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    Mep1b meprin 1 beta [ Mus musculus (house mouse) ]

    Gene ID: 17288, updated on 21-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Meprin beta knockout reduces brain Abeta levels and rescues learning and memory impairments in the APP/lon mouse model for Alzheimer's disease.

    Meprin β knockout reduces brain Aβ levels and rescues learning and memory impairments in the APP/lon mouse model for Alzheimer's disease.
    Marengo L, Armbrust F, Schoenherr C, Storck SE, Schmitt U, Zampar S, Wirths O, Altmeppen H, Glatzel M, Kaether C, Weggen S, Becker-Pauly C, Pietrzik CU., Free PMC Article

    03/12/2022
    Meprin-beta enhances ischemia reperfusion-induced kidney injury in part by modulating mediators of the PKA-Cbeta signaling pathway.

    Meprin-β activity modulates the β-catalytic subunit of protein kinase A in ischemia-reperfusion-induced acute kidney injury.
    Ahmed F, Mwiza JM, Fernander M, Yahaya I, Abousaad S, Ongeri EM., Free PMC Article

    07/18/2020
    meprin-beta activity enhances diabetic kidney injury in part by altering the metabolite balance in kidneys, favoring high levels of uremic toxins such as indoxyl sulfate and N-methyl-pyridone-carboxamide

    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.
    Gooding J, Cao L, Ahmed F, Mwiza JM, Fernander M, Whitaker C, Acuff Z, McRitchie S, Sumner S, Ongeri EM., Free PMC Article

    04/4/2020
    Results provide evidence that meprin beta is involved in collagen deposition in vivo in the lung of bleomycin treated mice and it localized in region with immature collagen. This suggests that meprin beta can favor the progression of the fibrotic process enhancing collagen processing and deposition.

    Meprin β contributes to collagen deposition in lung fibrosis.
    Biasin V, Wygrecka M, Marsh LM, Becker-Pauly C, Brcic L, Ghanim B, Klepetko W, Olschewski A, Kwapiszewska G., Free PMC Article

    11/3/2018
    This secreted cysteine protease potently converts membrane-bound meprin beta into its active form, impairing meprin beta shedding and its function as a mucus-detaching protease

    Mucus Detachment by Host Metalloprotease Meprin β Requires Shedding of Its Inactive Pro-form, which Is Abrogated by the Pathogenic Protease RgpB.
    Wichert R, Ermund A, Schmidt S, Schweinlin M, Ksiazek M, Arnold P, Knittler K, Wilkens F, Potempa B, Rabe B, Stirnberg M, Lucius R, Bartsch JW, Nikolaus S, Falk-Paulsen M, Rosenstiel P, Metzger M, Rose-John S, Potempa J, Hansson GC, Dempsey PJ, Becker-Pauly C.

    08/4/2018
    Meprin alphabeta knockout (alphabetaKO) mice and their wild-type (WT) counterparts to streptozotocin-induced type 1 diabetes. The 18-week survival rates were significantly lower for diabetic meprin alphabetaKO mice when compared to those for their wild type counterparts.

    Meprin Metalloprotease Deficiency Associated with Higher Mortality Rates and More Severe Diabetic Kidney Injury in Mice with STZ-Induced Type 1 Diabetes.
    Bylander JE, Ahmed F, Conley SM, Mwiza JM, Ongeri EM., Free PMC Article

    05/26/2018
    no significant dentin malformation was observed in Mep1b (-/-) or Mep1a (-/-) deficient mice.

    Deficiency of the DSPP-cleaving enzymes meprin α and meprin β does not result in dentin malformation in mice.
    Arnold P, Koopmann L, Peters F, Birkenfeld F, Goff SV, Damm T, Qin C, Moali C, Lucius R, Becker-Pauly C.

    06/3/2017
    meprin alpha and meprin beta join the modulators of Reelin signalling as they cleave Reelin at a specific site and are upregulated under specific pathological conditions.

    Determination of cleavage site of Reelin between its sixth and seventh repeat and contribution of meprin metalloproteases to the cleavage.
    Sato Y, Kobayashi D, Kohno T, Kidani Y, Prox J, Becker-Pauly C, Hattori M.

    09/3/2016
    These studies provide strong evidence for a pathophysiological link between meprin beta and urinary excretion of cleaved nidogen-1 during cisplatin-induced acute kidney injury.

    Basement membrane protein nidogen-1 is a target of meprin β in cisplatin nephrotoxicity.
    Herzog C, Marisiddaiah R, Haun RS, Kaushal GP., Free PMC Article

    08/15/2015
    While meprin A only cleaved protein kinase A (PKA) catalytic subunit beta1, meprin B cleaved all three PKA catalytic isoforms.

    Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.
    Niyitegeka JM, Bastidas AC, Newman RH, Taylor SS, Ongeri EM., Free PMC Article

    03/21/2015
    Meprin beta is an endogenous zinc-dependent metalloprotease now shown to cleave the N-terminal region of the MUC2 mucin at two specific sites.

