Immunoproteasome Deficiency Is a Feature of Non-Small Cell Lung
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Genetic Variations in the PSMA6 and PSMC6 Proteasome Genes Are Associated with Multiple Sclerosis and Response to Interferon‑Β Therapy in Latvians
EXPERIMENTAL AND THERAPEUTIC MEDICINE 21: 478, 2021 Genetic variations in the PSMA6 and PSMC6 proteasome genes are associated with multiple sclerosis and response to interferon‑β therapy in Latvians NATALIA PARAMONOVA1, JOLANTA KALNINA1, KRISTINE DOKANE1, KRISTINE DISLERE1, ILVA TRAPINA1, TATJANA SJAKSTE1 and NIKOLAJS SJAKSTE1,2 1Genomics and Bioinformatics, Institute of Biology of The University of Latvia; 2Department of Medical Biochemistry of The University of Latvia, LV‑1004 Riga, Latvia Received July 8, 2020; Accepted December 8, 2020 DOI: 10.3892/etm.2021.9909 Abstract. Several polymorphisms in genes related to the Introduction ubiquitin‑proteasome system exhibit an association with pathogenesis and prognosis of various human autoimmune Multiple sclerosis (MS) is a lifelong demyelinating disease of diseases. Our previous study reported the association the central nervous system. The clinical onset of MS tends to between multiple sclerosis (MS) and the PSMA3‑rs2348071 be between the second and fourth decade of life. Similarly to polymorphism in the Latvian population. The current study other autoimmune diseases, women are affected 3‑4 times more aimed to evaluate the PSMA6 and PSMC6 genetic variations, frequently than men (1). About 10% of MS patients experience their interaction between each other and with the rs2348071, a primary progressive MS form characterized by the progres‑ on the susceptibility to MS risk and response to therapy in sion of neurological disability from the onset. In about 90% the Latvian population. PSMA6‑rs2277460, ‑rs1048990 and of MS patients, the disease undergoes the relapse‑remitting PSMC6‑rs2295826, ‑rs2295827 were genotyped in the MS MS course (RRMS); in most of these patients, the condition case/control study and analysed in terms of genotype‑protein acquires secondary progressive course (SPMS) (2). -
An Integrative Analysis of Gene Expression and Molecular
Muraro and Simmons BMC Bioinformatics (2016) 17:42 DOI 10.1186/s12859-016-0886-z RESEARCH ARTICLE Open Access An integrative analysis of gene expression and molecular interaction data to identify dys-regulated sub-networks in inflammatory bowel disease Daniele Muraro* and Alison Simmons Abstract Background: Inflammatory bowel disease (IBD) consists of two main disease-subtypes, Crohn’s disease (CD) and ulcerative colitis (UC); these subtypes share overlapping genetic and clinical features. Genome-wide microarray data enable unbiased documentation of alterations in gene expression that may be disease-specific. As genetic diseases are believed to be caused by genetic alterations affecting the function of signalling pathways, module-centric optimisation algorithms, whose aim is to identify sub-networks that are dys-regulated in disease, are emerging as promising approaches. Results: In order to account for the topological structure of molecular interaction networks, we developed an optimisation algorithm that integrates databases of known molecular interactions with gene expression data; such integration enables identification of differentially regulated network modules. We verified the performance of our algorithm by testing it on simulated networks; we then applied the same method to study experimental data derived from microarray analysis of CD and UC biopsies and human interactome databases. This analysis allowed the extraction of dys-regulated subnetworks under different experimental conditions (inflamed and uninflamed tissues in CD and UC). Optimisation was performed to highlight differentially expressed network modules that may be common or specific to the disease subtype. Conclusions: We show that the selected subnetworks include genes and pathways of known relevance for IBD; in particular, the solutions found highlight cross-talk among enriched pathways, mainly the JAK/STAT signalling pathway and the EGF receptor signalling pathway. -
