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001-es BibID:	BIBFORM034731
Első szerző:	Bagoly Zsuzsa (orvos)
Cím:	Factor XIII, clot structure, thrombosis / Bagoly Zsuzsa, Koncz Zsuzsa, Hársfalvi Jolán, Muszbek László
Dátum:	2012
ISSN:	0049-3848
Megjegyzések:	Blood coagulation factor XIII (FXIII) is a tetrameric protein consisting of two catalytic A (FXIII-A) and two carrier/inhibitory B (FXIII-B) subunits. It is a zymogen, which becomes transformed into an active transglutaminase (FXIIIa) in the final phase of coagulation cascade by thrombin and Ca(2+). FXIII is essential for hemostasis, its deficiency results in severe bleeding diathesis. FXIIIa mechanically stabilizes fibrin by cross-linking its α-, and γ-chains. It also protects newly formed fibrin from fibrinolysis, primarily by cross-linking α(2)-plasmin inhibitor to fibrin. Beside the above prothrombotic effects, it is involved in limiting thrombus growth by down-regulating platelet adhesion to fibrin. Elevated FXIII level seems to be a gender-specific risk factor of both coronary artery disease and peripheral arterial disease, it represents an increased risk only in females. The association of FXIII level with the risk of ischemic stroke and venous thromboembolism was investigated only in a few studies from which no clear conclusion could be drawn. Among the FXIII subunit polymorphisms, concerning their effect on the risk of thrombotic diseases, only FXIII-A p.Val34Leu was investigated extensively. Meta-analyses of reported data suggest that this polymorphism provides a moderate protection against coronary artery disease and venous thromboembolism, but not against ischemic stroke. Gene-gene and gene-environmental interactions might modify its effect. Further studies are required to explore the effect of other FXIII subunit polymorphism on the risk of thrombotic diseases.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban atherothrombotic disease clot structure Molekuláris Medicina factor XIII factor XIII polymorphism fibrin venous thrombosis
Megjelenés:	Thrombosis Research. - 129 : 3 (2012), p. 382-387. -
További szerzők:	Koncz Zsuzsa (1983-) (orvos) Hársfalvi Jolán (1949-) (klinikai biokémikus) Muszbek László (1942-) (haematológus, kutató orvos)
Pályázati támogatás:	TÁMOP-4.2.1/B-09/1/KONV-2010-0007 TÁMOP A véralvadás XIII-as faktorának (FXIII) struktúrája, funkciója, előfordulása egyéb testnedvekben és kapcsolata trombotikus megbetegedésekkel TÁMOP-4.2.2/B-10/1-2010-0024 TÁMOP
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001-es BibID:	BIBFORM033201
Első szerző:	Mendelboum Raviv, Shlomit (biológus)
Cím:	4-thio-deoxyuridylate modified thrombin aptamer and its inhibitory effect on fibrin clot formation, platelet aggregation and thrombus growrth on subendothelial matrix / S. Mendelboum Raviv, A. Horváth, J. Aradi, Z. Bagoly, F. Fazakas, Z. Batta, L. Muszbek, J. Hársfalvi
Dátum:	2008
ISSN:	1538-7933
Megjegyzések:	Background:?The consensus thrombin aptamer C15-mer is a single-stranded DNA of 15 nucleotides [d(GGTTGGTGTGGTTGG)] that was identified by the selection of thrombin-binding molecules from a large combinatorial library of oligonucleotides. It is capable of inhibiting thrombin at nanomolar concentrations through binding to a specific region within thrombin exosite 1. As has been shown in our earlier studies, the 4-thio-deoxyuridylate (s4dU)-containing oligonucleotides have high affinity for a number of proteins, due to the reduced hydrophilic character of the modified oligonucleotide. Methods:?Three different analogs of the original thrombin-inhibiting sequence, in which some of the thymidylate residues were replaced by 4-thio-deoxyuridylates, were synthesized. The inhibitory effect of modified aptamers was tested on thrombin-catalyzed fibrin clot formation and fibrinopeptide A release from fibrinogen, thrombin-induced platelet aggregation/secretion, and the formation of thrombus on coverslips coated with human collagen type III, thrombin-treated fibrinogen or subendothelial matrix of human microvascular endothelial cells. Results:?As compared with the C15-mer, the analog with the sequence GG(s4dU)TGG(s4dU)G(s4dU)GGT(s4dU)GG (UC15-mer) showed a 2-fold increased inhibition of thrombin-catalyzed fibrin clot formation, fibrinopeptide A release, platelet aggregation and secretion in human plasma and thrombus formation on thrombin-treated fibrinogen surfaces under flow conditions. Concerning the inhibition of thrombin-induced fibrin formation from purified fibrinogen and activation of washed platelets, UC15-mer was 3-fold and twelve-fold more effective than C15-mer, respectively.Conclusion:?The replacement of four thymidylate residues in C15-mer by 4-thio-deoxyuridylate resulted in a new thrombin aptamer with increased anticoagulant and antithrombotic properties.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban 4-thio-deoxyuridylate aptamer platelets thrombin thrombin exosite thrombus
Megjelenés:	Journal Of Thrombosis And Haemostasis. - 6 : 10 (2008), p. 1764-1771. -
További szerzők:	Horváth András (1976-) (vegyész) Aradi János (1942-) (biokémikus, vegyész) Bagoly Zsuzsa (1978-) (orvos) Fazakas Ferenc (1969-) (molekuláris biológus) Batta Zoltán Muszbek László (1942-) (haematológus, kutató orvos) Hársfalvi Jolán (1949-) (klinikai biokémikus)
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