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Factor XII Contact Activation

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Factor XII Contact Activation. / Naudin, Clément; Burillo, Elena; Blankenberg, Stefan; Butler, Lynn; Renné, Thomas.

In: SEMIN THROMB HEMOST, Vol. 43, No. 8, 11.2017, p. 814-826.

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

Harvard

Naudin, C, Burillo, E, Blankenberg, S, Butler, L & Renné, T 2017, 'Factor XII Contact Activation', SEMIN THROMB HEMOST, vol. 43, no. 8, pp. 814-826. https://doi.org/10.1055/s-0036-1598003

APA

Naudin, C., Burillo, E., Blankenberg, S., Butler, L., & Renné, T. (2017). Factor XII Contact Activation. SEMIN THROMB HEMOST, 43(8), 814-826. https://doi.org/10.1055/s-0036-1598003

Vancouver

Naudin C, Burillo E, Blankenberg S, Butler L, Renné T. Factor XII Contact Activation. SEMIN THROMB HEMOST. 2017 Nov;43(8):814-826. https://doi.org/10.1055/s-0036-1598003

Bibtex

@article{f1cac4138608401bb04b351178a4fcf9,
title = "Factor XII Contact Activation",
abstract = "Contact activation is the surface-induced conversion of factor XII (FXII) zymogen to the serine protease FXIIa. Blood-circulating FXII binds to negatively charged surfaces and this contact to surfaces triggers a conformational change in the zymogen inducing autoactivation. Several surfaces that have the capacity for initiating FXII contact activation have been identified, including misfolded protein aggregates, collagen, nucleic acids, and platelet and microbial polyphosphate. Activated FXII initiates the proinflammatory kallikrein-kinin system and the intrinsic coagulation pathway, leading to formation of bradykinin and thrombin, respectively. FXII contact activation is well characterized in vitro and provides the mechanistic basis for the diagnostic clotting assay, activated partial thromboplastin time. However, only in the past decade has the critical role of FXII contact activation in pathological thrombosis been appreciated. While defective FXII contact activation provides thromboprotection, excess activation underlies the swelling disorder hereditary angioedema type III. This review provides an overview of the molecular basis of FXII contact activation and FXII contact activation-associated disease states.",
keywords = "Journal Article",
author = "Cl{\'e}ment Naudin and Elena Burillo and Stefan Blankenberg and Lynn Butler and Thomas Renn{\'e}",
note = "Thieme Medical Publishers 333 Seventh Avenue, New York, NY 10001, USA.",
year = "2017",
month = nov,
doi = "10.1055/s-0036-1598003",
language = "English",
volume = "43",
pages = "814--826",
journal = "SEMIN THROMB HEMOST",
issn = "0094-6176",
publisher = "Thieme Medical Publishers",
number = "8",

}

RIS

TY - JOUR

T1 - Factor XII Contact Activation

AU - Naudin, Clément

AU - Burillo, Elena

AU - Blankenberg, Stefan

AU - Butler, Lynn

AU - Renné, Thomas

N1 - Thieme Medical Publishers 333 Seventh Avenue, New York, NY 10001, USA.

PY - 2017/11

Y1 - 2017/11

N2 - Contact activation is the surface-induced conversion of factor XII (FXII) zymogen to the serine protease FXIIa. Blood-circulating FXII binds to negatively charged surfaces and this contact to surfaces triggers a conformational change in the zymogen inducing autoactivation. Several surfaces that have the capacity for initiating FXII contact activation have been identified, including misfolded protein aggregates, collagen, nucleic acids, and platelet and microbial polyphosphate. Activated FXII initiates the proinflammatory kallikrein-kinin system and the intrinsic coagulation pathway, leading to formation of bradykinin and thrombin, respectively. FXII contact activation is well characterized in vitro and provides the mechanistic basis for the diagnostic clotting assay, activated partial thromboplastin time. However, only in the past decade has the critical role of FXII contact activation in pathological thrombosis been appreciated. While defective FXII contact activation provides thromboprotection, excess activation underlies the swelling disorder hereditary angioedema type III. This review provides an overview of the molecular basis of FXII contact activation and FXII contact activation-associated disease states.

AB - Contact activation is the surface-induced conversion of factor XII (FXII) zymogen to the serine protease FXIIa. Blood-circulating FXII binds to negatively charged surfaces and this contact to surfaces triggers a conformational change in the zymogen inducing autoactivation. Several surfaces that have the capacity for initiating FXII contact activation have been identified, including misfolded protein aggregates, collagen, nucleic acids, and platelet and microbial polyphosphate. Activated FXII initiates the proinflammatory kallikrein-kinin system and the intrinsic coagulation pathway, leading to formation of bradykinin and thrombin, respectively. FXII contact activation is well characterized in vitro and provides the mechanistic basis for the diagnostic clotting assay, activated partial thromboplastin time. However, only in the past decade has the critical role of FXII contact activation in pathological thrombosis been appreciated. While defective FXII contact activation provides thromboprotection, excess activation underlies the swelling disorder hereditary angioedema type III. This review provides an overview of the molecular basis of FXII contact activation and FXII contact activation-associated disease states.

KW - Journal Article

U2 - 10.1055/s-0036-1598003

DO - 10.1055/s-0036-1598003

M3 - SCORING: Journal article

C2 - 28346966

VL - 43

SP - 814

EP - 826

JO - SEMIN THROMB HEMOST

JF - SEMIN THROMB HEMOST

SN - 0094-6176

IS - 8

ER -