Další formáty:
BibTeX
LaTeX
RIS
@inproceedings{788656,
author = {Ondroušková, Eva and Slováčková, Jana and Pelková, Vendula and Procházková, Jiřina and Souček, Karel and Beneš, Petr and Šmarda, Jan},
address = {Brno},
booktitle = {XIX. Biologické dny. Biologický výzkum pro lidské zdraví},
keywords = {Bcl-2; heavy metals; Jun N-terminal kinase; phosphorylation; posttranslational modification},
language = {eng},
location = {Brno},
isbn = {978-80-7399-545-4},
pages = {74-75},
publisher = {Československá biologická společnost a LF Univerzity Karlovy v Hradci Králové},
title = {Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase},
year = {2008}
}
TY - JOUR
ID - 788656
AU - Ondroušková, Eva - Slováčková, Jana - Pelková, Vendula - Procházková, Jiřina - Souček, Karel - Beneš, Petr - Šmarda, Jan
PY - 2008
TI - Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase
PB - Československá biologická společnost a LF Univerzity Karlovy v Hradci Králové
CY - Brno
SN - 9788073995454
KW - Bcl-2
KW - heavy metals
KW - Jun N-terminal kinase
KW - phosphorylation
KW - posttranslational modification
N2 - The Bcl-2 protein is one of the key components of biochemical pathways controling programmed cell death. Function of this protein can be regulated by posttranslational modifications. Phosphorylation of Bcl-2 has been considered to be significantly associated with cell cycle arrest in the G2/M phase of the cell cycle, and with cell death caused by defects of microtubule dynamics. In this study, we show that heavy metal-induced stress and cell death correlate with induction of the Bcl-2 protein phosphorylation in several cell lines. Zinc-induced phosphorylation of Bcl-2 is mediated by the Jun N-terminal kinase pathway, and it is not linked to cell cycle arrest at G2/M. Cells of breast carcinoma cell line MDA-MB-231 expressing the wild-type Bcl-2 protein are more resistant to zinc-induced cell death than those expressing mutant variant of Bcl-2 that cannot be phosphorylated at amino acid residues Ser70, Ser87, Thr69. These results suggest that phosphorylation of the Bcl-2 protein is an important part of cellular response to the stress and that this posttranslational modification is significantly involved in control of the Bcl-2 protein function.
ER -
ONDROUŠKOVÁ, Eva, Jana SLOVÁČKOVÁ, Vendula PELKOVÁ, Jiřina PROCHÁZKOVÁ, Karel SOUČEK, Petr BENEŠ a Jan ŠMARDA. Heavy metals induce phosphorylation of the Bcl-2 protein by Jun N-terminal kinase. In \textit{XIX. Biologické dny. Biologický výzkum pro lidské zdraví}. Brno: Československá biologická společnost a LF Univerzity Karlovy v Hradci Králové, 2008, s.~74-75. ISBN~978-80-7399-545-4.
|
