| Autor: |
Tsimokha AS, Mittenberg AG, Kulichkova VA, Vatazhok IuIa, Moiseeva TN, Evteeva IN, Ermolaeva IuB, Gauze LN, Konstantinova IM |
| Jazyk: |
ruština |
| Zdroj: |
Tsitologiia [Tsitologiia] 2007; Vol. 49 (6), pp. 451-9. |
| Abstrakt: |
Here we have studied changes in the subunit composition, phosphorylation state and enzymatic activities of 26S proteasomes in cells undergoing the programmed cell death. Apoptosis in proerythroleukemic K562 cells was induced by glutathione-depleting agent, diethylmaleate (DEM). We have shown for the first time that proteasomes isolated from the nuclei of control and induces K562 cells differ in their subunit patterns, as well as in the phosphorylation state of subunits on threonine and tyrosine residues. We observed trypsin- and chymotrypsin-like activities on nuclear proteasomes and the specificity of proteasomal nucleolysis of several individual messenger RNAs (c-fos and c-myc) to be changed under effect of DEM on K562 cells. Treatment of K562 cells with DEM leads to modification of zeta/alpha5 and iota/alpha6 proteasomal subunits associated with RNAse activity of proteasomes. These findings confirm our hypothesis about so-called reprogramming of nuclear proteasome population in undergoing apoptosis K562 cells which is manifested by the changes in proteasomal composition, phosphorylation state, and enzymatic activities during the programmed cell death. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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