Találati lista | Tudóstér

001-es BibID:	BIBFORM092840
035-os BibID:	(cikkazonosító)347 (WoS)000633434800001 (Scopus)85101254453
Első szerző:	Bagoly Zsuzsa (orvos)
Cím:	Incorporation of [alfa]2-Plasmin Inhibitor into Fibrin Clots and Its Association with the Clinical Outcome of Acute Ischemic Stroke Patients / Bagoly Zsuzsa, Baráth Barbara, Orbán-Kálmándi Rita, Szegedi István, Bogáti Réka, Sarkady Ferenc, Csiba László, Katona Éva
Dátum:	2021
ISSN:	2218-273X
Megjegyzések:	Cross-linking of ?2-plasmin inhibitor (?2-PI) to fibrin by activated factor XIII (FXIIIa) is essential for the inhibition of fibrinolysis. Little is known about the factors modifying ?2-PI incorporation into the fibrin clot and whether the extent of incorporation has clinical consequences. Herein we calculated the extent of ?2-PI incorporation by measuring ?2-PI antigen levels from plasma and serum obtained after clotting the plasma by thrombin and Ca2+. The modifying effect of FXIII was studied by spiking of FXIII-A-deficient plasma with purified plasma FXIII. Fibrinogen, FXIII, ?2-PI incorporation, in vitro clot-lysis, soluble fibroblast activation protein and ?2-PI p.Arg6Trp polymorphism were measured from samples of 57 acute ischemic stroke patients obtained before thrombolysis and of 26 healthy controls. Increasing FXIII levels even at levels above the upper limit of normal increased ?2-PI incorporation into the fibrin clot. ?2-PI incorporation of controls and patients with good outcomes did not differ significantly (49.4 ? 4.6% vs. 47.4 ? 6.7%, p = 1.000), however it was significantly lower in patients suffering post-lysis intracranial hemorrhage (37.3 ? 14.0%, p = 0.004). In conclusion, increased FXIII levels resulted in elevated incorporation of ?2-PI into fibrin clots. In stroke patients undergoing intravenous thrombolysis treatment, ?2-PI incorporation shows an association with the outcome of therapy, particularly with thrombolysis-associated intracranial hemorrhage.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Biomolecules. - 11 : 3 (2021), p. 1-13. -
További szerzők:	Baráth Barbara (1991-) (orvosírnok) Orbán-Kálmándi Rita Angéla (1993-) (klinikai laboratóriumi kutató) Szegedi István (1992-) (orvos) Kissné Bogáti Réka (1988-) (tudományos segédmunkatárs) Sarkady Ferenc (1982-) (laboratóriumi analitikus) Csiba László (1952-) (neurológus, pszichiáter) Katona Éva (1961-) (klinikai biokémikus)
Pályázati támogatás:	GINOP-2.2.1-15-2017-00043 GINOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM093898
035-os BibID:	(cikkazonosító)544 (WoS)000642809000001 (Scopus)85103814901
Első szerző:	Gindele Réka (molekuláris biológus)
Cím:	Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods / Gindele Réka, Pénzes-Daku Krisztina, Balogh Gábor, Kállai Judit, Bogáti Réka, Bécsi Bálint, Erdődi Ferenc, Katona Éva, Bereczky Zsuzsanna
Dátum:	2021
ISSN:	2218-273X
Megjegyzések:	Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin. Mutations at the heparin-binding region lead to functional defect, type II heparin-binding site (IIHBS) AT deficiency. The aim of this study was to investigate and compare the molecular background of AT Budapest 3 (p.Leu131Phe, ATBp3), AT Basel (p.Pro73Leu), and AT Padua (p.Arg79His) mutations. Advanced in silico methods and heparin-binding studies of recombinant AT proteins using surface plasmon resonance method were used. Crossed immunoelectrophoresis and Differential Scanning Fluorimetry (NanoDSF) were performed in plasma samples. Heparin affinity of AT Padua was the lowest (KD = 1.08 x 10(-6) M) and had the most severe consequences affecting the allosteric pathways of activation, moreover significant destabilizing effects on AT were also observed. KD values for AT Basel, ATBp3 and wild-type AT were 7.64 x 10(-7) M, 2.15 x 10(-8) M and 6.4 x 10(-10) M, respectively. Heparin-binding of AT Basel was slower, however once the complex was formed the mutation had only minor effect on the secondary and tertiary structures. Allosteric activation of ATBp3 was altered, moreover decreased thermostability in ATBp3 homozygous plasma and increased fluctuations in multiple regions of ATBp3 were observed by in silico methods suggesting the presence of a quantitative component in the pathogenicity of this mutation due to molecular instability.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Biomolecules. - 11 : 4 (2021), p. 1-18. -
További szerzők:	Pénzes-Daku Krisztina (1978-) (biológus) Balogh Gábor (1991-) (gyógyszerész) Kállai Judit (1983-) (molekuláris biológus) Kissné Bogáti Réka (1988-) (tudományos segédmunkatárs) Bécsi Bálint (1981-) (vegyészmérnök) Erdődi Ferenc (1953-) (biokémikus) Katona Éva (1961-) (klinikai biokémikus) Bereczky Zsuzsanna (1974-) (orvosi laboratóriumi diagnosztika szakorvos)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00039 GINOP GINOP-2.3.2-15-2016-00044 GINOP GINOP-2.3.3-15-2016-00020 GINOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: