Supplementary Information Method CLEAR-CLIP. Mouse Keratinocytes
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Original Article Upregulation of HOXA13 As a Potential Tumorigenesis and Progression Promoter of LUSC Based on Qrt-PCR and Bioinformatics
Int J Clin Exp Pathol 2017;10(10):10650-10665 www.ijcep.com /ISSN:1936-2625/IJCEP0065149 Original Article Upregulation of HOXA13 as a potential tumorigenesis and progression promoter of LUSC based on qRT-PCR and bioinformatics Rui Zhang1*, Yun Deng1*, Yu Zhang1, Gao-Qiang Zhai1, Rong-Quan He2, Xiao-Hua Hu2, Dan-Ming Wei1, Zhen-Bo Feng1, Gang Chen1 Departments of 1Pathology, 2Medical Oncology, First Affiliated Hospital of Guangxi Medical University, Nanning, Guangxi Zhuang Autonomous Region, China. *Equal contributors. Received September 7, 2017; Accepted September 29, 2017; Epub October 1, 2017; Published October 15, 2017 Abstract: In this study, we investigated the levels of homeobox A13 (HOXA13) and the mechanisms underlying the co-expressed genes of HOXA13 in lung squamous cancer (LUSC), the signaling pathways in which the co-ex- pressed genes of HOXA13 are involved and their functional roles in LUSC. The clinical significance of 23 paired LUSC tissues and adjacent non-tumor tissues were gathered. HOXA13 levels in LUSC were detected by quantita- tive real-time polymerase chain reaction (qRT-PCR). HOXA13 levels in LUSC from The Cancer Genome Atlas (TCGA) and Oncomine were analyzed. We performed receiver operator characteristic (ROC) curves of various clinicopath- ological features of LUSC. Co-expressed of HOXA13 were collected from MEM, cBioPortal and GEPIA. The func- tions and pathways of the most reliable overlapped genes were achieved from the Gene Otology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) databases, respectively. The protein-protein interaction (PPI) net- works were mapped using STRING. HOXA13 in LUSC were markedly upregulated compared with those in the non- cancerous controls as demonstrated by qRT-PCR (LUSC: 0.330±0.360; CONTROLS: 0.155±0.142; P=0.021). -
Pathway-Specific Dopaminergic Deficits in a Mouse Model of Angelman Syndrome
Pathway-specific dopaminergic deficits in a mouse model of Angelman syndrome Thorfinn T. Riday, … , Benjamin D. Philpot, C.J. Malanga J Clin Invest. 2012;122(12):4544-4554. https://doi.org/10.1172/JCI61888. Research Article Neuroscience Angelman syndrome (AS) is a neurodevelopmental disorder caused by maternal deletions or mutations of the ubiquitin ligase E3A (UBE3A) allele and characterized by minimal verbal communication, seizures, and disorders of voluntary movement. Previous studies have suggested that abnormal dopamine neurotransmission may underlie some of these deficits, but no effective treatment currently exists for the core features of AS. A clinical trial of levodopa (l-DOPA) in AS is ongoing, although the underlying rationale for this treatment strategy has not yet been thoroughly examined in preclinical models. We found that AS model mice lacking maternal Ube3a (Ube3am–/p+ mice) exhibit behavioral deficits that correlated with abnormal dopamine signaling. These deficits were not due to loss of dopaminergic neurons or impaired dopamine synthesis. Unexpectedly, Ube3am–/p+ mice exhibited increased dopamine release in the mesolimbic pathway while also exhibiting a decrease in dopamine release in the nigrostriatal pathway, as measured with fast-scan cyclic voltammetry. These findings demonstrate the complex effects of UBE3A loss on dopamine signaling in subcortical motor pathways that may inform ongoing clinical trials of l-DOPA therapy in patients with AS. Find the latest version: https://jci.me/61888/pdf Research article Pathway-specific dopaminergic deficits in a mouse model of Angelman syndrome Thorfinn T. Riday,1,2 Elyse C. Dankoski,1 Michael C. Krouse,3 Eric W. Fish,3 Paul L. -
Focus on Cdc42 in Breast Cancer: New Insights, Target Therapy Development and Non-Coding Rnas
