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Profiling of Cell Cycle Genes of Breast Cells Exposed to Etodolac
1383-1391.qxd 29/3/2010 11:48 Ì ™ÂÏ›‰·1383 ONCOLOGY REPORTS 23: 1383-1391, 2010 Profiling of cell cycle genes of breast cells exposed to etodolac D. ROY1,2*, G.A. ARASON2*, B. CHOWDHURY3,4, A. MITRA5 and G.M. CALAF6,7 1Department of Natural Sciences, Hostos College of the City University of New York, Bronx, NY; 2Graduate Biotechnology Program, Manhattan College, Riverdale, NY; 3Human Retrovirus Section, Vaccine Branch, National Cancer Institute, National Institutes of Health, Frederick, MD; 4Department of Cellular Injury, Military Casualty Research, Walter Reed Army Institute of Research, Silver Spring, MD; 5Department of Chemistry, The College of Mount Saint Vincent, Riverdale, NY; 6Center for Radiological Research, Columbia University Medical Center, New York, NY, USA; 7Instituto de Alta Investigación, Universidad de Tarapaca, Arica, Chile Received September 29, 2009; Accepted November 6, 2009 DOI: 10.3892/or_00000775 Abstract. Breast cancer represents the second leading cause Introduction of cancer-related deaths in the world. There is increasing evidence that perturbation of cell cycle regulation is an Breast cancer represents the second leading cause of cancer- important contributing factor to various cancer progression related deaths in the United States and other Western countries; stages. There are key checkpoints in the cell cycle involving accounting for about 30-40% of all newly diagnosed cancers various regulatory proteins. The relationship between these (1,2). Hereditary breast cancer accounts for just 5-10% of cell cycle regulatory proteins and cell cycle arrest by cyclo- cases. It is generally believed that a family history of breast oxygenase (COX) inhibitors during neoplastic progression cancer and hormonal imbalances also contributes to the remains largely unknown. -
The Mitotic Checkpoint Protein MAD2 Delivers Monoamine Transporters to Endocytosis
bioRxiv preprint doi: https://doi.org/10.1101/2021.06.09.447721; this version posted June 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 1 The mitotic checkpoint protein MAD2 delivers monoamine transporters to endocytosis. Florian Koban1*, Michael Freissmuth1 https://orcid.org/0000-0003-0912-3114, https://orcid.org/0000-0001-9398-1765 1Institute of Pharmacology and the Gaston H. Glock Research Laboratories for Exploratory Drug Development, Center of Physiology and Pharmacology, Medical University of Vienna, Vienna, Austria. *Corresponding Author: Florian Koban, PhD Institute of Pharmacology and the Gaston H. Glock Research Laboratories for Exploratory Drug Development, Center of Physiology and Pharmacology, Medical University of Vienna. Waehringer Strasse 13A, 1090 Vienna, Austria E-mail: [email protected] Tel.: +43 1 40160 31328 Author contributions: F. K. conceptualized the study; F. K. conducted research; F. K. and M. F. analyzed data; F.K. and M.F. wrote the paper. bioRxiv preprint doi: https://doi.org/10.1101/2021.06.09.447721; this version posted June 10, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. 2 ABSTRACT Monoamine transporters retrieve serotonin (SERT), dopamine (DAT) and norepinephrine (NET) from the synaptic cleft. Surface levels of transporters are also regulated by internalization. Clathrin-mediated endocytosis of cargo proteins requires adaptor protein 2 (AP2), which recruits cargo to the nascent clathrin- cage. The transporter C-terminus is required for internalization but lacks an AP2- binding site. -
Identification of Conserved Genes Triggering Puberty in European Sea
