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Inhibition of protein phosphatases by microcystis and nodularin associated with hepatotoxicity
The hepatotoxicity of microcystins and nodularin may result from inhibition of protein phosphatases and the increase of phosphoproteins, which is similar to that of okadaic acid in the nanomolar range of concentration.
Interferon-gamma induces different subunit organizations and functional diversity of proteasomes.
The results indicate that IFN-gamma modifies not only the structural organization of the proteasome, but also its functions, and the role in the antigen processing/presentation pathway of proteasomes with functional diversity acquired through alteration of their subunit assembly in response to IFN -gamma stimulation.
Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
It is demonstrated that immunodepletion of proteasomes from cell extracts causes almost complete loss of ATP-and antizyme-dependent degradation of ODC, suggesting that the 26S proteasome, widely viewed as specific for ubiquitin-conjugated proteins, is the main enzyme responsible for ODC degradation.
Abnormally high expression of proteasomes in human leukemic cells.
Proteasome expression was also greatly increased in normal blood mononuclear cells during blastogenic transformation induced by phytohemagglutinin; their expression increased in parallel with induction of DNA synthesis and returned to the basal level with progress of the cell cycle.
Fas-mediated apoptosis in primary cultured mouse hepatocytes.
It is suggested that cultured mouse hepatocytes express protective proteins against apoptosis and that phosphorylation by PKC is also involved in protection of the hepatocytes from Fas-mediated apoptosis.