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001-es BibID:BIBFORM054369
Első szerző:Asijee, Guus M.
Cím:Platelet vinculin : a substrate of activated factor XIII / Guus M. Asijee, Lászlo Muszbek, János Kappelmayer, János Polgár, Andrea Horváth, Auguste Sturk
Dátum:1988
ISSN:0167-4838
Megjegyzések:In addition to plasma, Factor XIII of blood coagulation (FXIII) is also present in the cytosol of platelets, monocytes and macrophages. However, its intracellular function has not yet been revealed. Activated Factor XIII (FXIIIa) is a transglutaminase (protein-glutamine: amine γ-glutamyltransferase, EC 2.3.2.13) of highly restricted substrate specificity with only a few known protein substrates. In this report, we showed that FXIIIa can link dansylcadaverine, radiolabelled histamine and putrescine to vinculin. Quantitative determinations revealed that in the vinculin molecule a single glutamine residue can serve as acyl donor for the incorporation of small-molecular-weight amines. Vinculin could not be crosslinked to another vinculin molecule. It could be covalently bound, however, to fibrinogen, which indicates that the acyl donor glutamine residue can be engaged in an ?-(γ-glutamyl)lysyl crosslink formation. Since it has been shown that platelet actin and myosin, two main components of cytoskeleton, are also substrates for FXIIIa, and that vinculin is associated to the cytoskeleton during platelet activation, the involvement of FXIII in the stabilization of cytoskeleton at certain phases of cellular function is a likely possibility.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Vinculin
Cytoskeleton
Factor XIII
Transglutaminase
Protein-glutamin
γ-glutamyltransferase
Megjelenés:Biochimica et Biophysica Acta (BBA). Protein Structure and Molecular Enzymology. - 954 (1988), p. 303-308. -
További szerzők:Muszbek László (1942-) (haematológus, kutató orvos) Kappelmayer János (1960-) (laboratóriumi szakorvos) Polgár János Horváth Andrea Sturk, Auguste
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2.

001-es BibID:BIBFORM060642
Első szerző:Muszbek László (haematológus, kutató orvos)
Cím:Kinetic determination of blood coagulation Factor XIII in plasma / László Muszbek, János Polgár, László Fésüs
Dátum:1985
Megjegyzések:We have designed a new kinetic assay for estimating Factor XIII in plasma. Plasma fibrinogen is removed by treatment with bentonite (colloidal aluminum silicate) before measurement. During the lag phase, Factor XIII is transformed by thrombin and Ca2+ into active transglutaminase (EC 2.3.2.13), which attaches the substrate ethylamine to a glutamine residue in acetylated, dephosphorylated beta-casein. During the reaction, ammonia is released, which can be continuously monitored in an NADPH-dependent indicator reaction catalyzed by glutamate dehydrogenase (EC 1.4.1.4). We determined the optimal concentrations of substrate and activator and found that, to eliminate the clottable fibrinogen from the plasma samples, bentonite treatment was more advantageous than the traditional heat treatment. Results by the method correlate well with those by the most widely used amine incorporation and immunoinhibition assays for Factor XIII. We established a reference interval of 12.1-22.7 U/L; at optimal conditions, the variance of the method was less than 3% within this range. The method has several theoretical and practical advantages over traditional determinations of Factor XIII.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Clinical Chemistry 31 : 1 (1985), p. 35-40. -
További szerzők:Polgár János Fésüs László (1947-) (orvos biokémikus)
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3.

