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Such a modulation of proteasome activity is explained, at least in part, by the circadian expression of both Nuclear factor (erythroid-derived 2)-like 2 (Nrf2) and the proteasome activator PA28ab
Results show that PA28alpha was found to be overexpressed in oral squamous cell carcinoma cell lines and tumor tissues. High expression of PA28alpha was significantly associated with recurrence and poorer overall survival.
Constitutive expression of PA28 and ERAP1 in melanoma cells indicate that both interfere with MART-1(26-35) epitope generation even in the absence of IFN-gamma
PA28 is a tumor marker and a potential target for therapeutic intervention in prostate cancer.
Reduction in ATP levels triggers immunoproteasome activation by the 11S (PA28) regulator during early antiviral response mediated by IFNbeta in mouse pancreatic beta-cells.
the first evidence of a novel ovarian cancer-specific marker
PA28 selectively up-regulates the presentation of viral MHC class I epitopes and that down regulation PA28 in tumor cells results in impaired presentation of a human TRP2 tumor antigen.
Impaired expression of proteasome subunits is involved in the loss of HLA class I expression in human colon cancer cells.
The relationship between anti-PA28alpha and Ki antibodies suggests the importance of an antigen-driven system in the induction of an autoimmune response to PA28 complex.
DJ-1 and PA28alpha may have roles in the onset of hepatocarcinogenesis
the 11S proteasome activator complex, Reg alpha fragment, may have a role in ovarian cancer
bortezomib-adapted HL-60 cells showed increased expression and proteasome association of the 11S proteasome activator
In mouse models of both genetic and dietary obesity, stimulation of proteasomal activity by exogenously expressing Nrf1 or by treatment with the proteasome activator PA28alpha in BAT resulted in improved insulin sensitivity. In conclusion, Nrf1 emerges as a novel guardian of brown adipocyte function, providing increased proteometabolic quality control for adapting to cold or to obesity.
PA28a overexpression quadruples the number of surviving photoreceptors in the inferior retina of mice with inherited retinal degeneration.
Study clarifies the subunit composition and arrangement of PA28ab and provides key insights into the assembly of an asymmetric complex from two highly homologous subunits. Differential scanning fluorimetry experiments and activity assays classify PA28alpha4beta3 as most stable and most active, indicating that this assembly might represent the physiologically relevant species.
Inhibiting accumulation of PA28alpha using microRNA counteracted the removal of damaged proteins demonstrating that PA28alphabeta has a role required for resetting the levels of protein damage at the transition from self-renewal to cell differentiation.
this study performed biophysical and biochemical characterization of the structure and function of the PA28 hetero-oligomer.
Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress.
demonstrate that PA28 and the proteasome immunosubunits use fundamentally different mechanisms to enhance the supply of MHC class I-binding peptides
PA28alphaOE is sufficient to up-regulate 11S proteasomes, enhance proteasome-mediated removal of misfolded and oxidized proteins, and protect against oxidative stress in cardiomyocytes
the processing of antigens is regulated by two distinct pathways, one requiring PA28 and the other hsp90
In immature dendritic cells, the assembly of PA28 alpha beta complexes appears to be limited by the low expression of PA28 beta, whereas PA28 alpha expression is already high.
PA28-associated proteasome preferentially digested within epitopic sequences of K(d), although correct C-terminal flankings were removed
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits\; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the alpha subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three alpha and three beta subunits combine to form a heterohexameric ring. Two transcripts encoding different isoforms have been identified.
proteasome activator complex subunit 1
, proteasome activator subunit 1
, 11S regulator complex subunit alpha
, activator of multicatalytic protease subunit 1
, protease (prosome, macropain) 28 subunit, alpha
, proteasome (prosome, macropain) 28 subunit, alpha
, proteasome activator 28 subunit alpha
, 29-kD MCP activator subunit
, IGUP I-5111
, interferon gamma up-regulated I-5111 protein
, interferon-gamma IEF SSP 5111
, interferon-gamma-inducible protein 5111
, PA28 alpha subunit
, proteasome activator 28 alpha subunit
, proteasome activator PA28 alpha subunit