Cloned (Comment) | Organism |
---|---|
recombinant expression of C-terminally Flag-tagged meprin beta in HEK-293 cells | Homo sapiens |
recombinant expression of C-terminally Flag-tagged meprin beta in HEK-293 cells | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
E153A | site-directed mutagenesis, a proteolytic inactive mutant enzyme | Homo sapiens |
additional information | generation of enzyme knockout Mep1beta-/- mice from wild-type C57/BL6N, isolation of bone marrow-derived macrophages and phenotype, overview | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | - |
Homo sapiens | 9986 | - |
cell surface | - |
Mus musculus | 9986 | - |
membrane | membrane-bound | Homo sapiens | 16020 | - |
membrane | membrane-bound | Mus musculus | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | a zinc-dependent metalloprotease | Homo sapiens | |
Zn2+ | a zinc-dependent metalloprotease | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADAM10 + H2O | Homo sapiens | i.e. a disintegrin and metalloproteinase 10 | ? | - |
? | |
ADAM10 + H2O | Mus musculus | i.e. a disintegrin and metalloproteinase 10 | ? | - |
? | |
ADAM10 + H2O | Mus musculus C57/BL6N | i.e. a disintegrin and metalloproteinase 10 | ? | - |
? | |
ADAM17 + H2O | Homo sapiens | i.e. a disintegrin and metalloproteinase 17 | ? | - |
? | |
ADAM17 + H2O | Mus musculus | i.e. a disintegrin and metalloproteinase 17 | ? | - |
? | |
ADAM17 + H2O | Mus musculus C57/BL6N | i.e. a disintegrin and metalloproteinase 17 | ? | - |
? | |
ADAM9 + H2O | Homo sapiens | i.e. a disintegrin and metalloproteinase 9 | ? | - |
? | |
ADAM9 + H2O | Mus musculus | i.e. a disintegrin and metalloproteinase 9 | ? | - |
? | |
ADAM9 + H2O | Mus musculus C57/BL6N | i.e. a disintegrin and metalloproteinase 9 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q16820 | - |
- |
Mus musculus | Q61847 | - |
- |
Mus musculus C57/BL6N | Q61847 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant Flag-tagged meprin beta from HEK-293 cells by protein G affinity chromatography. Co-immunoprecipitation of C-terminal Flag-tagged meprin beta and C-terminal Myc-tagged ADAM proteases is performed in HEK-293T cells | Homo sapiens |
recombinant Flag-tagged meprin beta from HEK-293 cells by protein G affinity chromatography. Co-immunoprecipitation of C-terminal Flag-tagged meprin beta and C-terminal Myc-tagged ADAM proteases is performed in HEK-293T cells | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
macrophage | bone marrow-derived | Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADAM10 + H2O | i.e. a disintegrin and metalloproteinase 10 | Homo sapiens | ? | - |
? | |
ADAM10 + H2O | i.e. a disintegrin and metalloproteinase 10 | Mus musculus | ? | - |
? | |
ADAM10 + H2O | i.e. a disintegrin and metalloproteinase 10, reombinant C-terminally Myc-tagged substrate, recombinant N-terminally Strep-tagged meprin beta cleaves the ADAM10 prodomain at amino acids Gln198/Glu199 and Glu199/Glu200 | Homo sapiens | ? | - |
? | |
ADAM10 + H2O | i.e. a disintegrin and metalloproteinase 10 | Mus musculus C57/BL6N | ? | - |
? | |
ADAM17 + H2O | i.e. a disintegrin and metalloproteinase 17 | Homo sapiens | ? | - |
? | |
ADAM17 + H2O | i.e. a disintegrin and metalloproteinase 17 | Mus musculus | ? | - |
? | |
ADAM17 + H2O | i.e. a disintegrin and metalloproteinase 17, reombinant C-terminally Myc-tagged substrate | Homo sapiens | ? | - |
? | |
ADAM17 + H2O | i.e. a disintegrin and metalloproteinase 17 | Mus musculus C57/BL6N | ? | - |
? | |
ADAM9 + H2O | i.e. a disintegrin and metalloproteinase 9 | Homo sapiens | ? | - |
? | |
ADAM9 + H2O | i.e. a disintegrin and metalloproteinase 9 | Mus musculus | ? | - |
? | |
ADAM9 + H2O | i.e. a disintegrin and metalloproteinase 9, reombinant C-terminally Myc-tagged substrate, recombinant N-terminally Strep-tagged meprin beta cleaves the ADAM9 prodomain at amino acids Gly189/Asp190 and Glu191/Glu192 | Homo sapiens | ? | - |
