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1.
001-es BibID:
BIBFORM060771
Első szerző:
Fésüs László (orvos biokémikus)
Cím:
Apoptosis : molecular mechanisms in programmed cell death / L. Fésüs, P. J. A. Davies, M. Piacentini
Dátum:
1991
Tárgyszavak:
Orvostudományok
Elméleti orvostudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:
European Journal of Cell Biology 56 : 2 (1991), p. 170-177. -
További szerzők:
Davies, Peter J. A.
Piacentini, Mauro
Borító:
Saját polcon:
2.
001-es BibID:
BIBFORM060767
Első szerző:
Nemes Z.
Cím:
Expression and activation of tissue transglutaminase in apoptotic cells of involuting rodent mammary tissue / Z. Nemes, R. R. Friis, D. Aeschlimann, S. Saurer, M. Paulsson, L. Fésüs
Dátum:
1996
ISSN:
0171-9335
Megjegyzések:
Apoptosis is a form of cell death in which cellular integrity is maintained and neither cytoplasmic nor nuclear content is released. The Ca(2+)-dependent tissue transglutaminase (tTG) is an enzyme that forms protein cross-links between specific glutamyl and lysyl side-chains of intra- and extracellular proteins, therefore it may be responsible for the structural stabilization observed during the death process. In this study, the expression of tTG was investigated following the physiological process of forced weaning which results in an almost complete elimination of secretory epithelium by apoptosis and remodelling of the tissue structure. A dramatic induction of tTG was detected by immunoblotting of total mammary gland homogenates prepared from the involuting glands. The concentration of epsilon(gamma-glutamyl)-lysine crosslinks was also elevated in these samples, showing that the enzyme is activated during apoptosis. To determine the distribution of tTG and its relationship to apoptotic cells, paraffin-embedded specimens were studied by RNA in situ hybridization and immunohistochemical methods as well as using in situ labeling for nuclear fragmentation. All of these approaches indicated that mammary secretory epithelium expressed tissue transglutaminase coincident with the onset of apoptosis. The apoptotic and tTG-expressing cells were found to be identical as demonstrated by a histological double-labeling technique.
Tárgyszavak:
Orvostudományok
Elméleti orvostudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:
European Journal of Cell Biology 70 : 2 (1996), p. 125-133. -
További szerzők:
Friis, Bob R. R.
Aeschlimann, Daniel
Saurer, S.
Paulsson, M.
Fésüs László (1947-) (orvos biokémikus)
Borító:
Saját polcon:
3.
001-es BibID:
BIBFORM060772
Első szerző:
Piacentini, Mauro
Cím:
The expression of "tissue" transglutaminase in two human cancer cell lines is related with the programmed cell death (apoptosis) / M. Piacentini, L. Fésüs, M. G. Farrace, L. Ghibelli, G. Melino
Dátum:
1991
ISSN:
0171-9335
Megjegyzések:
The expression of "tissue" transglutaminase (tTG) in two human tumor cell lines (the cervix adenocarcinoma line HeLa-TV and the neuroblastoma cells SK-N-BE-2) was found to be in correlation with the rate of physiological cell death (apoptosis) in culture. We investigated the effect of retinoic acid (RA) and alpha-difluoromethylornithine (DFMO) in order to elucidate the relationship between tTG expression and apoptosis. RA led to a 6-fold increase of tTG activity in HeLa-TV cells and to a 12-fold increase in SK-N-BE(2) cells, which was paralleled in both cell lines by a proportional increase in the number of apoptotic bodies recovered from the cultures. On the contrary, DFMO determined a dramatic reduction of tTG expression and of the apoptotic index. Immunohistochemical analysis using an anti-tTG antibody showed that the enzyme was accumulated in both cell lines within typical apoptotic bodies. Immunocytochemistry and cell cloning of SK-N-BE(2) line demonstrated that tTG was absent in cells showing neurite outgrowth, indicating that the enzyme expression is not associated with neural differentiation, even though both phenomena are elicited by retinoic acid. On the whole, these data indicate that also in tumors tTG activation takes place in cells undergoing apoptosis. The enzyme is activated in apoptotic cells to form cross-linked protein envelopes which are insoluble in detergents and chaotropic agents. The number of insoluble protein envelopes as well as the N,N-bis(gamma-glutamyl)polyamine cross-links is related with both tTG expression and apoptotic index, strongly suggesting the participation of the enzyme in the apoptotic program.
Tárgyszavak:
Orvostudományok
Elméleti orvostudományok
idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:
European Journal of Cell Biology 54 : 2 (1991), p. 246-254. -
További szerzők:
Fésüs László (1947-) (orvos biokémikus)
Farrace, Maria Grazia
Ghibelli, L.
Melino, Gerry
Borító:
Saját polcon:
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