On the Role of the Immunoproteasome in Transplant Rejection
Immunogenetics (2019) 71:263–271 https://doi.org/10.1007/s00251-018-1084-0 REVIEW On the role of the immunoproteasome in transplant rejection Michael Basler1,2 & Jun Li1,3 & Marcus Groettrup1,2 Received: 17 July 2018 /Accepted: 4 September 2018 /Published online: 15 September 2018 # Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract The immunoproteasome is expressed in cells of hematopoietic origin and is induced during inflammation by IFN-γ. Targeting the immunoproteasome with selective inhibitors has been shown to be therapeutically effective in pre-clinical models for autoim- mune diseases, colitis-associated cancer formation, and transplantation. Immunoproteasome inhibition prevents activation and proliferation of lymphocytes, lowers MHC class I cell surface expression, reduces the expression of cytokines of activated immune cells, and curtails T helper 1 and 17 cell differentiation. This might explain the in vivo efficacy of immunoproteasome inhibition in different pre-clinical disease models for autoimmunity, cancer, and transplantation. In this review, we summarize the effect of immunoproteasome inhibition in different animal models for transplantation. Keywords Proteasome . Immunoproteasome . Antigen processing . Antigen presentation . Transplantation Introduction et al. 2012). Depending on the cell type and the presence or absence of the pro-inflammatory cytokine interferon (IFN)-γ, The proteasome is responsible for the degradation of proteins the three inducible β subunits of the immunoproteasome low in the cytoplasm and nuclei of all eukaryotic cells and exerts molecular mass polypeptide (LMP)2 (β1i), multicatalytic en- numerous essential regulatory functions in nearly all cell bio- dopeptidase complex-like (MECL)-1 (β2i), and LMP7 (β5i), logical pathways. The 26S proteasome degrades poly- can, in addition to the corresponding constitutive subunits ubiquitylated protein substrates and consists of a 19S regulator β1c, β2c, and β5c, enrich the cellular assortment of catalyti- and a 20S proteolytic core complex. -
Proteasome 26S Subunit, Non Atpase 7 (PSMD7)
RPG282Hu01 10µg Recombinant Proteasome 26S Subunit, Non ATPase 7 (PSMD7) Organism Species: Homo sapiens (Human) Instruction manual FOR IN VITRO USE AND RESEARCH USE ONLY NOT FOR USE IN CLINICAL DIAGNOSTIC PROCEDURES 10th Edition (Revised in Jan, 2014) [ PROPERTIES ] Residues: Met1~Lys324 Tags: Two N-terminal Tags, His-tag and T7-tag Accession: P51665 Host: E. coli Purity: >90% Endotoxin Level: <1.0EU per 1μg (determined by the LAL method). Formulation: Supplied as lyophilized form in 20mM Tris, 150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT, 0.01% sarcosyl, 5% trehalose, and preservative. Predicted isoelectric point: 6.7 Predicted Molecular Mass: 40.8kDa Applications: SDS-PAGE; WB; ELISA; IP. (May be suitable for use in other assays to be determined by the end user.) [ USAGE ] Reconstitute in sterile ddH2O. [ STORAGE AND STABILITY ] Storage: Avoid repeated freeze/thaw cycles. Store at 2-8oC for one month. Aliquot and store at -80oC for 12 months. Stability Test: The thermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37oC for 48h, and no obvious degradation and precipitation were observed. (Referring from China Biological Products Standard, which was calculated by the Arrhenius equation.) The loss of this protein is less than 5% within the expiration date under appropriate storage condition. [ SEQUENCES ] The sequence of the target protein is listed below. MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK DTTVGTLSQR ITNQVHGLKG LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR KEDKEKDKDK EKSDVKKEEK KEKK [ REFERENCES ] 1. -
Protein Expression Analysis of an in Vitro Murine Model of Prostate Cancer Progression: Towards Identification of High-Potential Therapeutic Targets
