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Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen

The contact system of coagulation can be activated when in contact with biomaterials. As collagen is being tested in novel biomaterials in this study, we have investigated how type IV collagen affects plasma kallikrein and C1-inhibitor. Firstly, we showed C1-inhibitor binds to type IV collagen with...

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Detalles Bibliográficos
Autores principales: Ravindran, Sriram, Schapira, Marc, Patston, Philip A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3296203/
https://www.ncbi.nlm.nih.gov/pubmed/22481936
http://dx.doi.org/10.1155/2012/212417
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author Ravindran, Sriram
Schapira, Marc
Patston, Philip A.
author_facet Ravindran, Sriram
Schapira, Marc
Patston, Philip A.
author_sort Ravindran, Sriram
collection PubMed
description The contact system of coagulation can be activated when in contact with biomaterials. As collagen is being tested in novel biomaterials in this study, we have investigated how type IV collagen affects plasma kallikrein and C1-inhibitor. Firstly, we showed C1-inhibitor binds to type IV collagen with a Kd of 0.86 μM. The effects of type IV collagen on plasma kallikrein, factor XIIa, and β-factor XIIa activity and on C1-inhibitor function were determined. Factor XIIa rapidly lost activity in the presence of type IV collagen, whereas plasma kallikrein and β-factor XIIa were more stable. The rate of inhibition of plasma kallikrein by C1-inhibitor was decreased by type IV collagen in a dose-dependent manner. These studies could be relevant to the properties of biomaterials, which contain collagen, and should be considered in the testing for biocompatibility.
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spelling pubmed-32962032012-04-05 Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen Ravindran, Sriram Schapira, Marc Patston, Philip A. Int J Biomater Research Article The contact system of coagulation can be activated when in contact with biomaterials. As collagen is being tested in novel biomaterials in this study, we have investigated how type IV collagen affects plasma kallikrein and C1-inhibitor. Firstly, we showed C1-inhibitor binds to type IV collagen with a Kd of 0.86 μM. The effects of type IV collagen on plasma kallikrein, factor XIIa, and β-factor XIIa activity and on C1-inhibitor function were determined. Factor XIIa rapidly lost activity in the presence of type IV collagen, whereas plasma kallikrein and β-factor XIIa were more stable. The rate of inhibition of plasma kallikrein by C1-inhibitor was decreased by type IV collagen in a dose-dependent manner. These studies could be relevant to the properties of biomaterials, which contain collagen, and should be considered in the testing for biocompatibility. Hindawi Publishing Corporation 2012 2012-02-12 /pmc/articles/PMC3296203/ /pubmed/22481936 http://dx.doi.org/10.1155/2012/212417 Text en Copyright © 2012 Sriram Ravindran et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Ravindran, Sriram
Schapira, Marc
Patston, Philip A.
Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen
title Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen
title_full Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen
title_fullStr Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen
title_full_unstemmed Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen
title_short Modulation of C1-Inhibitor and Plasma Kallikrein Activities by Type IV Collagen
title_sort modulation of c1-inhibitor and plasma kallikrein activities by type iv collagen
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3296203/
https://www.ncbi.nlm.nih.gov/pubmed/22481936
http://dx.doi.org/10.1155/2012/212417
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