| The putative pleiotropic functions of meprin beta in gastric cancer. | The putative pleiotropic functions of meprin β in gastric cancer.
Siemsen W, Halske C, Behrens HM, Krüger S, Becker-Pauly C, Röcken C., Free PMC Article | 06/23/2023 |
| Structure and Dynamics of Meprin beta in Complex with a Hydroxamate-Based Inhibitor. | Structure and Dynamics of Meprin β in Complex with a Hydroxamate-Based Inhibitor.
Linnert M, Fritz C, Jäger C, Schlenzig D, Ramsbeck D, Kleinschmidt M, Wermann M, Demuth HU, Parthier C, Schilling S., Free PMC Article | 06/19/2021 |
| The authors found that increased meprin beta G32R activity at the cell surface reduces cell proliferation, but increases cell invasion. | The cancer-associated meprin β variant G32R provides an additional activation site and promotes cancer cell invasion.
Schäffler H, Li W, Helm O, Krüger S, Böger C, Peters F, Röcken C, Sebens S, Lucius R, Becker-Pauly C, Arnold P. | 07/4/2020 |
| As meprin beta cleavage of APP has been shown to result in formation of highly aggregation-prone, truncated Abeta2-40/42 peptides, enhanced APP processing by this enzyme could contribute to Alzheimer's disease pathology. | Phosphorylation of the amyloid precursor protein (APP) at Ser-675 promotes APP processing involving meprin β.
Menon PK, Koistinen NA, Iverfeldt K, Ström AL., Free PMC Article | 06/13/2020 |
| 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 |
| For meprin beta a reduction and for BMP-1 an increase in activity was reported under increasing calcium concentrations. | Meprin β and BMP-1 are differentially regulated by CaCl(2).
Schneppenheim J, Scharfenberg F, Lucius R, Becker-Pauly C, Arnold P. | 03/10/2018 |
| In this review we report on recent findings that summarize the complex molecular regulation of meprins, particular folding, activation and shedding. Dysregulation of meprin alpha and meprin beta is often associated with pathological conditions such as neurodegeneration, inflammatory bowel disease and fibrosis | Meprin metalloproteases: Molecular regulation and function in inflammation and fibrosis.
Arnold P, Otte A, Becker-Pauly C. | 02/10/2018 |
| TSPAN8 might be important for the orchestration of meprin beta at the cell surface with impact on certain proteolytic processes | Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomains.
Schmidt F, Müller M, Prox J, Arnold P, Schönherr C, Tredup C, Minder P, Ebsen H, Janssen O, Annaert W, Pietrzik C, Schmidt-Arras D, Sterchi EE, Becker-Pauly C. | 07/15/2017 |
| n conclusion, we show that the concept of cleavable linkers specific for meprin beta is feasible, as the peptides are rapidly cleaved by the enzyme while retaining their biological properties | Evaluation of ¹¹¹in-labelled exendin-4 derivatives containing different meprin β-specific cleavable linkers.
Jodal A, Pape F, Becker-Pauly C, Maas O, Schibli R, Béhé M., Free PMC Article | 12/26/2015 |
| Meprin Beta was found to be activated at the cell surface by matriptase-2. | Metalloprotease meprin β is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing APP shedding.
Jäckle F, Schmidt F, Wichert R, Arnold P, Prox J, Mangold M, Ohler A, Pietrzik CU, Koudelka T, Tholey A, Gütschow M, Stirnberg M, Becker-Pauly C. | 10/31/2015 |
| promotes inflammation in macrophages via ADAM-10 dependent pathway | Meprin-β regulates production of pro-inflammatory factors via a disintegrin and metalloproteinase-10 (ADAM-10) dependent pathway in macrophages.
Li YJ, Fan YH, Tang J, Li JB, Yu CH. | 10/4/2014 |
| Overexpression of MEP1B is associated with pancreatic neuroendocrine tumors. | Overexpression of membrane proteins in primary and metastatic gastrointestinal neuroendocrine tumors.
Carr JC, Sherman SK, Wang D, Dahdaleh FS, Bellizzi AM, O'Dorisio MS, O'Dorisio TM, Howe JR., Free PMC Article | 08/30/2014 |
| 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 metalloproteases A and B inactivate interleukin 6 | Meprin metalloproteases inactivate interleukin 6.
Keiffer TR, Bond JS., Free PMC Article | 05/17/2014 |
| 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 |
| metalloprotease meprin beta generates amino terminal-truncated amyloid beta peptide species | The metalloprotease meprin β generates amino terminal-truncated amyloid β peptide species.
Bien J, Jefferson T, Causević M, Jumpertz T, Munter L, Multhaup G, Weggen S, Becker-Pauly C, Pietrzik CU., Free PMC Article | 12/22/2012 |
| 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 |
| Cystatin C was an inhibitor for human meprin alpha(K(i) = 8.5 x 10(-6) M) but, interestingly, not for meprin beta. | Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases.
Hedrich J, Lottaz D, Meyer K, Yiallouros I, Jahnen-Dechent W, Stöcker W, Becker-Pauly C. | 01/29/2011 |
| meprins could be important players in several remodeling processes involving collagen fiber deposition | Processing of procollagen III by meprins: new players in extracellular matrix assembly?
Kronenberg D, Bruns BC, Moali C, Vadon-Le Goff S, Sterchi EE, Traupe H, Böhm M, Hulmes DJ, Stöcker W, Becker-Pauly C. | 01/1/2011 |
| Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator) | Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article | 06/30/2010 |
| data indicate that, at least under pathological conditions, meprinbeta might attack specific functional sites in tenascin-C that are important for its oligomerization and anti-adhesive activity | Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading.
Ambort D, Brellier F, Becker-Pauly C, Stöcker W, Andrejevic-Blant S, Chiquet M, Sterchi EE. | 04/12/2010 |
| two different metalloprotease activities are responsible for the constitutive and the PMA-stimulated hmeprinbeta shedding | Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinbeta metalloprotease.
Hahn D, Pischitzis A, Roesmann S, Hansen MK, Leuenberger B, Luginbuehl U, Sterchi EE. | 01/21/2010 |
| Mephrin beta induced a dramatic change in cell morphology and reduced the cell number, indicating a function in terminal differentiation, whereas meprin alpha did not affect cell viability, and may play a role in basal keratinocyte proliferation. | The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation.
Becker-Pauly C, Höwel M, Walker T, Vlad A, Aufenvenne K, Oji V, Lottaz D, Sterchi EE, Debela M, Magdolen V, Traupe H, Stöcker W. | 01/21/2010 |