Blázquez et al. BMC Genomics (2017) 18:441 DOI 10.1186/s12864-017-3823-2 RESEARCHARTICLE Open Access Identification of conserved genes triggering puberty in European sea bass males (Dicentrarchus labrax) by microarray expression profiling Mercedes Blázquez1,2* , Paula Medina1,2,3, Berta Crespo1,4, Ana Gómez1 and Silvia Zanuy1* Abstract Background: Spermatogenesisisacomplexprocesscharacterized by the activation and/or repression of a number of genes in a spatio-temporal manner. Pubertal development in males starts with the onset of the first spermatogenesis and implies the division of primary spermatogonia and their subsequent entry into meiosis. This study is aimed at the characterization of genes involved in the onset of puberty in European sea bass, and constitutes the first transcriptomic approach focused on meiosis in this species. Results: European sea bass testes collected at the onset of puberty (first successful reproduction) were grouped in stage I (resting stage), and stage II (proliferative stage). Transition from stage I to stage II was marked by an increase of 11ketotestosterone (11KT), the main fish androgen, whereas the transcriptomic study resulted in 315 genes differentially expressed between the two stages. The onset of puberty induced 1) an up-regulation of genes involved in cell proliferation, cell cycle and meiosis progression, 2) changes in genes related with reproduction and growth, and 3) a down-regulation of genes included in the retinoic acid (RA) signalling pathway. The analysis of GO-terms and biological pathways showed that cell cycle, cell division, cellular metabolic processes, and reproduction were affected, consistent with the early events that occur during the onset of puberty. -
Human Pol Ζ Purified with Accessory Subunits Is Active in Translesion DNA Synthesis and Complements Pol Η in Cisplatin Bypass
Human Pol ζ purified with accessory subunits is active in translesion DNA synthesis and complements Pol η in cisplatin bypass Young-Sam Lee1, Mark T. Gregory, and Wei Yang2 Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892 Contributed by Wei Yang, December 27, 2013 (sent for review December 5, 2013) DNA polymerase ζ (Pol ζ) is a eukaryotic B-family DNA polymerase a nucleotide opposite either a cis–syn thymine or a 6-4 photo- that specializes in translesion synthesis and is essential for normal product (23). Genetic data indicate that a complete lesion bypass embryogenesis. At a minimum, Pol ζ consists of a catalytic subunit event may require two TLS DNA polymerases (24)—one for Rev3 and an accessory subunit Rev7. Mammalian Rev3 contains nucleotide incorporation opposite a lesion (insertion step) and >3,000 residues and is twice as large as the yeast homolog. To the other for the subsequent primer extension (extension step). date, no vertebrate Pol ζ has been purified for biochemical char- The insertion step of TLS is often accomplished by a Y-family acterization. Here we report purification of a series of human Rev3 polymerase, whose active site is uncommonly large, solvent- deletion constructs expressed in HEK293 cells and identification of exposed, and flexible (25). Studies of another B-family TLS DNA a minimally catalytically active human Pol ζ variant. With a tagged polymerase from Escherichia coli (Pol II) show that it efficiently form of an active Pol ζ variant, we isolated two additional acces- extends a DNA primer after a lesion by looping out the damaged sory subunits of human Pol ζ, PolD2 and PolD3. -
Protein Interactions in the Cancer Proteome† Cite This: Mol
Molecular BioSystems View Article Online PAPER View Journal | View Issue Small-molecule binding sites to explore protein– protein interactions in the cancer proteome† Cite this: Mol. BioSyst., 2016, 12,3067 David Xu,ab Shadia I. Jalal,c George W. Sledge Jr.d and Samy O. Meroueh*aef The Cancer Genome Atlas (TCGA) offers an unprecedented opportunity to identify small-molecule binding sites on proteins with overexpressed mRNA levels that correlate with poor survival. Here, we analyze RNA-seq and clinical data for 10 tumor types to identify genes that are both overexpressed and correlate with patient survival. Protein products of these genes were scanned for binding sites that possess shape and physicochemical properties that can accommodate small-molecule probes or therapeutic agents (druggable). These binding sites were classified as enzyme active sites (ENZ), protein–protein interaction