    Microbial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus.
    Schütte A, Ermund A, Becker-Pauly C, Johansson ME, Rodriguez-Pineiro AM, Bäckhed F, Müller S, Lottaz D, Bond JS, Hansson GC., Free PMC Article

    11/29/2014
    Suggest role for in meprin-beta-Fra2 axis in mediating vascular remodelling in pulmonary hypertension.

    Meprin β, a novel mediator of vascular remodelling underlying pulmonary hypertension.
    Biasin V, Marsh LM, Egemnazarov B, Wilhelm J, Ghanim B, Klepetko W, Wygrecka M, Olschewski H, Eferl R, Olschewski A, Kwapiszewska G.

    06/7/2014
    meprin alpha and meprin beta are unique in their ability to process and release both C- and N-propeptides from type I procollagen in vitro and in vivo

    Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength.
    Broder C, Arnold P, Vadon-Le Goff S, Konerding MA, Bahr K, Müller S, Overall CM, Bond JS, Koudelka T, Tholey A, Hulmes DJ, Moali C, Becker-Pauly C., Free PMC Article

    11/23/2013
    of the 151 new extracellular substrates identified, it was notable that ADAM10 the constitutive alpha-secretase-is activated by meprin beta through cleavage of the propeptide

    The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10.
    Jefferson T, Auf dem Keller U, Bellac C, Metz VV, Broder C, Hedrich J, Ohler A, Maier W, Magdolen V, Sterchi E, Bond JS, Jayakumar A, Traupe H, Chalaris A, Rose-John S, Pietrzik CU, Postina R, Overall CM, Becker-Pauly C., Free PMC Article

    03/2/2013
    the binding of S-MBP to meprins triggers the complement activation through the lectin pathway and may cause the acute renal failure due to ischemia/reperfusion injury on kidney transplantation and hemorrhagic shock

    Role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney.
    Hirano M, Ma BY, Kawasaki N, Oka S, Kawasaki T.

    03/31/2012
    Processing of APP by meprin beta was subsequently validated using in vitro and in vivo approaches. N-terminal APP fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin beta(-/-) mouse brain lysates

    Metalloprotease meprin beta generates nontoxic N-terminal amyloid precursor protein fragments in vivo.
    Jefferson T, Čaušević M, auf dem Keller U, Schilling O, Isbert S, Geyer R, Maier W, Tschickardt S, Jumpertz T, Weggen S, Bond JS, Overall CM, Pietrzik CU, Becker-Pauly C., Free PMC Article

    10/15/2011
    Demonstrate that the metalloprotease meprin beta and gamma-ENaC associate directly through cytoplasmic domains.

    Activation of the epithelial sodium channel by the metalloprotease meprin β subunit.
    Garcia-Caballero A, Ishmael SS, Dang Y, Gillie D, Bond JS, Milgram SL, Stutts MJ., Free PMC Article

    05/28/2011
    Absence of meprin A aggravates chronic inflammation and lack of meprin B affords some protection from injury. Manipulation of expression of meprin gene products may have therapeutic potential.

    Balance of meprin A and B in mice affects the progression of experimental inflammatory bowel disease.
    Banerjee S, Jin G, Bradley SG, Matters GL, Gailey RD, Crisman JM, Bond JS., Free PMC Article

    03/19/2011
    meprin alpha/beta null (alpha(-/-)/beta(-/-)) mice had decreased prevalence of resident monocytes and natural killer (NK) cells in blood, with a concomitant accumulation of inflammatory monocytes and NK cells in bone marrow.

    Disruption of the meprin alpha and beta genes in mice alters homeostasis of monocytes and natural killer cells.
    Sun Q, Jin HJ, Bond JS., Free PMC Article

    01/21/2010
    identifies proIL-18 as a biologically important substrate for meprin beta and implicates meprins in the modulation of inflammation

    Prointerleukin-18 is activated by meprin beta in vitro and in vivo in intestinal inflammation.
    Banerjee S, Bond JS., Free PMC Article

    01/21/2010
    meprinbeta may play a protective role against the progression of renal injury through the degradation of extracellular matrix and bioactive peptides

    Downregulated expression in high IgA (HIGA) mice and the renal protective role of meprinbeta.
    Yoshimura H, Ito M, Kuwahara Y, Ishii A, Tsuritani K, Nakamura A, Hirasawa Y, Nagamatsu T.

    01/21/2010
    Following ischemia-reperfusion the redistribution of active meprin-alpha/beta is a major contributor to renal injury and subsequent inflammation.

    Targeted disruption of the meprin metalloproteinase beta gene protects against renal ischemia-reperfusion injury in mice.
    Bylander J, Li Q, Ramesh G, Zhang B, Reeves WB, Bond JS.

    01/21/2010
    disruption of the meprin beta allele in mice affects embryonic viability, birth weight, renal gene expression profiles, and the distribution of meprin alpha in kidney and intestine.

    Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles.
    Norman LP, Jiang W, Han X, Saunders TL, Bond JS., Free PMC Article

    01/21/2010
    Meprin beta is expressed by leukocytes in the draining lymph node of the intestine, regardless of the inflammatory status of the animal, and is likely to contribute to leukocyte transmigration events important to intestinal immune responses.

    Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix.
    Crisman JM, Zhang B, Norman LP, Bond JS.

    01/21/2010
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