Enzymes produced by autoactivation of blood factor XII in buffer

Golas, Avantika; Pitakjakpipop, Harit; Rahn, Matthew S.; Siedlecki, Christopher A.; Vogler, Erwin A.

doi:10.1016/j.biomaterials.2014.09.015

Cited by 8 publications

(3 citation statements)

References 40 publications

(44 reference statements)

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“…Nor is surface negative charge a prerequisite for activation. 24 The serine protease inhibitor (serpin) antithrombin (AT) binds specifically to activated FXIIa, but not to the zymogen FXII and can therefore be used to detect the formation of FXIIa after its adsorption to foreign surfaces.…”

Section: Introductionmentioning

confidence: 99%

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

et al. 2017

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In previous investigations, the authors have examined the adsorption of albumin, immunoglobulin, and fibrinogen to a series of acrylate polymers with different backbone and side-group flexibility. The authors showed that protein adsorption to acrylates with high flexibility, such as poly(lauryl methacrylate) (PLMA), tends to preserve native conformation. In the present study, the authors have continued this work by examining the conformational changes that occur during the binding of complement factor 3 (C3) and coagulation factor XII (FXII). Native C3 adsorbed readily to all solid surfaces tested, including a series of acrylate surfaces of varying backbone flexibility. However, a monoclonal antibody recognizing a “hidden” epitope of C3 (only exposed during C3 activation or denaturation) bound to the C3 on the rigid acrylate surfaces or on polystyrene (also rigid), but not to C3 on the flexible PLMA, indicating that varying degrees of conformational change had occurred with binding to different surfaces. Similarly, FXII was activated only on the rigid poly(butyl methacrylate) surface, as assessed by the formation of FXIIa-antithrombin (AT) complexes; in contrast, it remained in its native form on the flexible PLMA surface. The authors also found that water wettability hysteresis, defined as the difference between the advancing and receding contact angles, was highest for the PLMA surface, indicating that a dynamic change in the interface polymer structure may help protect the adsorbed protein from conformational changes and denaturation.

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Section: Introductionmentioning

confidence: 99%

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

et al. 2017

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“…35 In this study, we show that this suite of activation products also includes molecules that can inhibit αFXIIa activity. In 2015, Golas et al 43 showed electrophoresis bands for FXII activated by three different surface chemistries. In these gel images, 99% of all FXII was seen as a single band at molecular weight of 80 kDa, corresponding to the molecular weight of fully intact FXII.…”

Section: αFxiia Activity Suppression Of Fxiia By Activator Surfacesmentioning

confidence: 99%

FXII contact activation products have an inhibitory effect on αFXIIa

Xu,

Siedlecki

2023

J Biomedical Materials Res

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It is accepted that the contact activation complex of the intrinsic pathway of blood coagulation cascade produces active enzymes that lead to plasma coagulation following biomaterial contact. In this study, FXII was activated through contact with hydrophilic glass beads and hydrophobic octadecyltrichlorosilane‐modified glass beads from neat buffer solutions. These FXII contact activation products generated from material interaction were found to suppress the procoagulant activity of exogenous αFXIIa, and this inhibition was dependent on surface wettability and the concentration of exogenous αFXIIa. Higher relative inhibition rates were generally observed at low concentrations of αFXIIa (1–2 μg/mL) while both hydrophobic and hydrophilic materials showed similar inhibition levels (~39%) at high concentrations of αFXIIa (20 μg/mL). The presence of prekallikrein in the activation system increased the amount of FXIIa produced during FXII contact activation, and also suppressed the apparent levels of inhibitors on hydrophilic surfaces, while having no effect on apparent levels of inhibitors on hydrophobic surface. The combination of FXII contact activation products and activator surfaces was found to dramatically increase inhibition of αFXIIa activity compared to the activation products alone, regardless of activator surface wettability and the presence of prekallikrein. This finding of inhibitors in the suite of proteins generated by contact activation provides additional knowledge into the complex series of interactions that occur when plasma comes into contact with material surfaces.

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“…However, it is recognized that negatively charged surfaces can promote the contact activation of FXII [ 243 ]. For example, glass can activate coagulation [ 244 ]. Negatively charged heparin can also promote the activation of FXII [ 245 ].…”

Section: Introductionmentioning

confidence: 99%

Advances in Enhancing Hemocompatibility of Hemodialysis Hollow-Fiber Membranes

et al. 2023

Adv. Fiber Mater.

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Enzymes produced by autoactivation of blood factor XII in buffer

Cited by 8 publications

References 40 publications

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

FXII contact activation products have an inhibitory effect on αFXIIa

Advances in Enhancing Hemocompatibility of Hemodialysis Hollow-Fiber Membranes

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