Research ExplorerPublicationsThe plasma contact system, a protease cascade at the nexus o...

The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity

Standard

The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity. / Weidmann, Henri; Heikaus, Laura; Long, Andy T; Naudin, Clément; Schlüter, Hartmut; Renné, Thomas.

In: BBA-MOL CELL RES, Vol. 1864, No. 11 Pt B, 11.2017, p. 2118-2127.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Weidmann, H, Heikaus, L, Long, AT, Naudin, C, Schlüter, H & Renné, T 2017, 'The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity', BBA-MOL CELL RES, vol. 1864, no. 11 Pt B, pp. 2118-2127. https://doi.org/10.1016/j.bbamcr.2017.07.009

APA

Weidmann, H., Heikaus, L., Long, A. T., Naudin, C., Schlüter, H., & Renné, T. (2017). The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity. BBA-MOL CELL RES, 1864(11 Pt B), 2118-2127. https://doi.org/10.1016/j.bbamcr.2017.07.009

Vancouver

Weidmann H, Heikaus L, Long AT, Naudin C, Schlüter H, Renné T. The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity. BBA-MOL CELL RES. 2017 Nov;1864(11 Pt B):2118-2127. https://doi.org/10.1016/j.bbamcr.2017.07.009

Bibtex

@article{11e983b2434343f1b5db2a6daeaafca1,
title = "The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity",
abstract = "The contact system is a potent procoagulant and proinflammatory plasma protease cascade that is initiated by binding ({"}contact{"})-induced, auto-activation of factor XII zymogen. Formed active serine protease FXIIa then cleaves plasma prekallikrein to kallikrein that in turn liberates the mediator bradykinin from its precursor high molecular weight kininogen. Bradykinin induces inflammation with implications for host defense and innate immunity. FXIIa also triggers the intrinsic pathway of coagulation that has been shown to critically contribute to thrombosis. Vice versa, FXII deficiency impairs thrombosis in animal models without inducing abnormal excessive bleeding. Recent work has established the FXIIa-driven contact system as promising target for anticoagulant and anti-inflammatory drugs. This review focuses on the biochemistry of the contact system, its regulation by endogenous and exogenous inhibitors, and roles in disease states. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.",
keywords = "Journal Article, Review",
author = "Henri Weidmann and Laura Heikaus and Long, {Andy T} and Cl{\'e}ment Naudin and Hartmut Schl{\"u}ter and Thomas Renn{\'e}",
note = "Copyright {\textcopyright} 2017. Published by Elsevier B.V.",
year = "2017",
month = nov,
doi = "10.1016/j.bbamcr.2017.07.009",
language = "English",
volume = "1864",
pages = "2118--2127",
journal = "BBA-MOL CELL RES",
issn = "0167-4889",
publisher = "Elsevier",
number = "11 Pt B",

}

RIS

TY - JOUR

T1 - The plasma contact system, a protease cascade at the nexus of inflammation, coagulation and immunity

AU - Weidmann, Henri

AU - Heikaus, Laura

AU - Long, Andy T

AU - Naudin, Clément

AU - Schlüter, Hartmut

AU - Renné, Thomas

N1 - Copyright © 2017. Published by Elsevier B.V.

PY - 2017/11

Y1 - 2017/11

N2 - The contact system is a potent procoagulant and proinflammatory plasma protease cascade that is initiated by binding ("contact")-induced, auto-activation of factor XII zymogen. Formed active serine protease FXIIa then cleaves plasma prekallikrein to kallikrein that in turn liberates the mediator bradykinin from its precursor high molecular weight kininogen. Bradykinin induces inflammation with implications for host defense and innate immunity. FXIIa also triggers the intrinsic pathway of coagulation that has been shown to critically contribute to thrombosis. Vice versa, FXII deficiency impairs thrombosis in animal models without inducing abnormal excessive bleeding. Recent work has established the FXIIa-driven contact system as promising target for anticoagulant and anti-inflammatory drugs. This review focuses on the biochemistry of the contact system, its regulation by endogenous and exogenous inhibitors, and roles in disease states. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.

AB - The contact system is a potent procoagulant and proinflammatory plasma protease cascade that is initiated by binding ("contact")-induced, auto-activation of factor XII zymogen. Formed active serine protease FXIIa then cleaves plasma prekallikrein to kallikrein that in turn liberates the mediator bradykinin from its precursor high molecular weight kininogen. Bradykinin induces inflammation with implications for host defense and innate immunity. FXIIa also triggers the intrinsic pathway of coagulation that has been shown to critically contribute to thrombosis. Vice versa, FXII deficiency impairs thrombosis in animal models without inducing abnormal excessive bleeding. Recent work has established the FXIIa-driven contact system as promising target for anticoagulant and anti-inflammatory drugs. This review focuses on the biochemistry of the contact system, its regulation by endogenous and exogenous inhibitors, and roles in disease states. This article is part of a Special Issue entitled: Proteolysis as a Regulatory Event in Pathophysiology edited by Stefan Rose-John.

KW - Journal Article

KW - Review

U2 - 10.1016/j.bbamcr.2017.07.009

DO - 10.1016/j.bbamcr.2017.07.009

M3 - SCORING: Journal article

C2 - 28743596

VL - 1864

SP - 2118

EP - 2127

JO - BBA-MOL CELL RES

JF - BBA-MOL CELL RES

SN - 0167-4889

IS - 11 Pt B

ER -