Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces

Sandra Konrath; Reiner K Mailer; Thomas Renné

doi:10.1055/a-1528-0499

Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces

Standard

Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces. / Konrath, Sandra ; Mailer, Reiner K ; Renné, Thomas.

In: HAMOSTASEOLOGIE, Vol. 41, No. 6, 12.2021, p. 489-501.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Konrath, S , Mailer, RK & Renné, T 2021, 'Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces', HAMOSTASEOLOGIE, vol. 41, no. 6, pp. 489-501. https://doi.org/10.1055/a-1528-0499

APA

Konrath, S., Mailer, R. K., & Renné, T. (2021). Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces. HAMOSTASEOLOGIE, 41(6), 489-501. https://doi.org/10.1055/a-1528-0499

Vancouver

Konrath S , Mailer RK , Renné T. Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces. HAMOSTASEOLOGIE. 2021 Dec;41(6):489-501. https://doi.org/10.1055/a-1528-0499

Bibtex

@article{973178d9e21b45eeb6387bcc9c7e41e2,

title = "Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces",

abstract = "Factor XII (FXII) is a serine protease zymogen produced by hepatocytes and secreted into plasma. The highly glycosylated coagulation protein consists of six domains and a proline-rich region that regulate activation and function. Activation of FXII results from a conformational change induced by binding ({"}contact{"}) with negatively charged surfaces. The activated serine protease FXIIa drives both the proinflammatory kallikrein-kinin pathway and the procoagulant intrinsic coagulation cascade, respectively. Deficiency in FXII is associated with a prolonged activated partial thromboplastin time (aPTT) but not with an increased bleeding tendency. However, genetic or pharmacological deficiency impairs both arterial and venous thrombosis in experimental models. This review summarizes current knowledge of FXII structure, mechanisms of FXII contact activation, and the importance of FXII for diagnostic coagulation testing and thrombosis.",

author = "Sandra Konrath and Mailer, {Reiner K} and Thomas Renn{\'e}",

year = "2021",

month = dec,

doi = "10.1055/a-1528-0499",

language = "English",

volume = "41",

pages = "489--501",

journal = "HAMOSTASEOLOGIE",

issn = "0720-9355",

publisher = "Schattauer",

number = "6",

}

RIS

TY - JOUR

T1 - Mechanism, Functions, and Diagnostic Relevance of FXII Activation by Foreign Surfaces

AU - Konrath, Sandra

AU - Mailer, Reiner K

AU - Renné, Thomas

PY - 2021/12

Y1 - 2021/12

N2 - Factor XII (FXII) is a serine protease zymogen produced by hepatocytes and secreted into plasma. The highly glycosylated coagulation protein consists of six domains and a proline-rich region that regulate activation and function. Activation of FXII results from a conformational change induced by binding ("contact") with negatively charged surfaces. The activated serine protease FXIIa drives both the proinflammatory kallikrein-kinin pathway and the procoagulant intrinsic coagulation cascade, respectively. Deficiency in FXII is associated with a prolonged activated partial thromboplastin time (aPTT) but not with an increased bleeding tendency. However, genetic or pharmacological deficiency impairs both arterial and venous thrombosis in experimental models. This review summarizes current knowledge of FXII structure, mechanisms of FXII contact activation, and the importance of FXII for diagnostic coagulation testing and thrombosis.

AB - Factor XII (FXII) is a serine protease zymogen produced by hepatocytes and secreted into plasma. The highly glycosylated coagulation protein consists of six domains and a proline-rich region that regulate activation and function. Activation of FXII results from a conformational change induced by binding ("contact") with negatively charged surfaces. The activated serine protease FXIIa drives both the proinflammatory kallikrein-kinin pathway and the procoagulant intrinsic coagulation cascade, respectively. Deficiency in FXII is associated with a prolonged activated partial thromboplastin time (aPTT) but not with an increased bleeding tendency. However, genetic or pharmacological deficiency impairs both arterial and venous thrombosis in experimental models. This review summarizes current knowledge of FXII structure, mechanisms of FXII contact activation, and the importance of FXII for diagnostic coagulation testing and thrombosis.

U2 - 10.1055/a-1528-0499

DO - 10.1055/a-1528-0499

M3 - SCORING: Review article

C2 - 34592776

VL - 41

SP - 489

EP - 501

JO - HAMOSTASEOLOGIE

JF - HAMOSTASEOLOGIE

SN - 0720-9355

IS - 6

ER -