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1.

001-es BibID:BIBFORM062128
Első szerző:Biri Beáta (Budapest)
Cím:Metastasis-associated S100A4 is a specific amine donor and an activity-independent binding partner of transglutaminase-2 / Beáta Biri, Bence Kiss, Róbert Király, Gitta Schlosser, Orsolya Láng, László Kőhidai, László Fésüs, László Nyitray
Dátum:2016
ISSN:0264-6021
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal 473 : 1 (2016), p. 31-42. -
További szerzők:Kiss Bence Király Róbert (1975-) (biológus) Schlosser Gitta Láng Orsolya Kőhidai László Fésüs László (1947-) (orvos biokémikus) Nyitray László
Pályázati támogatás:TÁMOP 4.2.4. A/2-11-1-2012-0001
TÁMOP
OTKA K108437
OTKA
OTKA NK105046
OTKA
Internet cím:Szerző által megadott URL
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2.

001-es BibID:BIBFORM065146
Első szerző:Ergülen, Elvan
Cím:Identification of DNAJA1 as a novel interacting partner and substrate of human transglutaminase 2 / Elvan Ergülen, Bálint Bécsi, István Csomós, László Fésüs, Kajal Kanchan
Dátum:2016
ISSN:0264-6021
Megjegyzések:Transglutaminase 2 (TG2) is a ubiquitously expressed multi-functional member of the transglutaminase enzyme family. It has been implicated to have roles in many physiological and pathological processes such as differentiation, apoptosis, signal transduction, adhesion and migration, wound healing and inflammation. Previous studies revealed that TG2 has various intra- and extracellular interacting partners, which contribute to these processes. In this study, we identified a molecular co-chaperone, DNAJA1 as novel interacting partner of human TG2 using a GST pull down assay and subsequent mass spectrometry analysis and further confirmed this interaction via ELISA and SPR measurements. Interaction studies were also performed with domain variants of TG2 and results suggest that the catalytic core domain of TG2 is essential for the TG2-DNAJA1 interaction. Crosslinking activity was not essential for the interaction since DNAJA1 was also found to interact with the catalytically inactive form of TG2. Further, we have showed that DNAJA1 interacts with the open form of TG2 and regulates its transamidation activity both in vitro and in situ conditions. We also found that DNAJA1 is a glutamine donor substrate of TG2. Since DNAJA1 and TG2 are reported to regulate common pathological conditions such as neurodegenerative disorders and cancer, the findings in this paper open up possibilities to explore molecular mechanisms behind TG2 regulated functions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Transglutaminase 2
transamidation
DNAJA1/HSP40
core domain
protein-protein interaction
in situ crosslinking activity
GST pull down assay
surface plasmon resonance
Megjelenés:Biochemical Journal. - 473 : 21 (2016), p. 3889-3901. -
További szerzők:Bécsi Bálint (1981-) (vegyészmérnök) Csomós István (1983-) (molekuláris biológus) Fésüs László (1947-) (orvos biokémikus) Kanchan, Kajal
Pályázati támogatás:NK 105046
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM060631
Első szerző:Fésüs László (orvos biokémikus)
Cím:Formation of N epsilon-(gamma-glutamyl)-lysine isodipeptide in Chinese-hamster ovary cells / Laszlo Fésüs, Edit Tarcsa
Dátum:1989
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal 263 (1989), p. 843-848. -
További szerzők:Tarcsa Edit
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM049593
035-os BibID:PMID:23941696
Első szerző:Kanchan, Kajal
Cím:Identification of a specific one amino acid change in recombinant human transglutaminase 2 that regulates its activity and calcium sensitivity / Kajal Kanchan, Elvan Ergülen, Robert Király, Zsófia Simon-Vecsei, Mónika Fuxreiter, László Fésüs
Dátum:2013
ISSN:0264-6021
Megjegyzések:TG2 (transglutaminase 2) is a calcium-dependent protein cross-linking enzyme which is involved in a variety of cellular processes. The threshold level of calcium needed for endogenous and recombinant TG2 activity has been controversial, the former being more sensitive to calcium than the latter. In the present study we address this question by identifying a single amino acid change from conserved valine to glycine at position 224 in recombinant TG2 compared with the endogenous sequence present in the available genomic databases. Substituting a valine residue for Gly224 in the recombinant TG2 increased its calcium-binding affinity and transamidation activity 10-fold and isopeptidase activity severalfold, explaining the inactivity of widely used recombinant TG2 at physiological calcium concentrations. ITC (isothermal titration calorimetry) measurements showed 7-fold higher calcium-binding affinities for TG2 valine residues which could be activated inside cells. The two forms had comparable substrate- and GTP-binding affinities and also bound fibronectin similarly, but coeliac antibodies had a higher affinity for TG2 valine residues. Structural analysis indicated a higher stability for TG2 valine residues and a decrease in flexibility of the calcium-binding loop resulting in improved metal-binding affinity. The results of the present study suggest that Val224 increases TG2 activity by modulating its calcium-binding affinity enabling transamidation reactions inside cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal. - 455 : 3 (2013), p. 261-272. -
További szerzők:Ergülen, Elvan Király Róbert (1975-) (biológus) Simon-Vecsei Zsófia (1980-) (biológus) Fuxreiter Mónika (1969-) (kutató vegyész) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:NK 105046
OTKA
TÁMOP-4.2.2.A-11/1/KONV-2012-0023-"VÉD-ELEM"
TÁMOP
TRANSCOM IAPP 251506
FP7
TRANSPATH ITN 289964
FP7
TÁMOP-4.2.4.A/2-11-1-2012-0001
TÁMOP
LP2012-41
Egyéb
Lendület program
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5.

