proteasome

(2006) A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes.

As other kinds of cells, RPE have a normally active UPP [17], and the activity of UPP decreases in different human tissues (including skin, muscle, kidney, liver, lung, heart, lentis, and RPE) with the increase of age [17, 31, 32], however, the relationship between the decline in proteasome activity in RPE and the production of inflammatory cytokine IL-6 which plays an important role in cell growth and inflammatory reactions [30, 33] remains to be obscured.

All eukaryotic cells contain proteasomes. Recent studies have shown that proteasomes are identified not only in tissues but also in fluids, such as serum, cerebrospinal fluid, or extracellular bronchoalveolar lavage fluids.

To investigate if the OPN release from mesangial cells exposed to high glucose was caused by the binding of Pa28[alpha]/[beta] proteins to the 20S proteasomes, we examined peptides capable of disrupting the association of Pa28[alpha]/[beta] with the 20S proteasome.

On the other hand, six enriched pathways were upregulated in the hyperglycemic donors (P < 0.05), while at FDR < 25% only two pathways (proteasome and spliceosome) were significant (Table 2 and Figures 1(c)-1(d)).

The bulk of protein turnover in the cell is governed by the 26S proteasome, a highly conserved multisubunit protease complex with essential roles in regulating proteins levels in the cytoplasm and nucleus of all eukaryotes [1-5].

Preliminary observations on white and grey matter of MS patients suggested that the degradation rates of short fluorogenic peptides by 20S proteasomes are decreased when compared to brain-tissue controls [18].

Sheng, "Autophosphorylated CaMKII[alpha] acts as a scaffold to recruit proteasomes to dendritic spines," Cell, vol.

in part, to a decline in the ability of proteasomes to degrade oxidatively-modified proteins

Bortezomib is a reversible and highly selective inhibitor of 26S proteasome. This drug can inhibit a group of proteins (known as proteasomes) that are needed by neoplastic cells to survive and multiply.

Hernebring can show that the damaged proteins in the cells are probably broken down by molecular machines called proteasomes. The proteasome activity increases considerably during the initial steps of embryonic stem cell differentiation in mice.