? | |
ADAM9 + H2O | i.e. a disintegrin and metalloproteinase 9 | Mus musculus C57/BL6N | ? | - |
? | |
additional information | specific N-terminal processing of ADAM9, 10, and 17 by meprin beta | Mus musculus | ? | - |
? | |
additional information | specific N-terminal processing of ADAM9, 10, and 17 by meprin beta and identification of cleavage sites within their prodomains. Direct interaction of meprin beta and ADAM proteases. Meprin beta specifically cleaves ADAM9, 10, and 17 N-terminal of the furin cleavage site | Homo sapiens | ? | - |
? | |
additional information | specific N-terminal processing of ADAM9, 10, and 17 by meprin beta | Mus musculus C57/BL6N | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
meprin beta | - |
Homo sapiens |
meprin beta | - |
Mus musculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
37 | - |
assay at | Mus musculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
7.5 | - |
assay at | Mus musculus |
General Information | Comment | Organism |
---|---|---|
evolution | meprin beta belongs to the astacins of the metzincin superfamily | Homo sapiens |
evolution | meprin beta belongs to the astacins of the metzincin superfamily | Mus musculus |
metabolism | identification of a proteolytic pathway of meprin beta with ADAM proteases to control protease activities at the cell surface as part of the protease web | Homo sapiens |
metabolism | identification of a proteolytic pathway of meprin beta with ADAM proteases to control protease activities at the cell surface as part of the protease web | Mus musculus |
additional information | enzyme sequence analysis and homology modeling of ADAM proteases, overview | Homo sapiens |
additional information | enzyme sequence analysis and homology modeling of ADAM proteases, overview | Mus musculus |
physiological function | meprin beta is a membrane-bound metalloprotease involved in extracellular matrix assembly and inflammatory processes in health and disease. A disintegrin and metalloproteinase (ADAM)10 and ADAM17 are physiologically relevant sheddases of inactive promeprin beta, which influences its substrate repertoire and subsequent biologic functions. Specific N-terminal processing of ADAM9, 10, and 17 by meprin beta. Because ADAM prodomains can act as specific inhibitors, meprin beta plays a role in the regulation of ADAM activities. Prodomain cleavage by meprin beta causes increased ADAM protease activities, e.g. demonstrated by increased ectodomain shedding activity. As demonstrated by a bacterial activator of meprin beta and additional measurement of TNF-alpha shedding on bone marrow-derived macrophages, meprin beta/ADAM protease interactions likely influence inflammatory conditions | Mus musculus |
physiological function | meprin beta is a membrane-bound metalloprotease involved in extracellular matrix assembly and inflammatory processes in health and disease. A disintegrin and metalloproteinase (ADAM)10 and ADAM17 are physiologically relevant sheddases of inactive promeprin beta, which influences its substrate repertoire and subsequent biologic functions. Specific N-terminal processing of ADAM9, 10, and 17 by meprin beta. Because ADAM prodomains can act as specific inhibitors, meprin beta plays a role in the regulation of ADAM activities. Prodomain cleavage by meprin beta causes increased ADAM protease activities, e.g. demonstrated by increased ectodomain shedding activity. As demonstrated by a bacterial activator of meprin beta and additional measurement of TNF-alpha shedding on bone marrow-derived macrophages, meprin beta/ADAM protease interactions likely influence inflammatory conditions. Meprin beta stimulates ADAM17 activity in macrophages because ADAM17-mediated TNF-alpha shedding is diminished in the absence of meprin beta | Homo sapiens |