Review Focus on Cdc42 in Breast Cancer: New Insights, Target Therapy Development and Non-Coding RNAs Yu Zhang †, Jun Li †, Xing-Ning Lai, Xue-Qiao Jiao, Jun-Ping Xiong and Li-Xia Xiong * Department of Pathophysiology, Jiangxi Province Key Laboratory of Tumor Pathogenesis and Molecular Pathology, Medical College, Nanchang University, 461 Bayi Road, Nanchang 330006, China; [email protected] (Y.Z.); [email protected] (J.L.); [email protected] (X.-N.L.); [email protected] (X.-Q.J.); [email protected] (J.-P.X.) * Correspondence: [email protected]; Tel.: +86-791-8636-0556 † These authors contributed equally to this work. Received: 30 December 2018; Accepted: 8 February 2019; Published: 11 February 2019 Abstract: Breast cancer is the most common malignant tumors in females. Although the conventional treatment has demonstrated a certain effect, some limitations still exist. The Rho guanosine triphosphatase (GTPase) Cdc42 (Cell division control protein 42 homolog) is often upregulated by some cell surface receptors and oncogenes in breast cancer. Cdc42 switches from inactive guanosine diphosphate (GDP)-bound to active GTP-bound though guanine-nucleotide- exchange factors (GEFs), results in activation of signaling cascades that regulate various cellular processes such as cytoskeletal changes, proliferation and polarity establishment. Targeting Cdc42 also provides a strategy for precise breast cancer therapy. In addition, Cdc42 is a potential target for several types of non-coding RNAs including microRNAs and lncRNAs. These non-coding RNAs is extensively involved in Cdc42-induced tumor processes, while many of them are aberrantly expressed. Here, we focus on the role of Cdc42 in cell morphogenesis, proliferation, motility, angiogenesis and survival, introduce the Cdc42-targeted non-coding RNAs, as well as present current development of effective Cdc42-targeted inhibitors in breast cancer. -
CBL Mutations in Myeloproliferative Neoplasms Are Also Found in the Gene’S Proline-Rich Domain and in Patients with the V617FJAK2
Articles and Brief Reports Chronic Myeloproliferative Disorders CBL mutations in myeloproliferative neoplasms are also found in the gene’s proline-rich domain and in patients with the V617FJAK2 Paula Aranaz,1 Cristina Hurtado,1 Ignacio Erquiaga,1 Itziar Miguéliz,1 Cristina Ormazábal,1 Ion Cristobal,2 Marina García-Delgado,1 Francisco Javier Novo,1 and José Luis Vizmanos1 1Department of Genetics, School of Sciences, University of Navarra, Pamplona; and 2CIMA, Center for Applied Medical Research, University of Navarra, Pamplona, Spain ABSTRACT Funding: this work was funded Background with the help of the Spanish Despite the discovery of the p.V617F in JAK2, the molecular pathogenesis of some chronic myelo- Ministry of Science and Innovation proliferative neoplasms remains unclear. Although very rare, different studies have identified CBL (SAF 2007-62473), the PIUNA (Cas-Br-Murine ecotropic retroviral transforming sequence) mutations in V617FJAK2-negative Program of the University of patients, mainly located in the RING finger domain. In order to determine the frequency of CBL Navarra, the Caja Navarra Foundation through the Program mutations in these diseases, we studied different regions of all CBL family genes (CBL, CBLB and “You choose, you decide” (Project CBLC) in a selected group of patients with myeloproliferative neoplasms. We also included 10.830) and ISCIII-RTICC V617FJAK2-positive patients to check whether mutations in CBL and JAK2 are mutually exclusive (RD06/0020/0078). events. PA received a predoctoral grant from the Government of Navarra. Design and Methods Using denaturing high performance liquid chromatography, we screened for mutations in CBL, Manuscript received on CBLB and CBLC in a group of 172 V617FJAK2-negative and 232 V617FJAK2-positive patients July 26, 2011. -
XIAP's Profile in Human Cancer
biomolecules Review XIAP’s Profile in Human Cancer Huailu Tu and Max Costa * Department of Environmental Medicine, Grossman School of Medicine, New York University, New York, NY 10010, USA; [email protected] * Correspondence: [email protected] Received: 16 September 2020; Accepted: 25 October 2020; Published: 29 October 2020 Abstract: XIAP, the X-linked inhibitor of apoptosis protein, regulates cell death signaling pathways through binding and inhibiting caspases. Mounting experimental research associated with XIAP has shown it to be a master regulator of cell death not only in apoptosis, but also in autophagy and necroptosis. As a vital decider on cell survival, XIAP is involved in the regulation of cancer initiation, promotion and progression. XIAP up-regulation occurs in many human diseases, resulting in a series of undesired effects such as raising the cellular tolerance to genetic lesions, inflammation