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001-es BibID:	BIBFORM010272
Első szerző:	Silva, Gabriella
Cím:	Oxidized hemoglobin is an endogenous proinflammatory agonist that targets vascular endothelial cells / Gabriella Silva, Viktoria Jeney, Angelo Chora, Rasmus Larsen, Jozsef Balla, Miguel P. Soares
Dátum:	2009
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	The Journal of Biological Chemistry. - 284 : 43 (2009), p. 29582-29595. -
További szerzők:	Jeney Viktória (1971-) (vegyész, kémia tanár) Chora, Angelo Larsen, Rasmus Balla József (1959-) (belgyógyász, nephrológus) Soares, Miguel P.
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM094508
035-os BibID:	(WoS)000470656500020 (Scopus)85066156398
Első szerző:	Szakács Dávid
Cím:	Novel MASP-2 inhibitors developed via directed evolution of human TFPI1 are potent lectin pathway inhibitors / Dávid Szakács, Andrea Kocsis, Róbert Szász, Péter Gál, Gábor Pál
Dátum:	2019
ISSN:	0021-9258 1083-351X
Megjegyzések:	The lectin pathway (LP) of the complement system is an important antimicrobial defense mechanism, but it also contributes significantly to ischemia reperfusion injury (IRI) associated with myocardial infarct, stroke, and several other clinical conditions. Mannan-binding lectin-associated serine proteinase 2 (MASP-2) is essential for LP activation, and therefore, it is a potential drug target. We have previously developed the first two generations of MASP-2 inhibitors by in vitro evolution of two unrelated canonical serine proteinase inhibitors. These inhibitors were selective LP inhibitors, but their nonhuman origin rendered them suboptimal lead molecules for drug development. Here, we present our third-generation MASP-2 inhibitors that were developed based on a human inhibitor scaffold. We subjected the second Kunitz domain of human tissue factor pathway inhibitor 1 (TFPI1 D2) to directed evolution using phage display to yield inhibitors against human and rat MASP-2. These novel TFPI1-based MASP-2 inhibitor (TFMI-2) variants are potent and selective LP inhibitors in both human and rat serum. Directed evolution of the first Kunitz domain of TFPI1 had already yielded the potent kallikrein inhibitor, Kalbitor? (ecallantide), which is an FDA-approved drug to treat acute attacks of hereditary angioedema. Like hereditary angioedema, acute IRI is also related to the uncontrolled activation of a specific plasma serine proteinase. Therefore, TFMI-2 variants are promising lead molecules for drug development against IRI.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk MASP TFPI1 MASP-2 inhibitor
Megjelenés:	Journal Of Biological Chemistry. - 294 : 20 (2019), p. 8227-8237. -
További szerzők:	Kocsis Andrea Szász Róbert (1972-) (belgyógyász, haematológus) Gál Péter Pál Gábor
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001-es BibID:	BIBFORM005097
Első szerző:	Szatmári István (biológus)
Cím:	Peroxisome proliferator-activated receptor gamma-regulated ABCG2 expression confers cytoprotection to human dendritic cells / Szatmari, I., Vamosi, G., Brazda, P., Balint, B. L., Benko, S., Szeles, L., Jeney, V., Ozvegy-Laczka, C., Szanto, A., Barta, E., Balla, J., Sarkadi, B., Nagy, L.
Dátum:	2006
ISSN:	021-9258 (Print)
Megjegyzések:	ABCG2, a member of the ATP-binding cassette transporters has been identified as a protective pump against endogenous and exogenous toxic agents. ABCG2 was shown to be expressed at high levels in stem cells and variably regulated during cell differentiation. Here we demonstrate that functional ABCG2 is expressed in human monocyte-derived dendritic cells by the activation of a nuclear hormone receptor, PPARgamma. We identified and characterized a 150-base pair long conserved enhancer region, containing three functional PPAR response elements (PPARE), upstream of the human ABCG2 gene. We confirmed the binding of the PPARgamma x RXR heterodimer to this enhancer region, suggesting that PPARgamma directly regulates the transcription of ABCG2. Consistent with these results, elevated expression of ABCG2 mRNA was coupled to enhanced protein production, resulting in increased xenobiotic extrusion capacity via ABCG2 in PPARgamma-activated cells. Furthermore PPARgamma instructed dendritic cells showed increased Hoechst dye extrusion and resistance to mitoxantrone. Collectively, these results uncovered a mechanism by which up-regulation of functional ABCG2 expression can be achieved via exogenous or endogenous activation of the lipid-activated transcription factor, PPARgamma. The increased expression of the promiscuous ABCG2 transporter can significantly modify the xenobiotic and drug resistance of human myeloid dendritic cells.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban agonists Animals antagonists & inhibitors ATP-Binding Cassette Transporters Base Sequence biosynthesis Cattle Cell Differentiation Cells cytology Cytoprotection Dendritic Cells Dogs Drug Resistance Drug Resistance,Neoplasm genetics Human Humans Hungary metabolism Mice Molecular Sequence Data Neoplasm Proteins Phenotype physiology PPAR gamma Proteins Research Support Up-Regulation Xenobiotics
Megjelenés:	The Journal of Biological Chemistry. - 281 : 33 (2006), p. 23812-23823. -
További szerzők:	Vámosi György (1967-) (biofizikus) Brázda Péter (1980-) (biológus, angol-magyar szakfordító) Bálint Bálint László (1971-) (kutató orvos) Benkő Szilvia (1973-) (molekuláris biológus) Széles Lajos (1971-) (molekuláris biológus) Jeney Viktória (1971-) (vegyész, kémia tanár) Özvegy-Laczka Csilla Szántó Attila (1976-) (orvos, biokémikus) Barta Endre (1963-) (molekuláris biológus) Balla József (1959-) (belgyógyász, nephrológus) Sarkadi Balázs Nagy László (1966-) (molekuláris sejtbiológus, biokémikus)
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