001-es BibID:BIBFORM041414
035-os BibID:PMID:2859670
Első szerző:Muszbek László (haematológus, kutató orvos)
Cím:Factor XIII of blood coagulation in human monocytes / L. Muszbek, R. Adany, Gy. Szegedi, J. Polgar, M. Kavai
Dátum:1985
Megjegyzések:The presence of Factor XIII subunit a was demonstrated in human monocytes by immunoperoxidase staining using specific antisera against Factor XIII and its subunits. This finding was verified by immunobiochemical techniques, as well. In an immunoblotting system after SDS polyacrylamide gel electrophoresis of denatured monocyte homogenate a protein band comigrating with Factor XIII subunit a showed positive reaction with antibodies against this subunit or whole Factor XIII. In contrast, no subunit b of Factor XIII could be detected by either of these methods in monocytes. Activity measurements were carried out by the dansylcadaverine incorporation assay in the absence and presence of anti-Factor XIII antibody with and without thrombin activation. The expression of transglutaminase activity required thrombin and was completely abolished in presence of anti- Factor XIII antibody, which clearly indicate that practically all the transglutaminase activity measured in monocytes comes from Factor XIII. Factor XIII of monocytes and macrophages might have a role in formation of focal fibrin thrombi as well as in organization of stable, fibrinolysis resistant fibrin clot at the site of inflammation or around tumor cells.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Factor XIII
monocytes
transglutaminase activity
immunoblotting
egyetemen (Magyarországon) készült közlemény
Megjelenés:Thrombosis Research. - 37 : 3 (1985), p. 401-410. -
További szerzők:Szegedi Gyula (1936-2013) (belgyógyász, immunológus) Polgár János Kávai Mária (1930-) (vegyész) Ádány Róza (1952-) (megelőző orvostan és népegészségtan szakorvos)
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4.

001-es BibID:BIBFORM036496
Első szerző:Muszbek László (haematológus, kutató orvos)
Cím:Platelet factor XIII becomes active without the release of activation peptide during platelet activation / László Muszbek, János Polgár, Zoltán Boda
Dátum:1993
ISSN:0340-6245
Megjegyzések:The potentially active A subunit of factor XIII of blood coagulation has also been detected in platelets and monocytes/macrophages through the exact function of this cellular protransglutaminase has not yet been elucidated. In physiological conditions the first step in the activation of plasma factor XIII is the removal of an activation peptide from the N-terminal end of subunit A by thrombin. The A subunit then, in the presence of Ca2+, dissociates from the inhibitory B subunit and assumes an active conformation. Cellular factor XIII, which lacks B subunit, can be proteolytically activated in vitro by thrombin and the intracellular Ca2+ sensitive protease, calpain, in the same way as plasma factor XIII subunit A, and calpain has been suggested as the intracellular protease involved in the activation of cellular factor XIII in platelets. In the present experiments it was shown by SDS PAGE that during long-term stimulation of platelets with thrombin nondisulfide-crosslinked high M(r) protein polymers not penetrating the concentrating gel were formed. The lack of these polymers in thrombin-stimulated factor XIII deficient platelets clearly indicated that their formation in normal platelets was due to factor XIII that became active during platelet activation. However, no release of the activation peptide could be detected by Western blotting during this process. Similarly, no proteolytic cleavage of factor XIII was detectable when platelets were stimulated by Ca2+ ionophore through this stimulus activated calpain as it was clearly demonstrated by the breakdown of major intracellular calpain substrate
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Thrombosis And Haemostasis. - 69 : 3 (1993), p. 282-285. -
További szerzők:Polgár János Boda Zoltán (1947-) (belgyógyász, haematologus, klinikai onkológus)
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5.

001-es BibID:BIBFORM085948
Első szerző:Polgár János
Cím:Thrombomodulin inhibits the activation of factor xiii by thrombin / Polgár J., Léránt I., Muszbek L., Machovich R.
Dátum:1986
ISSN:0049-3848
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Thrombosis Research. - 43 : 5 (1986), p. 585-590. -
További szerzők:Léránt I. Muszbek László (1942-) (haematológus, kutató orvos) Machovich, Raymund
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6.

001-es BibID:BIBFORM084145
Első szerző:Polgár János
Cím:Non-proteolytic activation of cellular protransglutaminase (placenta macrophage factor XIII) / Polgár J., Hidasi V., Muszbek L.
Dátum:1990
ISSN:0264-6021 1470-8728
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biochemical Journal. - 267 : 2 (1990), p. 557-560. -
További szerzők:Hidasi Vanda Muszbek László (1942-) (haematológus, kutató orvos)
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