001-es BibID:BIBFORM060634
Első szerző:Piacentini, Mauro
Cím:Retinoic acid-induced modulation of rat liver transglutaminase and total polyamines in vivo / Mauro Piacentini, Laszlo Fesus, Claudia Sartori, Maria Paola Ceru
Dátum:1988
ISSN:0264-6021
Megjegyzések:The effect of a single intraperitoneal injection of retinoic acid on liver transglutaminase (EC 2.3.2.13) activity and total putrescine, spermidine and spermine was studied. The results demonstrate that: (1) transglutaminase activity is increased over control values as early as 4-6 h after treatment, reaching a maximum (2-fold increase) at 12 h and returning to control values at 36 h; (2) the retinoic acid-induced form of enzyme is the soluble tissue transglutaminase; (3) actinomycin D treatment does not completely inhibit the early (6 h) increase of activity, while suppressing that at 12 h; (4) the immunoassay of the soluble transglutaminase shows that, 6 h after treatment, there is no increase in the protein, whereas at 12 and 24 h a significant increase is observed; (5) putrescine, but not spermidine and spermine, increases (5-7-fold) 6 and 18 h after the retinoic acid treatment. The possibility also that the expression of soluble transglutaminase is modulated in vivo by retinoic acid and the relationship to polyamine levels are discussed.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical Journal 253 : 1 (1988), p. 33-38. -
További szerzők:Fésüs László (1947-) (orvos biokémikus) Sartori, Claudia Cerù, Maria Paola
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6.

001-es BibID:BIBFORM028766
Első szerző:Szondy Zsuzsanna (molekuláris sejtbiológus, biokémikus)
Cím:Inhibition of activation-induced apoptosis of thymocytes by all-trans- and 9-cis-retinoic acid is mediated via retinoic acid receptor alpha / Zsuzsa Szondy, Uwe Reichert, Jean-Michel Bernardon, Serge Michel, Réka Tóth, Éva Karászi, László Fésüs
Dátum:1998
ISSN:0264-6021
Megjegyzések:Thymocytes can be induced to undergo apoptotic cell death by activation through the T-cell receptor (TCR). This process requires macromolecular synthesis and has been shown to be inhibited by retinoic acids (RAs). Two groups of nuclear receptors for RAs have been identified: retinoic acid receptors (RARs) and retinoid X receptors (RXRs). All-trans-RA is the high-affinity ligand for RARs, and 9-cis-RA additionally binds to RXRs with high affinity. Because 9-cis-RA is much more potent in inhibiting TCR-mediated death than all-trans-RA, it was suggested that RXRs participate in the process. In the present study various synthetic retinoid analogues were used to address this question further. The results presented suggest that the inhibitory effect of RAs on activation-induced death of thymocytes is mediated via RARalpha, because (1) it can be reproduced by various RARalpha analogues both in vitro and in vivo, (2) the effect of RAs can be inhibited by the addition of an RARalpha antagonist, (3) CD4+CD8+thymocytes, which die on TCR stimulation, express RARalpha. Stimulation of RARgamma, in contrast, enhances the activation-induced death of thymocytes and inhibits its prevention by RARalpha stimulation. RXR co-stimulation suspends this inhibitory effect of RARgamma and permits the preventive function of RARalpha on activation-induced death. Our results suggest a complex interaction between the various isoforms of retinoid receptors and demonstrate that low (physiological) concentrations of all-trans-RA do not affect the activation-induced death of thymocytes because the RARalpha-mediated inhibitory and the RARgamma-mediated enhancing pathways are in balance, whereas if 9-cis-RA is formed, additional stimulation of RXRs permits the inhibitory action of RARalpha.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Biochemical Journal. - 331 : 3 (1998), p. 767-774. -
További szerzők:Reichert, Uwe Bernardon, Jean Michel Michel, Serge Révészné Tóth Réka (1969-) (molekuláris biológus, biokémikus) Karászi Éva Fésüs László (1947-) (orvos biokémikus)
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