sites (PPI), or other sites whose function is unknown (OTH). Interestingly, the overwhelming majority of binding sites were classified as OTH. We find that ENZ, PPI, and OTH binding sites often occurred on the same structure suggesting that many of these OTH cavities can be used for allosteric modulation of Creative Commons Attribution 3.0 Unported Licence. enzyme activity or protein–protein interactions with small molecules. We discovered several ENZ (PYCR1, QPRT,andHSPA6)andPPI(CASC5, ZBTB32,andCSAD) binding sites on proteins that have been seldom explored in cancer. We also found proteins that have been extensively studied in cancer that have not been previously explored with small molecules that harbor ENZ (PKMYT1, STEAP3,andNNMT) and PPI (HNF4A, MEF2B,andCBX2) binding sites. All binding sites were classified by the signaling pathways to Received 29th March 2016, which the protein that harbors them belongs using KEGG. -
Anti-MAD2L2 Monoclonal Antibody, Clone FQS24768 (DCABH-6886) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-MAD2L2 monoclonal antibody, clone FQS24768 (DCABH-6886) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Rabbit Monoclonal to Mad2L2 Antigen Description Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation. Immunogen Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human Mad2L2 aa 150 to the C-terminus. The exact sequence is proprietary.Database link: Q9UI95 Isotype IgG Source/Host Rabbit Species Reactivity Mouse, Rat, Human Clone FQS24768 Purity Protein A purified Conjugate Unconjugated Applications IP, ICC/IF, Flow Cyt, IHC-P, WB Positive Control K562, SW480, Hela, Molt-4 cell lysates, human ovarian carcinoma tissue, Hela cells, Format Liquid Size 100 μl Buffer Preservative: 0.01% Sodium azide; Constituents: 59% PBS, 0.05% BSA, 40% Glycerol 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved Preservative 0.01% Sodium Azide Storage Store at +4°C short term (1-2 weeks). -
Identi Cation of Novel Hub Genes Associated with Gastric Cancer
Identication of Novel Hub Genes Associated With Gastric Cancer Using Integrated Bioinformatics Analysis Xiao-Qing Lu Department of Breast Surgery, the second hospital of Shanxi Medical University Jia-qian Zhang Shanxi Medical University Second Aliated Hospital https://orcid.org/0000-0001-9042-0305 Jun Qiao Department of Rheumatology, the Second Hospital of Shanxi Medical University Sheng-Xiao Zhang Department of Rheumatology, the Second Hospital of Shanxi Medical University Meng-Ting Qiu Department of Rheumatology, the Second Hospital of Shanxi Medical University Xiang-Rong Liu Department of Breast Surgery, the Second Hospital of Shanxi Medical University Xiao-Xia Chen Department of Breast Surgery, the Second Hospital of Shanxi Medical University Chong Gao Department of Pathology, Brigham and Women's Hospital, Harvard Medical School Huan-Hu Zhang ( [email protected] ) Department of Gastroenterology Shanxi Cancer Hospital Taiyuan, Shanxi 030001 China Research article Keywords: Gastric cancer, Bioinformatics analysis, Differentially expressed genes Posted Date: September 10th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-58756/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/25 Abstract Background: Gastric cancer (GC) is one of the most common solid malignant tumors worldwide with a high- recurrence-rate. Identifying the molecular signatures and specic biomarkers of GC might provide novel clues for GC prognosis and targeted therapy. Methods: Gene expression proles were obtained from the ArrayExpress and Gene Expression Omnibus database. Differentially expressed genes (DEGs) were picked out by R software. The hub genes were screened by cytoHubba plugin. Their prognostic values were assessed by Kaplan–Meier survival analyses and the gene expression proling interactive analysis (GEPIA). -
MAD2L2 Monoclonal ANTIBODY
