Autoactivation of human blood coagulation factor XII on dextran derivatives of different molecular weight

Tazi, Sanaa; Tans, Guido; Hemker, H.C.; Jm, Nigretto

doi:10.1016/0049-3848(92)90070-q

Cited by 11 publications

(7 citation statements)

References 9 publications

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“…Its essential role in in vitro blood clotting is much better understood. Extensive research has been performed on the type of surfaces and molecules that activate FXII in vitro, leading to initiation of the intrinsic coagulation pathway and the kallikreinkinin system (Griep et al, 1986;Tazi et al, 1992;Matata et al, 1996). The search for a physiological function of FXII has resulted in a number of possible roles, such as the induction of mitosis (Schmeidler-Sapiro et al, 1991;Gordon et al, 1996), angiogenesis (LaRusch et al, 2010), inflammation reactions (Jansen et al, 1996) and complement activation (Ghebrehiwet et al, 1981).…”

Section: Introductionmentioning

confidence: 99%

The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS

Beringer

Kroon-Batenburg

2013

Acta Cryst Sect F

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Coagulation factor XII (FXII) is a key protein in the intrinsic coagulation and kallikrein-kinin pathways. It has been found that negative surfaces and amyloids, such as A fibrils, can activate FXII. Additionally, it has been suggested that FXII simulates cells and that it plays an important role in thrombosis. To date, no structural data on FXII have been deposited, which makes it difficult to support any hypothesis on the mechanism of FXII function. The crystal structure of the FnI-EGF-like tandem domain of FXII presented here was solved using experimental phases. To determine the phases, a SIRAS approach was used with a native and a holmium chloride-soaked data set. The holmium cluster was coordinated by the C-terminal tails of two symmetryrelated molecules. Another observation was that the FnI domain was much more ordered than the EGF-like domain owing to crystal packing. Furthermore, the structure shows the same domain orientation as the homologous FnI-EGFlike tandem domain of tPA. The plausibility of several proposed interactions of these domains of FXII is discussed. Based on this FXII FnI-EGF-like structure, it could be possible that FXII binding to amyloid and negatively charged surfaces is mediated via this part of FXII.

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Section: Introductionmentioning

confidence: 99%

The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS

Beringer

Kroon-Batenburg

2013

Acta Cryst Sect F

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“…Recently, dextran sulphate derivatives of different molecular weight have been shown to induce, to a variable degree, autoactivation of FXII (Silverberg & Diehl, 1987;Tazi et al, 1992) or contact activation in human plasma (Corretge & Nigretto, 1990). To gain insight into the initial event of contact system activation we investigated the potency of dextran sulphates of different molecular weights to activate the contact system in plasma in relation to their capability to support FXII autoactivation or enhance FXII activation by kallikrein.…”

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confidence: 99%

Initiation of contact system activation in plasma is dependent on factor XII autoactivation and not on enhanced susceptibility of factor XII for kallikrein cleavage

et al. 1997

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Summary.Various mechanisms have been hypothesized to explain the initiation of contact system activation in plasma. We investigated the capability of dextran sulphate (DS) of different molecular weights to initiate contact system activation in normal human plasma, and compared this with their capability to support factor XII autoactivation and to enhance factor XII susceptibility for cleavage by kallikrein.Dextran sulphate of M r 500 000 (DS500) and 50 000 (DS50) was able to initiate contact system activation in plasma (determined by measuring the amount of factor XIIa-C1-inhibitor, kallikrein-C1-inhibitor and factor XIa-C1-inhibitor complexes generated) as well as to support factor XII autoactivation and to enhance factor XII susceptibility for cleavage by kallikrein (as measured with amidolytic assays using purified proteins). In contrast, dextran sulphate of M r 15 000 (DS15) and 5000 (DS5) neither induced contact system activation in plasma, nor supported autoactivation of factor XII, although both of these DS species enhanced the rate of activation of factor XII by kallikrein in the purified system. Based on these properties (i.e. binding of factor XII without inducing autoactivation), DS15 and DS5 were predicted to be inhibitors of contact system activation induced in plasma by DS500, which indeed was observed.We conclude that enhanced factor XII susceptibility for kallikrein activation and factor XII autoactivation are distinct phenomena, the latter being necessary to support activation of the contact system in plasma.

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“…Studies on the secondary structure of FXII/FXIIa using techniques such as circular dichroism, fluorescence spectroscopy and ultraviolet difference spectroscopy have been carried out in the past, but due to their low resolution they have been unable to provide detailed orientation information of the adsorbed proteins 128–130. In this case, SFG was able to show that the orientation of the secondary structures within FXII was affected by the degree of negative surface charge.…”

Section: Applications Of Sfg To the Study Of Bioadhesionmentioning

confidence: 99%

Sum Frequency Generation Studies on Bioadhesion: Elucidating the Molecular Structure of Proteins at Interfaces

Clair

Nguyen

Chen

2009

The Journal of Adhesion

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The study of bioadhesion is significant to applications in a variety of scientific fields. Techniques that are surface sensitive need to be utilized to examine these kinds of systems because bioadhesion occurs at the interface between two surfaces. Recently, Sum Frequency Generation (SFG) has been applied to investigate different bioadhesive processes because of its intrinsic surface specificity, excellent sensitivity and its ability to perform experiments in situ. SFG studies on the bioadhesion of fibrinogen, factor XII and mefp-3 on various surfaces will be discussed in this review.

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Autoactivation of human blood coagulation factor XII on dextran derivatives of different molecular weight

Cited by 11 publications

References 9 publications

The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS

The structure of the FnI-EGF-like tandem domain of coagulation factor XII solved using SIRAS

Initiation of contact system activation in plasma is dependent on factor XII autoactivation and not on enhanced susceptibility of factor XII for kallikrein cleavage

Sum Frequency Generation Studies on Bioadhesion: Elucidating the Molecular Structure of Proteins at Interfaces

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