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PA28alpha, REGalpha, PSME1
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MHC, IFN-gamma, CAN, Ubiquitin, fibrillin-1
Papers on PA28alpha
Gene Expression in HIV-Associated Neurocognitive Disorders: A Meta-Analysis.
Archer et al., Richmond, United States. In J Acquir Immune Defic Syndr, Jan 2016
Strong examples of the highly upregulated genes were PSMB8-AS1, APOL6, TRIM69, PSME1, CTSB, HLA-E, GPNMB, UBE2L6, PSME2, NET1, CAPG, B2M, RPL38, GBP1, and PLSCR1.
Comparative proteomic profiling of triple-negative breast cancer reveals that up-regulation of RhoGDI-2 is associated to the inhibition of caspase 3 and caspase 9.
López-Camarillo et al., Mexico. In J Proteomics, 2015
Proteomics profiling of TNBC and normal breast tissues through two-dimensional electrophoresis and ESI-MS/MS mass spectrometry revealed the existence of 16 proteins (RhoGDI-2, HSP27, SOD1, DJ1, UBE2N, PSME1, FTL, SH3BGRL, and eIF5A-1) with increased abundance in carcinomas.
Quantitative Proteomics Analysis of the Hepatitis C Virus Replicon High-Permissive and Low-Permissive Cell Lines.
Peng et al., Beijing, China. In Plos One, 2014
The differential expression of Glutathione S-transferase P (GSTP1), Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCHL1), carboxylesterase 1 (CES1), vimentin, Proteasome activator complex subunit1 (PSME1), and Cathepsin B (CTSB) were verified by western blot.
Bleomycin hydrolase and hyperhomocysteinemia modulate the expression of mouse proteins involved in liver homeostasis.
Jakubowski et al., Poznań, Poland. In Amino Acids, 2014
The down-regulated proteins are involved in lipoprotein metabolism (ApoA1, ApoE), antigen processing (Psme1), energy metabolism (Atp5h, Gamt), methylglyoxal detoxification (Glo1), oxidative stress response (Sod1), and inactivation of catecholamine neurotransmitters (Comt).
Aptamer-based proteomic signature of intensive phase treatment response in pulmonary tuberculosis.
Ochsner et al., San Francisco, United States. In Tuberculosis (edinb), 2014
RESULTS: We identified protein expression differences associated with 8-week culture status, including Coagulation Factor V, SAA, XPNPEP1, PSME1, IL-11 Rα, HSP70, Galectin-8, α2-Antiplasmin, ECM1, YES, IGFBP-1, CATZ, BGN, LYNB, and IL-7.
Blood transcriptomic biomarkers in adult primary care patients with major depressive disorder undergoing cognitive behavioral therapy.
Mohr et al., Chicago, United States. In Transl Psychiatry, 2013
Blood transcript levels of nine markers of ADCY3, DGKA, FAM46A, IGSF4A/CADM1, KIAA1539, MARCKS, PSME1, RAPH1 and TLR7, differed significantly between participants with MDD (N=32) and ND controls (N=32) at baseline (q< 0.05).
System vaccinology for the evaluation of influenza vaccine safety by multiplex gene detection of novel biomarkers in a preclinical study and batch release test.
Yamaguchi et al., Tokyo, Japan. In Plos One, 2013
We recently developed a systems biological approach to vaccine safety evaluation where identification of specific biomarkers in a rat pre-clinical study evaluated the safety of vaccines for pandemic H5N1 influenza including Irf7, Lgals9, Lgalsbp3, Cxcl11, Timp1, Tap2, Psmb9, Psme1, Tapbp, C2, Csf1, Mx2, Zbp1, Ifrd1, Trafd1, Cxcl9, β2m, Npc1, Ngfr and Ifi47.
Antibody-validated proteins in inflamed islets of fulminant type 1 diabetes profiled by laser-capture microdissection followed by mass spectrometry.
