Nicola J. Mutch
University of Illinois at Urbana–Champaign
What is this?
Publications 17
#1Steven R. FraserH-Index: 5
#2Nuala A. BoothH-Index: 35
Last. Nicola J. MutchH-Index: 8
view all 3 authors...
Factor XIII (FXIII) generates fibrin-fibrin and fibrin-inhibitor cross-links. Our flow model, which is sensitive to cross-linking, was used to assess the effects of FXIII and the fibrinolytic inhibitor, 2antiplasmin (2AP) onfibrinolysis. Plasma model thrombi formed from FXIII or 2AP depleted plasma lysed at strikingly similar rates, 9-fold faster than pooled normal plasma (PNP). In contrast, no change was observed on depletion of PAI-1 or thrombin activatablefibrinolysis inhibitor (TAFI). Inhibi...
#1Claire S. WhyteH-Index: 6
#2Irina N. Chernysh (UPenn: University of Pennsylvania)H-Index: 8
Last. Nicola J. MutchH-Index: 8
view all 7 authors...
Polyphosphate (polyP) binds to fibrin(ogen) and alters fibrin structure, generating a heterogeneous network composed of ‘knots’ interspersed by large pores. Here we show platelet-derived polyP elicits similar structural changes in fibrin and examine the mechanism by which polyP alters fibrin structure. Polymerisation of fibrinogen with thrombin and CaCl2 was studied using spinning disk confocal (SDC) microscopy. PolyP delayed fibrin polymerisation generating shorter protofibrils emanating from a...
6 CitationsSource
#1Nicola J. MutchH-Index: 8
#2Ruchira EngelH-Index: 3
Last. Helen PhilippouH-Index: 27
view all 4 authors...
Activated platelets secrete a negatively charged polymer, polyphosphate (polyP). Here, we explore the interactions of polyP with fibrin(ogen) and its effect on fibrin structure andfibrinolysis. Electrophoretic mobility and binding assays indicate that polyP interacts with fibrinogen and soluble fibrin. Clots formed in the presence of polyP exhibited reduced turbidity and permeability indicative of a tighter fibrin network, but these changes were not related to cross-linking or fibrinopeptide rel...
#1Joanne L. MitchellH-Index: 4
Last. Nicola J. MutchH-Index: 8
view all 6 authors...
#1Peter AllanH-Index: 3
#2Sumitra MohanH-Index: 1
Last. Julian I. BorissoffH-Index: 11
view all 9 authors...
#1Joke Konings (UM: Maastricht University)H-Index: 7
#2José W. P. Govers-Riemslag (UM: Maastricht University)H-Index: 24
Last. Robert A. S. Ariëns (University of Leeds)H-Index: 41
view all 10 authors...
Recent data indicate an important contribution of coagulation factor (F)XII to in vivo thrombus formation. Because fibrin structure plays a key role in clot stability and thrombosis, we hypothesized that FXII(a) interacts with fibrin(ogen) and thereby regulates clot structure and function. In plasma and purified system, we observed a dose-dependent increase in fibrin fiber density and decrease in turbidity, reflecting a denser structure, and a nonlinear increase in clot stiffness with FXIIa. In ...
86 CitationsSource
#1Felicitas Mueller (KI: Karolinska Institutet)
#2Nicola J. MutchH-Index: 8
Last. Thomas Renné (KI: Karolinska Institutet)H-Index: 41
view all 10 authors...
#1Nicola J. Mutch (University of Leeds)H-Index: 8
#2J S Koikkalainen (Aberd.: University of Aberdeen)H-Index: 1
Last. Nuala A. Booth (Aberd.: University of Aberdeen)H-Index: 35
view all 8 authors...
Background: Activated factor XIII (FXIIIa), a transglutaminase, introduces fibrin-fibrin and fibrin-inhibitor cross-links, resulting in more mechanically stable clots. The impact of cross-linking on resistance to fibrinolysis has proved challenging to evaluate quantitatively. Methods: We used a whole blood model thrombus system to characterize the role of cross-linking in resistance to fibrinolytic degradation. Model thrombi, which mimic arterial thrombi formed in vivo, were prepared with incorp...
43 CitationsSource
#1K M BaetenH-Index: 1
#2M C Richard (Aberd.: University of Aberdeen)H-Index: 1
Last. Nuala A. BoothH-Index: 35
view all 6 authors...
Summary. Background and Objective: Platelets are essential for hemostasis, and they cause resistance to fibrinolysis by tissue-type plasminogen activator. In contrast, platelets enhance fibrinolysis mediated by single-chain urokinase-type plasminogen activator (scu-PA). This study investigated the mechanism behind this profibrinolytic role of platelets. Methods and Results: Platelets enhanced scu-PA activity, but not urokinase-type plasminogen activator (u-PA) activity, in plasma clot lysis and ...
15 CitationsSource