and cytotoxicity. Hence, anti-tumor drugs targeting XIAP have become an important focus for cancer therapy research. RNA–XIAP interaction is a focus, which has enriched the general profile of XIAP regulation in human cancer. In this review, the basic functions of XIAP, its regulatory role in cancer, anti-XIAP drugs and recent findings about RNA–XIAP interactions are discussed. Keywords: XIAP; apoptosis; cancer; therapeutics; non-coding RNA 1. Introduction X-linked inhibitor of apoptosis protein (XIAP), also known as inhibitor of apoptosis protein 3 (IAP3), baculoviral IAP repeat-containing protein 4 (BIRC4), and human IAPs like protein (hILP), belongs to IAP family which was discovered in insect baculovirus [1]. Eight different IAPs have been isolated from human tissues: NAIP (BIRC1), BIRC2 (cIAP1), BIRC3 (cIAP2), XIAP (BIRC4), BIRC5 (survivin), BIRC6 (apollon), BIRC7 (livin) and BIRC8 [2]. -
Type of the Paper (Article
Supplementary Material A Proteomics Study on the Mechanism of Nutmeg-induced Hepatotoxicity Wei Xia 1, †, Zhipeng Cao 1, †, Xiaoyu Zhang 1 and Lina Gao 1,* 1 School of Forensic Medicine, China Medical University, Shenyang 110122, P. R. China; lessen- [email protected] (W.X.); [email protected] (Z.C.); [email protected] (X.Z.) † The authors contributed equally to this work. * Correspondence: [email protected] Figure S1. Table S1. Peptide fraction separation liquid chromatography elution gradient table. Time (min) Flow rate (mL/min) Mobile phase A (%) Mobile phase B (%) 0 1 97 3 10 1 95 5 30 1 80 20 48 1 60 40 50 1 50 50 53 1 30 70 54 1 0 100 1 Table 2. Liquid chromatography elution gradient table. Time (min) Flow rate (nL/min) Mobile phase A (%) Mobile phase B (%) 0 600 94 6 2 600 83 17 82 600 60 40 84 600 50 50 85 600 45 55 90 600 0 100 Table S3. The analysis parameter of Proteome Discoverer 2.2. Item Value Type of Quantification Reporter Quantification (TMT) Enzyme Trypsin Max.Missed Cleavage Sites 2 Precursor Mass Tolerance 10 ppm Fragment Mass Tolerance 0.02 Da Dynamic Modification Oxidation/+15.995 Da (M) and TMT /+229.163 Da (K,Y) N-Terminal Modification Acetyl/+42.011 Da (N-Terminal) and TMT /+229.163 Da (N-Terminal) Static Modification Carbamidomethyl/+57.021 Da (C) 2 Table S4. The DEPs between the low-dose group and the control group. Protein Gene Fold Change P value Trend mRNA H2-K1 0.380 0.010 down Glutamine synthetase 0.426 0.022 down Annexin Anxa6 0.447 0.032 down mRNA H2-D1 0.467 0.002 down Ribokinase Rbks 0.487 0.000 -
Small Rho Gtpase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis
University of Denver Digital Commons @ DU Electronic Theses and Dissertations Graduate Studies 1-1-2017 Small Rho GTPase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis Noelle Christine Punessen University of Denver Follow this and additional works at: https://digitalcommons.du.edu/etd Part of the Biology Commons, and the Genetics and Genomics Commons Recommended Citation Punessen, Noelle Christine, "Small Rho GTPase Family Member Cdc42 and Its Role in Neuronal Survival and Apoptosis" (2017). Electronic Theses and Dissertations. 1337. https://digitalcommons.du.edu/etd/1337 This Thesis is brought to you for free and open access by the Graduate Studies at Digital Commons @ DU. It has been accepted for inclusion in Electronic Theses and Dissertations by an authorized administrator of Digital Commons @ DU. For more information, please contact [email protected],[email protected]. Small Rho GTPase Family Member Cdc42 and its Role in Neuronal Survival and Apoptosis A Thesis Presented to the Faculty of Natural Sciences and Mathematics University of Denver In Partial Fulfillment of the Requirements for the Degree Master of Science by Noelle C. Punessen August 2017 Advisor: Dr. Daniel A. Linseman Author: Noelle C. Punessen Title: Small Rho GTPase Family Member Cdc42 and its Role in Neuronal Survival and Apoptosis Advisor: Dr. Daniel A. Linseman Degree Date: August 2017 Abstract Neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), Alzheimer’s and Parkinson’s disease are caused by a progressive and aberrant destruction of neurons in the brain and spinal cord. These disorders lack effective long term treatments, and existing options focus primarily on either delaying disease onset or alleviating symptomology. -
Transcriptomic Profile Induced in Bone Marrow Mesenchymal Stromal Cells After Interaction with Multiple Myeloma Cells
