Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8
ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released und...
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Walter de Gruyter ; 2006 |
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©2006 by Walter de Gruyter Berlin New York |
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10 |
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Walter de Gruyter Online Zeitschriften |
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Enthalten in: Biological chemistry - Berlin [u.a.] : de Gruyter, 1996, 387(2006), 3 vom: 17. März, Seite 337-346 |
| Übergeordnetes Werk: |
volume:387 ; year:2006 ; number:3 ; day:17 ; month:03 ; pages:337-346 ; extent:10 |
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| DOI / URN: |
10.1515/BC.2006.045 |
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| 520 | |a ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. | ||
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10.1515/BC.2006.045 doi artikel_Grundlieferung.pp (DE-627)NLEJ246520752 DE-627 ger DE-627 rakwb Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 Walter de Gruyter 2006 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2006 by Walter de Gruyter Berlin New York ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. Walter de Gruyter Online Zeitschriften ADAM protease candidate substrates ectodomain shedding fluorescence assay peptide cleavage Naus, Silvia oth Reipschläger, Simone oth Wildeboer, Dirk oth Lichtenthaler, Stefan F. oth Mitterreiter, Stefan oth Guan, Ziqiang oth Moss, Marcia L. oth Bartsch, Jörg W. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 387(2006), 3 vom: 17. März, Seite 337-346 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:387 year:2006 number:3 day:17 month:03 pages:337-346 extent:10 https://doi.org/10.1515/BC.2006.045 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 387 2006 3 17 03 337-346 10 |
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10.1515/BC.2006.045 doi artikel_Grundlieferung.pp (DE-627)NLEJ246520752 DE-627 ger DE-627 rakwb Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 Walter de Gruyter 2006 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2006 by Walter de Gruyter Berlin New York ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. Walter de Gruyter Online Zeitschriften ADAM protease candidate substrates ectodomain shedding fluorescence assay peptide cleavage Naus, Silvia oth Reipschläger, Simone oth Wildeboer, Dirk oth Lichtenthaler, Stefan F. oth Mitterreiter, Stefan oth Guan, Ziqiang oth Moss, Marcia L. oth Bartsch, Jörg W. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 387(2006), 3 vom: 17. März, Seite 337-346 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:387 year:2006 number:3 day:17 month:03 pages:337-346 extent:10 https://doi.org/10.1515/BC.2006.045 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 387 2006 3 17 03 337-346 10 |
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10.1515/BC.2006.045 doi artikel_Grundlieferung.pp (DE-627)NLEJ246520752 DE-627 ger DE-627 rakwb Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 Walter de Gruyter 2006 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2006 by Walter de Gruyter Berlin New York ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. Walter de Gruyter Online Zeitschriften ADAM protease candidate substrates ectodomain shedding fluorescence assay peptide cleavage Naus, Silvia oth Reipschläger, Simone oth Wildeboer, Dirk oth Lichtenthaler, Stefan F. oth Mitterreiter, Stefan oth Guan, Ziqiang oth Moss, Marcia L. oth Bartsch, Jörg W. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 387(2006), 3 vom: 17. März, Seite 337-346 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:387 year:2006 number:3 day:17 month:03 pages:337-346 extent:10 https://doi.org/10.1515/BC.2006.045 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 387 2006 3 17 03 337-346 10 |
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10.1515/BC.2006.045 doi artikel_Grundlieferung.pp (DE-627)NLEJ246520752 DE-627 ger DE-627 rakwb Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 Walter de Gruyter 2006 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2006 by Walter de Gruyter Berlin New York ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. Walter de Gruyter Online Zeitschriften ADAM protease candidate substrates ectodomain shedding fluorescence assay peptide cleavage Naus, Silvia oth Reipschläger, Simone oth Wildeboer, Dirk oth Lichtenthaler, Stefan F. oth Mitterreiter, Stefan oth Guan, Ziqiang oth Moss, Marcia L. oth Bartsch, Jörg W. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 387(2006), 3 vom: 17. März, Seite 337-346 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:387 year:2006 number:3 day:17 month:03 pages:337-346 extent:10 https://doi.org/10.1515/BC.2006.045 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 387 2006 3 17 03 337-346 10 |
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10.1515/BC.2006.045 doi artikel_Grundlieferung.pp (DE-627)NLEJ246520752 DE-627 ger DE-627 rakwb Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 Walter de Gruyter 2006 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2006 by Walter de Gruyter Berlin New York ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. Walter de Gruyter Online Zeitschriften ADAM protease candidate substrates ectodomain shedding fluorescence assay peptide cleavage Naus, Silvia oth Reipschläger, Simone oth Wildeboer, Dirk oth Lichtenthaler, Stefan F. oth Mitterreiter, Stefan oth Guan, Ziqiang oth Moss, Marcia L. oth Bartsch, Jörg W. oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 387(2006), 3 vom: 17. März, Seite 337-346 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:387 year:2006 number:3 day:17 month:03 pages:337-346 extent:10 https://doi.org/10.1515/BC.2006.045 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 387 2006 3 17 03 337-346 10 |
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identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin adam8 |
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Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 |
| abstract |
ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. ©2006 by Walter de Gruyter Berlin New York |
| abstractGer |
ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. ©2006 by Walter de Gruyter Berlin New York |
| abstract_unstemmed |
ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved in ectodomain shedding of membrane proteins and is linked to inflammation and neurodegeneration. To identify potential substrates released under these pathologic conditions, we screened 10-mer peptides representing amino acid sequences from extracellular domains of various membrane proteins using the ProteaseSpot™ system. A soluble ADAM8 protease containing a pro- and metalloprotease domain was expressed in E. coli and purified as active protease owing to autocatalytic prodomain removal. From 34 peptides tested in the peptide cleavage assay, significant cleavage by soluble ADAM8 was observed for 14 peptides representing membrane proteins with functions in inflammation and neurodegeneration, among them the β-amyloid precursor protein (APP). The in vivo relevance of the ProteaseSpot™ method was confirmed by cleavage of full-length APP with ADAM8 in human embryonic kidney 293 cells expressing tagged APP. ADAM8 cleaved APP with similar efficiency as ADAM10, whereas the inactive ADAM8 mutant did not. Exchanging amino acids at defined positions in the cleavage sequence of myelin basic protein (MBP) revealed sequence criteria for ADAM8 cleavage. Taken together, the results allowed us to identify novel candidate substrates that could be cleaved by ADAM8 in vivo under pathologic conditions. ©2006 by Walter de Gruyter Berlin New York |
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| title_short |
Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8 |
| url |
https://doi.org/10.1515/BC.2006.045 |
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| author2 |
Naus, Silvia Reipschläger, Simone Wildeboer, Dirk Lichtenthaler, Stefan F. Mitterreiter, Stefan Guan, Ziqiang Moss, Marcia L. Bartsch, Jörg W. |
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Naus, Silvia Reipschläger, Simone Wildeboer, Dirk Lichtenthaler, Stefan F. Mitterreiter, Stefan Guan, Ziqiang Moss, Marcia L. Bartsch, Jörg W. |
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10.1515/BC.2006.045 |
| up_date |
2024-07-06T08:42:29.198Z |
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