Journal of Personalized Medicine Article Protein Expression Analysis of an In Vitro Murine Model of Prostate Cancer Progression: Towards Identification of High-Potential Therapeutic Targets Hisham F. Bahmad 1,2,3 , Wenjing Peng 4, Rui Zhu 4, Farah Ballout 1, Alissar Monzer 1, 1,5 6, , 1, , 4, , Mohamad K. Elajami , Firas Kobeissy * y , Wassim Abou-Kheir * y and Yehia Mechref * y 1 Department of Anatomy, Cell Biology and Physiological Sciences, Faculty of Medicine, American University of Beirut, Beirut 1107-2020, Lebanon; [email protected] (H.F.B.); [email protected] (F.B.); [email protected] (A.M.); [email protected] (M.K.E.) 2 Arkadi M. Rywlin M.D. Department of Pathology and Laboratory Medicine, Mount Sinai Medical Center, Miami Beach, FL 33140, USA 3 Herbert Wertheim College of Medicine, Florida International University, Miami, FL 33199, USA 4 Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409, USA; [email protected] (W.P.); [email protected] (R.Z.) 5 Department of Internal Medicine, Mount Sinai Medical Center, Miami Beach, FL 33140, USA 6 Department of Biochemistry and Molecular Genetics, Faculty of Medicine, American University of Beirut, Beirut 1107-2020, Lebanon * Correspondence: [email protected] (F.K.); [email protected] (W.A.-K.); [email protected] (Y.M.); Tel.: +961-1-350000 (ext. 4805) (F.K.); +961-1-350000 (ext. 4778) (W.A.K.); +1-806-834-8246 (Y.M.); Fax: +1-806-742-1289 (Y.M.); 961-1-744464 (W.A.K.) These authors have contributed equally to this work as joint senior authors. -
Proteasome System of Protein Degradation and Processing
ISSN 0006-2979, Biochemistry (Moscow), 2009, Vol. 74, No. 13, pp. 1411-1442. © Pleiades Publishing, Ltd., 2009. Original Russian Text © A. V. Sorokin, E. R. Kim, L. P. Ovchinnikov, 2009, published in Uspekhi Biologicheskoi Khimii, 2009, Vol. 49, pp. 3-76. REVIEW Proteasome System of Protein Degradation and Processing A. V. Sorokin*, E. R. Kim, and L. P. Ovchinnikov Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: [email protected]; [email protected] Received February 5, 2009 Abstract—In eukaryotic cells, degradation of most intracellular proteins is realized by proteasomes. The substrates for pro- teolysis are selected by the fact that the gate to the proteolytic chamber of the proteasome is usually closed, and only pro- teins carrying a special “label” can get into it. A polyubiquitin chain plays the role of the “label”: degradation affects pro- teins conjugated with a ubiquitin (Ub) chain that consists at minimum of four molecules. Upon entering the proteasome channel, the polypeptide chain of the protein unfolds and stretches along it, being hydrolyzed to short peptides. Ubiquitin per se does not get into the proteasome, but, after destruction of the “labeled” molecule, it is released and labels another molecule. This process has been named “Ub-dependent protein degradation”. In this review we systematize current data on the Ub–proteasome system, describe in detail proteasome structure, the ubiquitination system, and the classical ATP/Ub- dependent mechanism of protein degradation, as well as try to focus readers’ attention on the existence of alternative mech- anisms of proteasomal degradation and processing of proteins. -
A Novel Proteasome Inhibitor NPI-0052 As an Anticancer Therapy
British Journal of Cancer (2006) 95, 961 – 965 & 2006 Cancer Research UK All rights reserved 0007 – 0920/06 $30.00 www.bjcancer.com Minireview A novel proteasome inhibitor NPI-0052 as an anticancer therapy 1 1 ,1 D Chauhan , T Hideshima and KC Anderson* 1Department of Medical Oncology, Harvard Medical School, Dana Farber Cancer Institute, The Jerome Lipper Multiple Myeloma Center, Boston, MA 02115, USA Proteasome inhibitor Bortezomib/Velcade has emerged as an effective anticancer therapy for the treatment of relapsed and/or refractory multiple myeloma (MM), but prolonged treatment can be associated with toxicity and development of drug resistance. In this review, we discuss the recent discovery of a novel proteasome inhibitor, NPI-0052, that is distinct from Bortezomib in its chemical structure, mechanisms of action, and effects on