Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor
Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of...
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De Gruyter ; 2013 |
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7 |
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Walter de Gruyter Online Zeitschriften |
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Enthalten in: Biological chemistry - Berlin [u.a.] : de Gruyter, 1996, 394(2013), 3 vom: 02. Feb., Seite 385-391 |
| Übergeordnetes Werk: |
volume:394 ; year:2013 ; number:3 ; day:02 ; month:02 ; pages:385-391 ; extent:7 |
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10.1515/hsz-2012-0291 |
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| 520 | |a Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. | ||
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10.1515/hsz-2012-0291 doi artikel_Grundlieferung.pp (DE-627)NLEJ246932724 DE-627 ger DE-627 rakwb Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor De Gruyter 2013 7 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. Walter de Gruyter Online Zeitschriften angiogenesis kallikrein-related peptidase 12 kininogenase serine protease Kryza, Thomas oth Lalmanach, Gilles oth Lavergne, Marion oth Lecaille, Fabien oth Reverdiau, Pascale oth Courty, Yves oth Heuzé-Vourc’h, Nathalie oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 394(2013), 3 vom: 02. Feb., Seite 385-391 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:394 year:2013 number:3 day:02 month:02 pages:385-391 extent:7 https://doi.org/10.1515/hsz-2012-0291 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 394 2013 3 02 02 385-391 7 |
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10.1515/hsz-2012-0291 doi artikel_Grundlieferung.pp (DE-627)NLEJ246932724 DE-627 ger DE-627 rakwb Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor De Gruyter 2013 7 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. Walter de Gruyter Online Zeitschriften angiogenesis kallikrein-related peptidase 12 kininogenase serine protease Kryza, Thomas oth Lalmanach, Gilles oth Lavergne, Marion oth Lecaille, Fabien oth Reverdiau, Pascale oth Courty, Yves oth Heuzé-Vourc’h, Nathalie oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 394(2013), 3 vom: 02. Feb., Seite 385-391 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:394 year:2013 number:3 day:02 month:02 pages:385-391 extent:7 https://doi.org/10.1515/hsz-2012-0291 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 394 2013 3 02 02 385-391 7 |
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10.1515/hsz-2012-0291 doi artikel_Grundlieferung.pp (DE-627)NLEJ246932724 DE-627 ger DE-627 rakwb Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor De Gruyter 2013 7 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. Walter de Gruyter Online Zeitschriften angiogenesis kallikrein-related peptidase 12 kininogenase serine protease Kryza, Thomas oth Lalmanach, Gilles oth Lavergne, Marion oth Lecaille, Fabien oth Reverdiau, Pascale oth Courty, Yves oth Heuzé-Vourc’h, Nathalie oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 394(2013), 3 vom: 02. Feb., Seite 385-391 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:394 year:2013 number:3 day:02 month:02 pages:385-391 extent:7 https://doi.org/10.1515/hsz-2012-0291 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 394 2013 3 02 02 385-391 7 |
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10.1515/hsz-2012-0291 doi artikel_Grundlieferung.pp (DE-627)NLEJ246932724 DE-627 ger DE-627 rakwb Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor De Gruyter 2013 7 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. Walter de Gruyter Online Zeitschriften angiogenesis kallikrein-related peptidase 12 kininogenase serine protease Kryza, Thomas oth Lalmanach, Gilles oth Lavergne, Marion oth Lecaille, Fabien oth Reverdiau, Pascale oth Courty, Yves oth Heuzé-Vourc’h, Nathalie oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 394(2013), 3 vom: 02. Feb., Seite 385-391 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:394 year:2013 number:3 day:02 month:02 pages:385-391 extent:7 https://doi.org/10.1515/hsz-2012-0291 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 394 2013 3 02 02 385-391 7 |
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10.1515/hsz-2012-0291 doi artikel_Grundlieferung.pp (DE-627)NLEJ246932724 DE-627 ger DE-627 rakwb Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor De Gruyter 2013 7 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. Walter de Gruyter Online Zeitschriften angiogenesis kallikrein-related peptidase 12 kininogenase serine protease Kryza, Thomas oth Lalmanach, Gilles oth Lavergne, Marion oth Lecaille, Fabien oth Reverdiau, Pascale oth Courty, Yves oth Heuzé-Vourc’h, Nathalie oth Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 394(2013), 3 vom: 02. Feb., Seite 385-391 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:394 year:2013 number:3 day:02 month:02 pages:385-391 extent:7 https://doi.org/10.1515/hsz-2012-0291 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 394 2013 3 02 02 385-391 7 |
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pro-angiogenic effect of human kallikrein-related peptidase 12 (klk12) in lung endothelial cells does not depend on kinin-mediated activation of b2 receptor |
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Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor |
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Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. |
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Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. |
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Kallikrein-12 (KLK12) may play an important role in angiogenesis modulating proangiogenic factor bioavailability and activating the kinin receptor B2 pathway. We studied whether KLK12 had an impact on angiogenesis and the activation of kinin receptor B2 results from the KLK12-dependent generation of kinins. KLK12 efficiently hydrolyzed high molecular weight kininogen, liberating a fragment containing the carboxy-terminal end of kinins. The kininogenase activity of KLK12 was poor, however, due to the cleavage resistance of the N-terminal side of the kinin sequence. A very low amount of kinins was accordingly released after in vitro incubation of high molecular weight kininogen with KLK12 and thus the proangiogenic activity of KLK12 in lung endothelial cells was not related to a kinin release. |
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Pro-angiogenic effect of human kallikrein-related peptidase 12 (KLK12) in lung endothelial cells does not depend on kinin-mediated activation of B2 receptor |
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Kryza, Thomas Lalmanach, Gilles Lavergne, Marion Lecaille, Fabien Reverdiau, Pascale Courty, Yves Heuzé-Vourc’h, Nathalie |
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Kryza, Thomas Lalmanach, Gilles Lavergne, Marion Lecaille, Fabien Reverdiau, Pascale Courty, Yves Heuzé-Vourc’h, Nathalie |
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| doi_str |
10.1515/hsz-2012-0291 |
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2024-07-06T09:37:54.546Z |
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