For Research Use Only MAD2L2 Monoclonal ANTIBODY www.ptgcn.com Catalog Number:67100-1-Ig Basic Information Catalog Number: GenBank Accession Number: CloneNo.: 67100-1-Ig BC015244 2A4C2 Size: GeneID (NCBI): Recommended Dilutions: 1000 μg/ml 10459 WB 1:5000-1:20000 Source: Full Name: IHC 1:500-1:2000 Mouse MAD2 mitotic arrest deficient-like 2 (yeast) Isotype: Calculated MW: IgG2b 211aa,24 kDa Purification Method: Observed MW: Protein A purification 24 kDa Immunogen Catalog Number: AG28233 Applications Tested Applications: Positive Controls: IHC, WB, ELISA WB : HeLa cells; Species Specificity: IHC : human lymphoma tissue; Human, mouse, rat Note-IHC: suggested angen retrieval with TE buffer pH 9.0; (*) Alternavely, angen retrieval may be performed with citrate buffer pH 6.0 MAD family, together with BUB and Mps1,Cdc20k, play roles in the mitotic spindle checkpoint. MAD2L2 is one of the MAD family. It can mediate the second Background Information polymerase switching in translation DNA synthesis by mediating the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1. Through regulation of the JNK-mediate phosphorylation and activation of the transcriptional activator ELK1, MAD2L2 involves in cellular response to DNA damage. Also it has role in the progression of cell cycle and peithelial-mesenchymal transdifferentiation. Storage: Storage Store at -20ºC. Stable for one year after shipment. Storage Buffer: PBS with 0.1% sodium azide and 50% glycerol pH 7.3. Aliquoting is unnecessary for -20ºC storage For technical support and original validation data for this product please contact: This product is exclusively available under T: 4006900926 E: [email protected] W: ptgcn.com Proteintech Group brand and is not available to purchase from any other manufacturer. -
Proteomic Analysis of Ubiquitin Ligase KEAP1 Reveals Associated Proteins That Inhibit NRF2 Ubiquitination
Published OnlineFirst February 4, 2013; DOI: 10.1158/0008-5472.CAN-12-4400 Cancer Molecular and Cellular Pathobiology Research Proteomic Analysis of Ubiquitin Ligase KEAP1 Reveals Associated Proteins That Inhibit NRF2 Ubiquitination Bridgid E. Hast1, Dennis Goldfarb2, Kathleen M. Mulvaney1, Michael A. Hast4, Priscila F. Siesser1, Feng Yan1, D. Neil Hayes3, and Michael B. Major1,2 Abstract Somatic mutations in the KEAP1 ubiquitin ligase or its substrate NRF2 (NFE2L2) commonly occur in human cancer, resulting in constitutive NRF2-mediated transcription of cytoprotective genes. However, many tumors display high NRF2 activity in the absence of mutation, supporting the hypothesis that alternative mechanisms of pathway activation exist. Previously, we and others discovered that via a competitive binding mechanism, the proteins WTX (AMER1), PALB2, and SQSTM1 bind KEAP1 to activate NRF2. Proteomic analysis of the KEAP1 protein interaction network revealed a significant enrichment of associated proteins containing an ETGE amino acid motif, which matches the KEAP1 interaction motif found in NRF2. Like WTX, PALB2, and SQSTM1, we found that the dipeptidyl peptidase 3 (DPP3) protein binds KEAP1 via an "ETGE" motif to displace NRF2, thus inhibiting NRF2 ubiquitination and driving NRF2-dependent transcription. Comparing the spectrum of KEAP1-interacting proteins with the genomic profile of 178 squamous cell lung carcinomas characterized by The Cancer Genome Atlas revealed amplification and mRNA overexpression of the DPP3 gene in tumors with high NRF2 activity but lacking NRF2 stabilizing mutations. We further show that tumor-derived mutations in KEAP1 are hypomorphic with respect to NRF2 inhibition and that DPP3 overexpression in the presence of these mutants further promotes NRF2 activation. -
Expression and Mutational Analyses of the Human MAD2L1 Gene in Breast Cancer Cells