proteasomal activities; most importantly, it overcomes resistance to conventional and Bortezomib therapies. In vivo studies using human MM xenografts shows that NPI-0052 is well tolerated, prolongs survival, and reduces tumour recurrence. These preclinical studies provided the basis for Phase-I clinical trial of NPI-0052 in relapsed/ refractory MM patients. British Journal of Cancer (2006) 95, 961–965. doi:10.1038/sj.bjc.6603406 www.bjcancer.com & 2006 Cancer Research UK Keywords: protein degradation; proteasomes; multiple myeloma; novel therapy; apoptosis; drug resistance The systemic regulation of protein synthesis and protein degrada- inducible immunoproteasomes b-5i, b-1i, b-2i with different tion is essential -
Molecular Pathology and Novel Clinical Therapy for Uterine
ANTICANCER RESEARCH 36 : 4997-5008 (2016) doi:10.21873/anticanres.11068 Review Molecular Pathology and Novel Clinical Therapy for Uterine Leiomyosarcoma TAKUMA HAYASHI 1,2 , MIKI KAWANO 2,3 , TOMOYUKI ICHIMURA 4, KOICHI IDA 1, HIROFUMI ANDO 1, DORIT ZHARHARY 5, YAE KANAI 6, HIROYUKI ABURATANI 7, SUSUMU TONEGAWA 8, TANRI SHIOZAWA 1, NOBUO YAEGASHI 9 and IKUO KONISHI 10 1Department of Obstetrics and Gynecology, Shinshu University School of Medicine, Nagano, Japan; 2Department of Medical Technology, International University of Health and Welfare, Chiba, Japan; 3Department of Health Science, Kyushu University Graduate School of Medicine, Fukuoka, Japan; 4Department of Obstetrics and Gynecology, Osaka City University Graduate School of Medicine, Osaka, Japan; 5SIGMA-Aldrich Israel, Rehovot, Israel; 6Pathology Division, Keio University School of Medicine, Tokyo, Japan; 7The Cancer System Laboratory, Research Center for Advanced Science and Technology, The University of Tokyo, Tokyo, Japan; 8Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, U.S.A.; 9Department of Obstetrics and Gynecology, Tohoku University Graduate School of Medicine, Miyagi, Japan; 10 National Hospital Organization Kyoto Medical Centre, Kyoto, Japan Abstract. Patients with uterine leiomyosarcoma (LMS) disease prevalence of ~37% by 12 months of age. Furthermore, typically present with vaginal bleeding, pain, and a pelvic a recent report showed the loss of ability to induce PSMB9/ β1 i mass, with atypical presentations of hypercalcemia and expression, -
Micrornas in the Etiology of Colorectal Cancer: Pathways and Clinical Implications Ashlee M
Washington University School of Medicine Digital Commons@Becker Open Access Publications 2017 MicroRNAs in the etiology of colorectal cancer: Pathways and clinical implications Ashlee M. Strubberg Washington University School of Medicine in St. Louis Blair B. Madison Washington University School of Medicine in St. Louis Follow this and additional works at: https://digitalcommons.wustl.edu/open_access_pubs Recommended Citation Strubberg, Ashlee M. and Madison, Blair B., ,"MicroRNAs in the etiology of colorectal cancer: Pathways and clinical implications." Disease Models & Mechanisms.10,3. 197-214. (2017). https://digitalcommons.wustl.edu/open_access_pubs/5644 This Open Access Publication is brought to you for free and open access by Digital Commons@Becker. It has been accepted for inclusion in Open Access Publications by an authorized administrator of Digital Commons@Becker. For more information, please contact [email protected]. © 2017. Published by The Company of Biologists Ltd | Disease Models & Mechanisms (2017) 10, 197-214 doi:10.1242/dmm.027441 REVIEW MicroRNAs in the etiology of colorectal cancer: pathways and clinical implications Ashlee M. Strubberg and Blair B. Madison* ABSTRACT rates from colorectal cancer have declined over the past 20 years, MicroRNAs (miRNAs) are small single-stranded RNAs that repress largely thanks to early detection; however, CRC incidence still mRNA translation and trigger mRNA degradation. Of the ∼1900 remains high (Siegel et al., 2015) and new treatments have been miRNA-encoding genes present in the human genome, ∼250 lagging. Treatment usually entails surgical removal of tumors, miRNAs are reported to have changes in abundance or altered which may be followed with chemotherapy and/or targeted functions in colorectal cancer. -
