Coagulation Factor XIIIa Substrates in Human Plasma. Identification and Incorporation Into the Clot

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Standard

Coagulation Factor XIIIa Substrates in Human Plasma. Identification and Incorporation Into the Clot. / Nikolajsen, Camilla Lund; Dyrlund, Thomas Franck; Toftgaard Poulsen, Ebbe; Enghild, Jan J; Scavenius, Carsten.

In: Journal of Biological Chemistry, Vol. 289, 07.03.2014, p. 6526-6534.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

APA

CBE

MLA

Vancouver

Author

Nikolajsen, Camilla Lund ; Dyrlund, Thomas Franck ; Toftgaard Poulsen, Ebbe ; Enghild, Jan J ; Scavenius, Carsten. / Coagulation Factor XIIIa Substrates in Human Plasma. Identification and Incorporation Into the Clot. In: Journal of Biological Chemistry. 2014 ; Vol. 289. pp. 6526-6534.

Bibtex

@article{7003581134ba4dbf97c5fb03a6a0b2cf,
title = "Coagulation Factor XIIIa Substrates in Human Plasma. Identification and Incorporation Into the Clot",
abstract = "Coagulation factor XIIIa (FXIIIa) is a transglutaminase with a well-defined role in the final stages of blood coagulation. The active enzyme catalyzes the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific Gln and Lys residues. The primary physiological outcome of this catalytic activity is stabilization of the fibrin clot during coagulation. The stabilization is achieved through the introduction of cross-links between fibrin monomers and through cross-linking of proteins with anti-fibrinolytic activity to fibrin. FXIIIa additionally cross-links several proteins with other functionalities to the clot. Cross-linking of proteins to the clot is generally believed to modify clot characteristics such as proteolytic susceptibility and hereby affect the outcome of tissue damage. In the present study, we use a proteomic approach in combination with transglutaminase-specific labeling to identify FXIIIa plasma protein substrates and their reactive residues. The results revealed a total of 147 FXIIIa substrates of which 132 have not previously been described. We confirm that 48 of the FXIIIa substrates were indeed incorporated into the insoluble fibrin clot during the coagulation of plasma. The identified substrates are involved in among others complement activation, coagulation, inflammatory and immune responses and extracellular matrix organization.",
author = "Nikolajsen, {Camilla Lund} and Dyrlund, {Thomas Franck} and {Toftgaard Poulsen}, Ebbe and Enghild, {Jan J} and Carsten Scavenius",
year = "2014",
month = mar,
day = "7",
doi = "10.1074/jbc.M113.517904",
language = "English",
volume = "289",
pages = "6526--6534",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

}

RIS

TY - JOUR

T1 - Coagulation Factor XIIIa Substrates in Human Plasma. Identification and Incorporation Into the Clot

AU - Nikolajsen, Camilla Lund

AU - Dyrlund, Thomas Franck

AU - Toftgaard Poulsen, Ebbe

AU - Enghild, Jan J

AU - Scavenius, Carsten

PY - 2014/3/7

Y1 - 2014/3/7

N2 - Coagulation factor XIIIa (FXIIIa) is a transglutaminase with a well-defined role in the final stages of blood coagulation. The active enzyme catalyzes the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific Gln and Lys residues. The primary physiological outcome of this catalytic activity is stabilization of the fibrin clot during coagulation. The stabilization is achieved through the introduction of cross-links between fibrin monomers and through cross-linking of proteins with anti-fibrinolytic activity to fibrin. FXIIIa additionally cross-links several proteins with other functionalities to the clot. Cross-linking of proteins to the clot is generally believed to modify clot characteristics such as proteolytic susceptibility and hereby affect the outcome of tissue damage. In the present study, we use a proteomic approach in combination with transglutaminase-specific labeling to identify FXIIIa plasma protein substrates and their reactive residues. The results revealed a total of 147 FXIIIa substrates of which 132 have not previously been described. We confirm that 48 of the FXIIIa substrates were indeed incorporated into the insoluble fibrin clot during the coagulation of plasma. The identified substrates are involved in among others complement activation, coagulation, inflammatory and immune responses and extracellular matrix organization.

AB - Coagulation factor XIIIa (FXIIIa) is a transglutaminase with a well-defined role in the final stages of blood coagulation. The active enzyme catalyzes the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific Gln and Lys residues. The primary physiological outcome of this catalytic activity is stabilization of the fibrin clot during coagulation. The stabilization is achieved through the introduction of cross-links between fibrin monomers and through cross-linking of proteins with anti-fibrinolytic activity to fibrin. FXIIIa additionally cross-links several proteins with other functionalities to the clot. Cross-linking of proteins to the clot is generally believed to modify clot characteristics such as proteolytic susceptibility and hereby affect the outcome of tissue damage. In the present study, we use a proteomic approach in combination with transglutaminase-specific labeling to identify FXIIIa plasma protein substrates and their reactive residues. The results revealed a total of 147 FXIIIa substrates of which 132 have not previously been described. We confirm that 48 of the FXIIIa substrates were indeed incorporated into the insoluble fibrin clot during the coagulation of plasma. The identified substrates are involved in among others complement activation, coagulation, inflammatory and immune responses and extracellular matrix organization.

U2 - 10.1074/jbc.M113.517904

DO - 10.1074/jbc.M113.517904

M3 - Journal article

C2 - 24443567

VL - 289

SP - 6526

EP - 6534

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -