplatin nephrotoxicity.Meprin-alpha in chronic diabetic nephropathy: interaction with the renin-angiotensin axis.Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities.
P2860
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P2860
An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin
description
1994 nî lūn-bûn
@nan
1994 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
An old enzyme with a new funct ...... d its identification as meprin
@ast
An old enzyme with a new funct ...... d its identification as meprin
@en
An old enzyme with a new funct ...... d its identification as meprin
@nl
type
label
An old enzyme with a new funct ...... d its identification as meprin
@ast
An old enzyme with a new funct ...... d its identification as meprin
@en
An old enzyme with a new funct ...... d its identification as meprin
@nl
prefLabel
An old enzyme with a new funct ...... d its identification as meprin
@ast
An old enzyme with a new funct ...... d its identification as meprin
@en
An old enzyme with a new funct ...... d its identification as meprin
@nl
P2093
P2860
P356
P1476
An old enzyme with a new funct ...... d its identification as meprin
@en
P2093
P2860
P304
P356
10.1083/JCB.126.5.1319
P407
P577
1994-09-01T00:00:00Z