GENES,CHROMOSOMES&CANCER29:356–362(2000) BRIEFCOMMUNICATION ExpressionandMutationalAnalysesoftheHuman MAD2L1GeneinBreastCancerCells MelanieJ.Percy,1 KenuteA.Myrie,2 ChristopherK.Neeley,1 JamesN.Azim,1 StephenP.Ethier,3 and ElizabethM.Petty1,2* 1DepartmentofInternalMedicine,UniversityofMichiganMedicalCenter,AnnArbor,Michigan 2DepartmentofHumanGenetics,UniversityofMichiganMedicalCenter,AnnArbor,Michigan 3DepartmentofRadiationOncology,UniversityofMichiganComprehensiveCancerCenter,AnnArbor,Michigan Breastcancerisaheterogeneousdisorderinwhichmosttumorsdisplaysomedegreeofaneuploidy,especiallythoseatlater stagesofthedisease.Aneuploidyandassociatedchromosomeinstabilitymaybeimportantintheprogressionofmammary tumorigenesis.Aneuploidyispreventedduringnormalcelldivisioninpartthroughregulationofamitoticspindlecheckpoint wheremitoticarrestpreventssegregationofmisalignedchromosomesintodaughtercellsatanaphase.Mitoticarrestgenes, includingtheMADfamily,whichwasoriginallycharacterizedinyeast,helpregulatenormalfunctionofthemitoticspindle checkpoint.DecreasedexpressionofthehumangeneMAD2L1waspreviouslyreportedinabreastcancercelllineexhibiting chromosomeinstabilityandaneuploidy.ToexplorefurtherthepotentialroleofMAD2L1inbreastcancer,weanalyzed MAD2L1geneexpressionin13minimallytogrosslyaneuploidhumanbreastcancercelllinesandfoundsignificantdifferences ofexpressioninthreelines.SequenceanalysisofMAD2L1cDNAintheseaswellasnineadditionalaneuploidbreastcancer andfiveimmortalizednormalhumanmammaryepithelialcelllinesrevealedoneheterozygousframeshift(572delA)mutation inacancercelllinethatdemonstratedahighleveloftranscriptexpression.Inaddition,two3ЈUTRsequencevariantswere -
Shieldin Complex Promotes DNA End-Joining and Counters Homologous Recombination in BRCA1-Null Cells
This is a repository copy of Shieldin complex promotes DNA end-joining and counters homologous recombination in BRCA1-null cells. White Rose Research Online URL for this paper: http://eprints.whiterose.ac.uk/136933/ Version: Accepted Version Article: Dev, H, Chiang, T-WW, Lescale, C et al. (27 more authors) (2018) Shieldin complex promotes DNA end-joining and counters homologous recombination in BRCA1-null cells. Nature Cell Biology, 20. pp. 954-965. ISSN 1465-7392 https://doi.org/10.1038/s41556-018-0140-1 © 2018 Springer Nature Limited. This is an author produced version of a paper published in Nature Cell Biology. Uploaded in accordance with the publisher's self-archiving policy. Reuse Items deposited in White Rose Research Online are protected by copyright, with all rights reserved unless indicated otherwise. They may be downloaded and/or printed for private study, or other acts as permitted by national copyright laws. The publisher or other rights holders may allow further reproduction and re-use of the full text version. This is indicated by the licence information on the White Rose Research Online record for the item. Takedown If you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing [email protected] including the URL of the record and the reason for the withdrawal request. [email protected] https://eprints.whiterose.ac.uk/ 1 Shieldin complex promotes DNA end-joining and counters 2 homologous recombination in BRCA1-null cells 3 4 Harveer Dev1,2, Ting-Wei Will Chiang1Y, Chloe Lescale3Y, Inge de Krijger4Y, Alistair G. -
MAD1 (MAD1L1) (NM 003550) Human Tagged ORF Clone Lentiviral Particle Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for RC203471L4V MAD1 (MAD1L1) (NM_003550) Human Tagged ORF Clone Lentiviral Particle Product data: Product Type: Lentiviral Particles Product Name: MAD1 (MAD1L1) (NM_003550) Human Tagged ORF Clone Lentiviral Particle Symbol: MAD1L1 Synonyms: MAD1; PIG9; TP53I9; TXBP181 Vector: pLenti-C-mGFP-P2A-Puro (PS100093) ACCN: NM_003550 ORF Size: 2154 bp ORF Nucleotide The ORF insert of this clone is exactly the same as(RC203471). Sequence: OTI Disclaimer: The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info OTI Annotation: This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. RefSeq: NM_003550.2 RefSeq Size: 2754 bp RefSeq ORF: 2157 bp Locus ID: 8379 UniProt ID: Q9Y6D9 Protein Families: Druggable Genome Protein Pathways: Cell cycle MW: 83.1 kDa This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 2 MAD1 (MAD1L1) (NM_003550) Human Tagged ORF Clone Lentiviral Particle – RC203471L4V Gene Summary: MAD1L1 is a component of the mitotic spindle-assembly checkpoint that prevents the onset of anaphase until all chromosome are properly aligned at the metaphase plate.