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001-es BibID:	BIBFORM034624
Első szerző:	Balogh István (molekuláris biológus, genetikus)
Cím:	Val34Leu polymorphism of plasma factor XIII : biochemistry and epidemiology in familial thrombophilia / István Balogh, Gabriella Szőke, Levente Kárpáti, Ulla Wartiovaara, Éva Katona, István Komáromi, Gizella Haramura, György Pfliegler, Hanna Mikkola, László Muszbek
Dátum:	2000
ISSN:	0006-4971
Megjegyzések:	Val34Leu polymorphism of the A subunit of coagulation factor XIII (FXIII-A) is located in the activation peptide (AP) just 3 amino acids away from the thrombin cleavage site. This mutation has been associated with a protective effect against occlusive arterial diseases and venous thrombosis; however, its biochemical consequences have not been explored. In the current study it was demonstrated that the intracellular stability and the plasma concentration of FXIII of different Val34Leu genotypes are identical, which suggests that there is no difference in the rate of synthesis and externalization of wild-type and mutant FXIII-A. In contrast, the release of AP by thrombin from the Leu34 allele proceeded significantly faster than from its wild-type Val34 counterpart. By molecular modeling larger interaction energy was calculated between the Leu34 variant and the respective domains of thrombin than between the Val34 variant and thrombin. In agreement with these findings, the activation of mutant plasma FXIII by thrombin was faster and required less thrombin than that of the wild-type variant. Full thrombin activation of purified plasma FXIII of different genotypes, however, resulted in identical specific transglutaminase activities. Similarly, the mean specific FXIII activity in the plasma was the same in the groups with wild-type, heterozygous, and homozygous variants. Faster activation of the Leu34 allele hardly could be associated with its presumed protective effect against venous thrombosis. No such protective effect was observed in a large group of patients with familial thrombophilia.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Blood. - 96 : 7 (2000), p. 2479-2486. -
További szerzők:	Szőke Gabriella Kárpáti Levente (1968-) (okleveles vegyész) Wartiovaara, Ulla Katona Éva (1961-) (klinikai biokémikus) Komáromi István (1957-) (vegyész, molekuláris biológus, biokémikus) Haramura Gizella (1957-) (vezető analitikus) Pfliegler György (1949-) (belgyógyász, hematológus, labor szakorvos) Mikkola, Hanna Muszbek László (1942-) (haematológus, kutató orvos)
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001-es BibID:	BIBFORM084005
Első szerző:	Mikkola, Hanna
Cím:	Molecular Mechanism of a Mild Phenotype in Coagulation Factor XIII (FXIII) Deficiency : a Splicing Mutation Permitting Partial Correct Splicing of FXIII A-Subunit mRNA / Mikkola Hanna, Muszbek Laszlo, Laiho Elina, Syrjälä Martti, Hämäläinen Eija, Haramura Gizella, Salmi Toivo, Peltonen Leena, Palotie Aarno
Dátum:	1997
ISSN:	0006-4971
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Blood. - 89 : 4 (1997), p. 1279-1287. -
További szerzők:	Muszbek László (1942-) (haematológus, kutató orvos) Laiho, Elina Syrjälä, Martti Hämäläinen, Eija Haramura Gizella (1957-) (vezető analitikus) Salmi, Toivo Peltonen, Leena Palotie, Aarno
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001-es BibID:	BIBFORM041610
035-os BibID:	PMID:8922891
Első szerző:	Muszbek László (haematológus, kutató orvos)
Cím:	Novel aspects of blood coagulation factor XIII. I. Structure, distribution, activation, and function / László Muszbek, Róza Ádány, Hanna Mikkola
Dátum:	1996
Megjegyzések:	Blood coagulation factor XIII (FXIII) is a protransglutaminase that becomes activated by the concerted action of thrombin and Ca2+ in the final stage of the clotting cascade. In addition to plasma, FXIII also occurs in platelets, monocytes, and monocyte-derived macrophages. While the plasma factor is a heterotetramer consisting of paired A and B subunits (A2B2), its cellular counterpart lacks the B subunits and is a homodimer of potentially active A subunits (A2). The gene coding for the A and B subunits has been localized to chromosomes 6p24-25 and 1q31-32.1, respectively. The genomic as well as the primary protein structure of both subunits has been