CCL

Összesen 3 találat.
#/oldal:
Részletezés:
Rendezés:

1.

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
Borító:

2.

001-es BibID:BIBFORM060510
Első szerző:Kanchan, Kajal
Cím:Physiological, pathological, and structural implications of nonenzymatic protein-protein interactions of the multifunctional human transglutaminase 2 / Kajal Kanchan, Mónika Fuxreiter, László Fésüs
Dátum:2015
ISSN:1420-682X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cellular And Molecular Life Sciences. - 72 : 16 (2015), p. 3009-3035. -
További szerzők:Fuxreiter Mónika (1969-) (kutató vegyész) Fésüs László (1947-) (orvos biokémikus)
Pályázati támogatás:TAMOP-4.2.2.A-11/1/KONV-2012-0023 "VÉDELEM"
TÁMOP
OTKA-NK105046
OTKA
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

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
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Rekordok letöltése1