Supplementary Table S1. Correlation Between the Mutant P53-Interacting Partners and PTTG3P, PTTG1 and PTTG2, Based on Data from Starbase V3.0 Database
Supplementary Table S1. Correlation between the mutant p53-interacting partners and PTTG3P, PTTG1 and PTTG2, based on data from StarBase v3.0 database. PTTG3P PTTG1 PTTG2 Gene ID Coefficient-R p-value Coefficient-R p-value Coefficient-R p-value NF-YA ENSG00000001167 −0.077 8.59e-2 −0.210 2.09e-6 −0.122 6.23e-3 NF-YB ENSG00000120837 0.176 7.12e-5 0.227 2.82e-7 0.094 3.59e-2 NF-YC ENSG00000066136 0.124 5.45e-3 0.124 5.40e-3 0.051 2.51e-1 Sp1 ENSG00000185591 −0.014 7.50e-1 −0.201 5.82e-6 −0.072 1.07e-1 Ets-1 ENSG00000134954 −0.096 3.14e-2 −0.257 4.83e-9 0.034 4.46e-1 VDR ENSG00000111424 −0.091 4.10e-2 −0.216 1.03e-6 0.014 7.48e-1 SREBP-2 ENSG00000198911 −0.064 1.53e-1 −0.147 9.27e-4 −0.073 1.01e-1 TopBP1 ENSG00000163781 0.067 1.36e-1 0.051 2.57e-1 −0.020 6.57e-1 Pin1 ENSG00000127445 0.250 1.40e-8 0.571 9.56e-45 0.187 2.52e-5 MRE11 ENSG00000020922 0.063 1.56e-1 −0.007 8.81e-1 −0.024 5.93e-1 PML ENSG00000140464 0.072 1.05e-1 0.217 9.36e-7 0.166 1.85e-4 p63 ENSG00000073282 −0.120 7.04e-3 −0.283 1.08e-10 −0.198 7.71e-6 p73 ENSG00000078900 0.104 2.03e-2 0.258 4.67e-9 0.097 3.02e-2 Supplementary Table S2. -
Datasheet: VPA00155 Product Details
Datasheet: VPA00155 Description: GOAT ANTI PSMB8 Specificity: PSMB8 Format: Purified Product Type: PrecisionAb™ Polyclonal Isotype: Polyclonal IgG Quantity: 100 µl Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Western Blotting 1/1000 PrecisionAb antibodies have been extensively validated for the western blot application. The antibody has been validated at the suggested dilution. Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Further optimization may be required dependant on sample type. Target Species Human Species Cross Reacts with: Rat Reactivity N.B. Antibody reactivity and working conditions may vary between species. Product Form Purified IgG - liquid Preparation Goat polyclonal antibody purified by affinity chromatography Buffer Solution TRIS buffered saline Preservative 0.02% Sodium Azide (NaN ) 0.5 % BSA Stabilisers 3 Immunogen Peptide with the sequence C-DVSDLLHQYREANQ, from the C terminus of the protein sequence External Database Links UniProt: P28062 Related reagents Entrez Gene: 5696 PSMB8 Related reagents Synonyms LMP7, PSMB5i, RING10, Y2 Page 1 of 2 Specificity Goat anti Human PSMB8 antibody recognizes proteasome subunit beta type-8, also known as Low molecular mass protein 7, macropain subunit C13, multicatalytic endopeptidase complex subunit C13, proteasome component C13, and proteasome subunit beta-5i. The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. -
Proteasome Immunosubunits Protect Against the Development of CD8 T Cell-Mediated Autoimmune Diseases
Proteasome Immunosubunits Protect against the Development of CD8 T Cell-Mediated Autoimmune Diseases This information is current as Dietmar M. W. Zaiss, Cornelis P. J. Bekker, Andrea Gröne, of September 29, 2021. Benedicte A. Lie and Alice J. A. M. Sijts J Immunol published online 29 July 2011 http://www.jimmunol.org/content/early/2011/07/29/jimmun ol.1101003 Downloaded from Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision http://www.jimmunol.org/ • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: by guest on September 29, 2021 http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2011 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. Published July 29, 2011, doi:10.4049/jimmunol.1101003 The Journal of Immunology Proteasome Immunosubunits Protect against the Development of CD8 T Cell-Mediated Autoimmune Diseases Dietmar M. W. Zaiss,* Cornelis P. J. Bekker,* Andrea Gro¨ne,† Benedicte A. Lie,‡ and Alice J. A. M. Sijts* Exposure of cells to inflammatory cytokines induces the expression of three proteasome immunosubunits, two of which are encoded in the MHC class II region.