established, and most recently the three-dimensional structure of recombinant cellular FXIII has also been revealed. Monocytes/macrophages synthesize their own FXIII, and very likely FXIII in platelets is synthesized by the megakaryocytes. Cells of bone marrow origin seem to be the primary site for the synthesis of subunit A in plasma FXIII, but hepatocytes might also contribute. The B subunit of plasma FXIII is synthesized in the liver. Plasma FXIII circulates in association with its substrate precursor, fibrinogen. Fibrin(ogen) has an important regulatory role in the activation of plasma FXIII. The most important steps of the activation of plasma FXIII are the proteolytic removal of activation peptide by thrombin, the dissociation of subunits A and B, and the exposure of the originally buried active site on the free A subunits. The end result of this process is the formation of an active transglutaminase, which cross-links peptide chains through epsilon(gamma-glutamyl)lysyl isopeptide bonds. Cellular FXIII in platelets becomes activated through a nonproteolytic process. When intracytoplasmic Ca2+ is raised during platelet activation, the zymogen--in the absence of subunit B--assumes an active configuration. The protein substrates of activated FXIII include components of the clotting-fibrinolytic system, adhesive and contractile proteins. The main physiological function of plasma FXIII is to cross-link fibrin and protect it from the fibrinolytic plasmin. The latter effect is achieved mainly by covalently linking alpha 2 antiplasmin, the most potent physiological inhibitor of plasmin, to fibrin. Plasma FXIII seems to be involved in wound healing and tissue repair, and it is essential to maintaining pregnancy. Cellular FXIII, if exposed to the surface of the cells, might support or perhaps take over the hemostatic functions of plasma FXIII; however, its intracellular role has remained mostly unexplored.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban factor XIII transglutaminase platelets monocytes macrophages calcium thrombin fibrinolysis fibrinogen fibrin alpha2 antiplasmin fibronectin wound healing pregnancy egyetemen (Magyarországon) készült közlemény
Megjelenés:	Critical Reviews in Clinical Laboratory Sciences. - 33 : 5 (1996), p. 357-421. -
További szerzők:	Mikkola, Hanna Ádány Róza (1952-) (megelőző orvostan és népegészségtan szakorvos)
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001-es BibID:	BIBFORM058217
Első szerző:	Wartiovaara, Ulla
Cím:	Effect of Val34Leu polymorphism on the activation of the coagulation factor XIII-A / U. Wartiovaara, H. Mikkola, G. Szőke, G. Haramura, L. Kárpáti, I. Balogh, R. Lassila, L. Muszbek, A. Palotie
Dátum:	2000
ISSN:	0340-6245
Megjegyzések:	Coagulation factor XIII (FXIII) is a protransglutaminase involved in the last step of the coagulation cascade by stabilising the fibrin clot. Recently, a common variation (FXIII Val34Leu) has been associated with a decreased risk of myocardial infarction and deep venous thrombosis. Val34Leu is critically located near the thrombin activation site of FXIII-A. In this study we investigated its effects on the activation of FXIII. Both recombinant and platelet-derived FXIII Val34Leu variants were shown to be more susceptible to thrombin cleavage than the wild type FXIII. The rate of enzymatic activation of FXIII Val34Leu was found increased, however, the specific activity of fully activated wild type FXIII and the Val34Leu mutant did not differ. During the course of thrombin-induced activation of FXIII fibrin gamma-chain dimerisation and alpha-chain polymerisation developed more rapidly with the Val34Leu mutant. The increased rate of fibrin stabilisation brought about by the Val34Leu FXIII seems to be paradoxically associated with a protective effect against pathological thrombosis.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Factor XIII Factor XII Val34Leu thrombin peptide
Megjelenés:	Thrombosis and Haemostasis. - 84 : 4 (2000), p. 595-600. -
További szerzők:	Mikkola, Hanna Szőke Gabriella Haramura Gizella (1957-) (vezető analitikus) Kárpáti L. Balogh István (1972-) (molekuláris biológus, genetikus) Lassila, Riitta Muszbek László (1942-) (haematológus, kutató orvos) Palotie, Aarno
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