www.impactjournals.com/oncotarget/ Oncotarget, Vol. 5, No. 18 Transcriptomic profile induced in bone marrow mesenchymal stromal cells after interaction with multiple myeloma cells: implications in myeloma progression and myeloma bone disease Antonio Garcia-Gomez1,2,3, Javier De Las Rivas1, Enrique M. Ocio1,2, Elena Díaz- Rodríguez1, Juan C. Montero1, Montserrat Martín1,3, Juan F. Blanco2, Fermín M. Sanchez-Guijo2,3, Atanasio Pandiella1,2, Jesús F. San Miguel1,2,3 and Mercedes Garayoa1,2,3 1 Centro de Investigación del Cáncer, IBMCC (Universidad de Salamanca-CSIC), Salamanca, Spain 2 Hospital Universitario de Salamanca-IBSAL, Salamanca, Spain 3 Centro en Red de Medicina Regenerativa y Terapia Celular de Castilla y León, Salamanca, Spain Correspondence to: Mercedes Garayoa, email: [email protected] Keywords: multiple myeloma, bone marrow mesenchymal stromal cells, tumor-stroma interactions, gene expression profiling, co- culture techniques, myeloma bone disease Received: January 6, 2014 Accepted: June 2, 2014 Published: June 4, 2014 This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ABSTRACT Despite evidence about the implication of the bone marrow (BM) stromal microenvironment in multiple myeloma (MM) cell growth and survival, little is known about the effects of myelomatous cells on BM stromal cells. Mesenchymal stromal cells (MSCs) from healthy donors (dMSCs) or myeloma patients (pMSCs) were co- cultured with the myeloma cell line MM.1S, and the transcriptomic profile of MSCs induced by this interaction was analyzed. Deregulated genes after co-culture common to both d/pMSCs revealed functional involvement in tumor microenvironment cross- talk, myeloma growth induction and drug resistance, angiogenesis and signals for osteoclast activation and osteoblast inhibition. -
Under Serratia Marcescens Treatment Kai Feng1,2, Xiaoyu Lu1,2, Jian Luo1,2 & Fang Tang1,2*
www.nature.com/scientificreports OPEN SMRT sequencing of the full‑length transcriptome of Odontotermes formosanus (Shiraki) under Serratia marcescens treatment Kai Feng1,2, Xiaoyu Lu1,2, Jian Luo1,2 & Fang Tang1,2* Odontotermes formosanus (Shiraki) is an important pest in the world. Serratia marcescens have a high lethal efect on O. formosanus, but the specifc insecticidal mechanisms of S. marcescens on O. formosanus are unclear, and the immune responses of O. formosanus to S. marcescens have not been clarifed. At present, genetic database resources of O. formosanus are extremely scarce. Therefore, using O. formosanus workers infected by S. marcescens and the control as experimental materials, a full-length transcriptome was sequenced using the PacBio Sequel sequencing platform. A total of 10,364 isoforms were obtained as the fnal transcriptome. The unigenes were further annotated with the Nr, Swiss-Prot, EuKaryotic Orthologous Groups (KOG), Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) Ortholog public databases. In a comparison between the control group and a Serratia marcescens-infected group, a total of 259 diferentially expressed genes (DEGs) were identifed, including 132 upregulated and 127 downregulated genes. Pathway enrichment analysis indicated that the expression of the mitogen-activated protein kinase (MAPK) pathway, oxidative stress genes and the AMP-activated protein kinase (AMPK) pathway in O. formosanus may be associated with S. marcescens treatment. This research intensively studied O. formosanus at the high-throughput full-length transcriptome level, laying a foundation for further development of molecular markers and mining of target genes in this species and thereby promoting the biological control of O. -
Anti-CBLB Antibody (ARG57312)
Product datasheet [email protected] ARG57312 Package: 100 μl anti-CBLB antibody Store at: -20°C Summary Product Description Rabbit Polyclonal antibody recognizes CBLB Tested Reactivity Hu, Ms Tested Application IHC-P, WB Host Rabbit Clonality Polyclonal Isotype IgG Target Name CBLB Antigen Species Human Immunogen Recombinant Protein of Human CBLB. Conjugation Un-conjugated Alternate Names Nbla00127; EC 6.3.2.-; RNF56; Signal transduction protein CBL-B; Casitas B-lineage lymphoma proto- oncogene b; SH3-binding protein CBL-B; Cbl-b; E3 ubiquitin-protein ligase CBL-B; RING finger protein 56 Application Instructions Application table Application Dilution IHC-P 1:50 - 1:200 WB 1:500 - 1:2000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Positive Control Jurkat Calculated Mw 109 kDa Properties Form Liquid Purification Affinity purification with immunogen. Buffer PBS (pH 7.3), 0.02% Sodium azide and 50% Glycerol. Preservative 0.02% Sodium azide Stabilizer 50% Glycerol Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. Note For laboratory research only, not for drug, diagnostic or other use. www.arigobio.com 1/2 Bioinformation Gene Symbol CBLB Gene Full Name Cbl proto-oncogene B, E3 ubiquitin protein ligase Function E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. -
