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001-es BibID:BIBFORM028779
Első szerző:Fésüs László (orvos biokémikus)
Cím:Transglutaminase 2 in the balance of cell death and survival / László Fésüs, Zsuzsa Szondy
Dátum:2005
ISSN:0014-5793
Megjegyzések:Transglutaminase 2 (TG2), a multifunctional enzyme with Ca(2+)-dependent protein crosslinking activity and GTP-dependent G protein functions, is often upregulated in cells undergoing apoptosis. In cultured cells TG2 may exert both pro- and anti-apoptotic effects depending upon the type of cell, the kind of death stimuli, the intracellular localization of the enzyme and the type of its activities switched on. The majority of data support the notion that transamidation by TG2 can both facilitate and inhibit apoptosis, while the GTP-bound form of the enzyme generally protects cells against death. In vivo studies confirm the Janus face of TG2 in the initiation of the apoptotic program. In addition, they reveal a further role: the prevention of inflammation, tissue injury and autoimmunity once the apoptosis has already been initiated. This function of TG2 is partially achieved by being expressed and activated also in macrophages digesting apoptotic cells and mediating a crosstalk between dying and phagocytic cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:Febs Letters. - 579 : 15 (2005), p. 3297-3302. -
További szerzők:Szondy Zsuzsanna (1959-) (molekuláris sejtbiológus, biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:BIBFORM028734
Első szerző:Szondy Zsuzsanna (molekuláris sejtbiológus, biokémikus)
Cím:Differential expression of tissue transglutaminase during in vivo apoptosis of thymocytes induced via distinct signalling pathways / Zsuzsa Szondy, Peter Molnar, Zoltán Nemes, Michael Boyiadzis, Noémi Kedei, Réka Tóth, László Fésüs
Dátum:1997
ISSN:0014-5793
Megjegyzések:A significant increase in the expression and activity of tissue transglutaminase (tTG), one of the effector elements of apoptosis, was observed during involution of thymus elicited by treatment with either anti-CD3 antibody or dexamethasone or by irradiation. The blood plasma concentration of epsilon(gamma-glutamyl)lysine isodipeptide, the end-product of the digestion of transglutaminase cross-linked proteins, was also elevated in each of these cases. tTG was localized in cells of the cortical layer of the thymus and immunofluorescence double staining revealed that the enzyme appeared in the apoptotic cells. None of these observations could be made when apoptosis was induced by fas-receptor stimulation. The lack of tTG activity in fas-stimulated cells was accompanied with a less organized apoptotic morphology. Our data suggest that distinct signalling pathways, which induce apoptosis within the same cell type, can differentially regulate the expression of tTG, and this enzyme may be involved in structural stabilization of the apoptotic cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Febs Letters. - 404 : 2-3 (1997), p. 307-313. -
További szerzők:Molnár Péter Pál (1951-) (pathológus) Nemes Zoltán (1969-) (molekuláris biológus, pszichiáter) Boyiadzis, Michael Kedei Noémi Révészné Tóth Réka (1969-) (molekuláris biológus, biokémikus) Fésüs László (1947-) (orvos biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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