Kobayashi et al., Japan. In Plos One, 2013
Proteins involved in successive signaling in innate/adaptive immunity were identified, including SAM domain and HD domain-containing protein 1 (SAMHD1), Ras GTPase-activating-like protein (IQGAP1), proteasome activator complex subunit 1 (PSME1), HLA class I histocompatibility antigen (HLA-C), and signal transducer and activator of transcription 1-alpha/beta (STAT1).
Genetic myostatin decrease in the golden retriever muscular dystrophy model does not significantly affect the ubiquitin proteasome system despite enhancing the severity of disease.
Willis et al., Columbus, United States. In Am J Transl Res, 2012
To examine the role of the ubiquitin proteasome and calpain systems in this accelerated decline, we determined the expression of the muscle ubiquitin ligases MuRF1, Atrogin-1, RNF25, RNF11, and CHIP: the proteasome subunits PSMA6, PSMB4, and PSME1: and calpain 1/2 by real time PCR in the cranial sartorius and vastus lateralis muscles in control, affected GRMD, and GRippet dogs.
The C-terminal fragment of the immunoproteasome PA28S (Reg alpha) as an early diagnosis and tumor-relapse biomarker: evidence from mass spectrometry profiling.
Salzet et al., Villeneuve-d'Ascq, France. In Histochem Cell Biol, 2012
the first evidence of a novel ovarian cancer-specific marker
Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress.
Davies et al., Los Angeles, United States. In J Biol Chem, 2012
Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress.
PA28 and the proteasome immunosubunits play a central and independent role in the production of MHC class I-binding peptides in vivo.
Sijts et al., Utrecht, Netherlands. In Eur J Immunol, 2011
demonstrate that PA28 and the proteasome immunosubunits use fundamentally different mechanisms to enhance the supply of MHC class I-binding peptides
Enhancement of proteasome function by PA28α overexpression protects against oxidative stress.
Wang et al., United States. In Faseb J, 2011
PA28alphaOE is sufficient to up-regulate 11S proteasomes, enhance proteasome-mediated removal of misfolded and oxidized proteins, and protect against oxidative stress in cardiomyocytes
Characterization of the ubiquitin-proteasome system in bortezomib-adapted cells.
Driessen et al., Tübingen, Germany. In Leukemia, 2009
bortezomib-adapted HL-60 cells showed increased expression and proteasome association of the 11S proteasome activator
Regulation of proteasome complexes by gamma-interferon and phosphorylation.
Broadfoot et al., Bristol, United Kingdom. In Biochimie, 2001
26S proteasomes contain the core 20S proteasome together with two 19S regulatory complexes.
Structural plasticity of the proteasome and its function in antigen processing.
Schmidtke et al., Sankt Gallen, Switzerland. In Crit Rev Immunol, 2000
Proteasome activity is further changed by the IFN-gamma-mediated induction of the proteasome regulator PA28alpha/beta and the downregulation of PA28gamma.
The proteasome activator 11 S REG (PA28) and class I antigen presentation.
Ustrell et al., Salt Lake City, United States. In Biochem J, 2000
Two protein complexes have been found to bind the ends of the proteasome and activate it.
Structure of the proteasome activator REGalpha (PA28alpha).
Hill et al., Salt Lake City, United States. In Nature, 1998
The specificity of the 20S proteasome, which degrades many intracellular proteins, is regulated by protein complexes that bind to one or both ends of the cylindrical proteasome structure.
Structural and functional properties of proteasome activator PA28.
Dahlmann et al., Düsseldorf, Germany. In Mol Biol Rep, 1997
The proteasome activator PA28 or 11S regulator is a protein complex composed of two different but homologous polypeptides, termed PA28alpha and PA28beta.
A role for the proteasome regulator PA28alpha in antigen presentation.
Kloetzel et al., Berlin, Germany. In Nature, 1996
A mouse fibroblast line expressing the murine cytomegalovirus pp89 protein was transfected with either the human or murine gene encoding the PA28alpha subunit, which is sufficient to activate the peptide-hydrolysing activity of the 20S proteasome in vitro.
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