The PRKCI and SOX2 Oncogenes Are Coamplified and Cooperate to Activate Hedgehog Signaling in Lung Squamous Cell Carcinoma
Cancer Cell Article The PRKCI and SOX2 Oncogenes Are Coamplified and Cooperate to Activate Hedgehog Signaling in Lung Squamous Cell Carcinoma Verline Justilien,1 Michael P. Walsh,1 Syed A. Ali,1 E. Aubrey Thompson,1 Nicole R. Murray,1 and Alan P. Fields1,* 1Department of Cancer Biology, Mayo Clinic Cancer Center, Jacksonville, FL 32224, USA *Correspondence: fi[email protected] http://dx.doi.org/10.1016/j.ccr.2014.01.008 SUMMARY We report that two oncogenes coamplified on chromosome 3q26, PRKCI and SOX2, cooperate to drive a stem-like phenotype in lung squamous cell carcinoma (LSCC). Protein kinase Ci (PKCi) phosphorylates SOX2, a master transcriptional regulator of stemness, and recruits it to the promoter of Hedgehog (Hh) acyltransferase (HHAT) that catalyzes the rate-limiting step in Hh ligand production. PKCi-mediated SOX2 phosphorylation is required for HHAT promoter occupancy, HHAT expression, and maintenance of a stem-like phenotype. Primary LSCC tumors coordinately overexpress PKCi, SOX2, and HHAT and require PKCi-SOX2-HHAT signaling to maintain a stem-like phenotype. Thus, PKCi and SOX2 are genetically, biochemically, and functionally linked in LSCC, and together they drive tumorigenesis by establishing a cell-autonomous Hh signaling axis. INTRODUCTION Similar cell populations exist in several cancer types (Chen et al., 2012; Driessens et al., 2012; Schepers et al., 2012). Line- Lung cancer is the major cause of cancer death, with a 5-year- age tracing reveals these cells clonally expand to give rise to survival rate of 16% (Siegel et al., 2012). Non-small cell lung malignant and nonmalignant, differentiated cell types. -
The Autism Protein Ube3a/E6AP Remodels Neuronal Dendritic Arborization Via Caspase-Dependent Microtubule Destabilization
The Journal of Neuroscience, January 10, 2018 • 38(2):363–378 • 363 Neurobiology of Disease The Autism Protein Ube3A/E6AP Remodels Neuronal Dendritic Arborization via Caspase-Dependent Microtubule Destabilization Natasha Khatri,1,2 James P. Gilbert,1 Yuda Huo,1 Roozhin Sharaflari,1 Michael Nee,1 Hui Qiao,1 and XHeng-Ye Man1,2 1Department of Biology, Boston University, Boston, Massachusetts 02215, and 2Department of Pharmacology & Experimental Therapeutics, Boston University School of Medicine, Boston, Massachusetts 02118 UBE3A gene copy number variation and the resulting overexpression of the protein E6AP is directly linked to autism spectrum disorders (ASDs).However,theunderlyingcellularandmolecularneurobiologyremainslessclear.HerewereporttheroleofASD-relatedincreased dosage of Ube3A/E6AP in dendritic arborization during brain development. We show that increased E6AP expression in primary cul- tured neurons leads to a reduction in dendritic branch number and length. The E6AP-dependent remodeling of dendritic arborization results from retraction of dendrites by thinning and fragmentation at the tips of dendrite branches, leading to shortening or removal of dendrites. This remodeling effect is mediated by the ubiquitination and degradation of XIAP (X-linked inhibitors of aptosis protein) by E6AP, which leads to activation of caspase-3 and cleavage of microtubules. In vivo, male and female Ube3A 2X ASD mice show decreased XIAP levels, increased caspase-3 activation, and elevated levels of tubulin cleavage. Consistently, dendritic branching and spine density are reduced in cortical neurons of Ube3A 2X ASD mice. In revealing an important role for Ube3A/E6AP in ASD-related developmental alteration in dendritic arborization and synapse formation, our findings provide new insights into the pathogenesis of Ube3A/E6AP- dependent ASD.