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1.

001-es BibID:BIBFORM006026
Első szerző:Basu, Hirak S.
Cím:Effect of polyamine depletion on chromatin structure in U-87 MG human brain tumour cells / Basu, H. S., Sturkenboom, M. C., Delcros, J. G., Csokan, P. P., Szollosi, J., Feuerstein, B. G., Marton, L. J.
Dátum:1992
Megjegyzések:The chromatin structure of polyamine-depleted U-87 MG human brain tumour cells was studied by following the kinetics of digestion of cell nuclei by micrococcal nuclease and bovine pancreatic DNAase I. Cells growing in monolayers were treated with either alpha-difluoromethylornithine (DFMO), to deplete putrescine and spermidine, or N1,N14-bis(ethyl)homospermine (BE-4-4-4), to deplete putrescine, spermidine and spermine. BE-4-4-4 increased the initial rates of digestion and the magnitudes of limit digest by both enzymes; DFMO increased the limit digests without affecting initial digestion rates. Addition of 1 mM-putrescine 1 day after addition of DFMO reversed the effect of DFMO on limit digests. (Because polyamine uptake is low in cells treated with BE-4-4-4, and because putrescine does not reverse the growth-inhibitory effects of BE-4-4-4, reversal of the effects of BE-4-4-4 with putrescine was not attempted.) The increases in initial rates and limit digests did not result from changes in the lengths of nucleosomal or linker DNA, from blocks in cell-cycle progression, or from growth inhibition caused by DFMO or BE-4-4-4. Thus, because the limit digest is highest in cells with the lowest polyamine levels, it seems clear that the enhanced enzymic digestion of nuclei is caused by polyamine depletion and its possible effect on chromatin structure.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
analogs and derivatives
Brain Neoplasms
Cell Cycle
Cell Nucleus
Chromatin
Culture Media
Culture Media,Serum-Free
Deoxyribonuclease I
Dna
drug effects
Eflornithine
Enzymes
Human
Intracellular Fluid
Kinetics
metabolism
Micrococcal Nuclease
pathology
pharmacology
Polyamines
Putrescine
Spermidine
Spermine
Support,Non-U.S.Gov't
Support,U.S.Gov't,P.H.S.
Tumor Cells,Cultured
ultrastructure
Megjelenés:The Biochemical Journal. - 282 : Pt 3 (1992), p. 723-727. -
További szerzők:Sturkenboom, M. C. Delcros, J. G. Csokan, P. P. Szöllősi János (1953-) (biofizikus) Feuerstein, Burt G. Marton, Laurence J.
Internet cím:elektronikus változat
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2.

001-es BibID:BIBFORM006032
Első szerző:Delcros, J. G.
Cím:Differential effects of spermine and its analogues on the structures of polynucleotides complexed with ethidium bromide / Delcros J. G., Sturkenboom M. C., Basu, H. S., Shafer R. H., Szöllösi, J., Feuerstein, B. G., Marton, L. J.
Dátum:1993
Megjegyzések:The interactions of spermine and polyamine analogues with synthetic polynucleotides of various base sequences complexed with ethidium bromide (EB) were investigated using measurements of fluorescence intensity and steady-state fluorescence polarization. Spermine and polyamine analogues displaced some but not all of the EB bound to poly(dA-dT).poly(dA-dT) or poly(dG-dC).poly(dG-dC), suggesting that polyamines may stabilize these polynucleotides in a conformation with reduced affinity for EB. Modifications of the aliphatic backbone of spermine have pronounced effects on its ability to displace EB from poly(dA-dT).poly(dA-dT) but not from poly-(dG-dC).poly(dG-dC). Spermine and some but not all of the polyamine analogues caused fluorescence depolarization when they interacted with the complex of EB and poly(dA-dT).poly-(dA-dT). Neither spermine nor any of the analogues, however, induced fluorescence depolarization in the complex of EB with poly(dG-dC).poly(dG-dC) or poly(dA).poly(dT). This suggests that spermine and some spermine analogues induce structural changes specific to alternating A-T sequences.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
chemistry
Ethidium
Fluorescence
Fluorescence Polarization
Nucleic Acid Conformation
pharmacology
Poly dA-dT
Polyamines
Polydeoxyribonucleotides
Polynucleotides
Spectrometry,Fluorescence
Spermine
Support,Non-U.S.Gov't
Support,U.S.Gov't,P.H.S.
Megjelenés:The Biochemical Journal. - 291 : Pt 1 (1993), p. 269-274. -
További szerzők:Sturkenboom, M. C. Basu, Hirak S. Shafer, R. H. Szöllősi János (1953-) (biofizikus) Feuerstein, Burt G. Marton, Laurence J.
Internet cím:elektronikus változat
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3.

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
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DOI
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