BNIP3L/Nix Antibody A
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Endoplasmic Reticulum–Mitochondria Crosstalk in NIX-Mediated Murine Cell Death Abhinav Diwan Washington University School of Medicine in St
Washington University School of Medicine Digital Commons@Becker ICTS Faculty Publications Institute of Clinical and Translational Sciences 2009 Endoplasmic reticulum–mitochondria crosstalk in NIX-mediated murine cell death Abhinav Diwan Washington University School of Medicine in St. Louis Scot J. Matkovich Washington University School of Medicine in St. Louis Qunying Yuan University of Cincinnati Wen Zhao University of Cincinnati Atsuko Yatani University of Medicine and Dentistry of New Jersey See next page for additional authors Follow this and additional works at: https://digitalcommons.wustl.edu/icts_facpubs Recommended Citation Diwan, Abhinav; Matkovich, Scot J.; Yuan, Qunying; Zhao, Wen; Yatani, Atsuko; Brown, Joan Heller; Molkentin, Jeffery D.; Kranias, Evangelia G.; and Dorn, Gerald W. II, "Endoplasmic reticulum–mitochondria crosstalk in NIX-mediated murine cell death". Journal of Clinical Investigation, 203-212. 2009. Paper 4. https://digitalcommons.wustl.edu/icts_facpubs/4 This Article is brought to you for free and open access by the Institute of Clinical and Translational Sciences at Digital Commons@Becker. It has been accepted for inclusion in ICTS Faculty Publications by an authorized administrator of Digital Commons@Becker. For more information, please contact [email protected]. Authors Abhinav Diwan, Scot J. Matkovich, Qunying Yuan, Wen Zhao, Atsuko Yatani, Joan Heller Brown, Jeffery D. Molkentin, Evangelia G. Kranias, and Gerald W. Dorn II This article is available at Digital Commons@Becker: https://digitalcommons.wustl.edu/icts_facpubs/4 Research article Endoplasmic reticulum–mitochondria crosstalk in NIX-mediated murine cell death Abhinav Diwan,1 Scot J. Matkovich,1 Qunying Yuan,2 Wen Zhao,2 Atsuko Yatani,3 Joan Heller Brown,4 Jeffery D. -
Dimerization of Mitophagy Receptor BNIP3L/NIX Is Essential for Recruitment of Autophagic Machinery
Autophagy ISSN: 1554-8627 (Print) 1554-8635 (Online) Journal homepage: https://www.tandfonline.com/loi/kaup20 Dimerization of mitophagy receptor BNIP3L/NIX is essential for recruitment of autophagic machinery Mija Marinković, Matilda Šprung & Ivana Novak To cite this article: Mija Marinković, Matilda Šprung & Ivana Novak (2020): Dimerization of mitophagy receptor BNIP3L/NIX is essential for recruitment of autophagic machinery, Autophagy, DOI: 10.1080/15548627.2020.1755120 To link to this article: https://doi.org/10.1080/15548627.2020.1755120 View supplementary material Accepted author version posted online: 14 Apr 2020. Published online: 24 Apr 2020. Submit your article to this journal Article views: 69 View related articles View Crossmark data Full Terms & Conditions of access and use can be found at https://www.tandfonline.com/action/journalInformation?journalCode=kaup20 AUTOPHAGY https://doi.org/10.1080/15548627.2020.1755120 RESEARCH PAPER Dimerization of mitophagy receptor BNIP3L/NIX is essential for recruitment of autophagic machinery Mija Marinković a, Matilda Šprung b, and Ivana Novak a aSchool of Medicine, University of Split, Split, Croatia; bFaculty of Science, University of Split, Split, Croatia ABSTRACT ARTICLE HISTORY Mitophagy is a conserved intracellular catabolic process responsible for the selective removal of Received 8 August 2019 dysfunctional or superfluous mitochondria to maintain mitochondrial quality and need in cells. Here, Revised 31 March 2020 we examine the mechanisms of receptor-mediated mitophagy activation, with the focus on BNIP3L/NIX Accepted 2 April 2020 mitophagy receptor, proven to be indispensable for selective removal of mitochondria during the KEYWORDS terminal differentiation of reticulocytes. The molecular mechanisms of selecting damaged mitochondria Autophagy; dimerization; from healthy ones are still very obscure. -
Datasheet: AHP1885 Product Details
Datasheet: AHP1885 Description: RABBIT ANTI HUMAN BNIP3L Specificity: BNIP3L Format: Purified Product Type: Polyclonal Antibody Isotype: Polyclonal IgG Quantity: 0.1 mg 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 Immunohistology - Paraffin (1) 2ug/ml Western Blotting 1ug/ml Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls. (1)This product requires antigen retrieval using heat treatment prior to staining of paraffin sections.Sodium citrate buffer pH 6.0 is recommended for this purpose. Target Species Human Species Cross Based on sequence similarity, is expected to react with:Mouse Reactivity N.B. Antibody reactivity and working conditions may vary between species. Product Form Purified IgG - liquid Antiserum Preparation Antiserum to human BNIP3L was raised by repeated immunisation of rabbits with highly purified antigen. Purified IgG was prepared from whole serum by affinity chromatography. Buffer Solution Phosphate buffered saline Preservative 0.02% Sodium Azide (NaN ) Stabilisers 3 Approx. Protein IgG concentration 0.5 mg/ml Concentrations Immunogen Synthetic peptide corresponding to the amino acids sequence 77 - 92 of human BNIP3L. -
Identification of Genes and Signaling Pathways Associated with the Pathogenesis of Juvenile Spondyloarthritis
MOLECULAR MEDICINE REPORTS 18: 1263-1270, 2018 Identification of genes and signaling pathways associated with the pathogenesis of juvenile spondyloarthritis ZHE WANG1,2*, YUDI HAN3*, ZHAOQING ZHANG4*, CUNFENG JIA4, QIANG ZHAO4, WEI SONG5, TAO CHEN6, YIFAN ZHANG7 and XIUHUI WANG8 1Department of Orthopedics, Zhongshan Hospital, Fudan University, Shanghai 200032; 2Department of Orthopedic Trauma, The First Affiliated Hospital of Dalian Medical University, Dalian, Liaoning 116011; 3Department of Plastic and Reconstructive Surgery, General Hospital of Chinese People's Liberation Army, Beijing 100853; 4Department of Spine Surgery, Zhangqiu People's Hospital, Jinan, Shandong 250200; 5School of Life Sciences, Shanghai University, Shanghai 200444; 6Department of Orthopedics, Fourth Hospital of Changsha, Changsha, Hunan 410006; 7Department of Rheumatism Immunity, People's Liberation Army General Hospital, Beijing 100700; 8Department of Orthopedics, Shanghai Zhoupu Hospital, Shanghai 201318, P.R. China Received October 19, 2017; Accepted February 20, 2018 DOI: 10.3892/mmr.2018.9136 Abstract. The aim of the present study was to identify key Introduction genes and signaling pathways associated with the pathogenesis of juvenile spondyloarthritis (JSA). The gene expression profile Spondyloarthritis (SpA) includes a group of immune-mediated dataset GSE58667, including data from 15 human whole blood inflammatory diseases with similar genetic and clinical mani- samples collected from 11 patients with JSA and four healthy festations, including ankylosing spondylitis (AS), psoriatic controls, was analyzed to identify differentially expressed genes arthritis (PsA) and juvenile SpA (JSA) (1,2). In particular, JSA (DEGs) associated with disease characteristics. Additionally, is a group of chronic inflammatory diseases associated with Gene Ontology term and Kyoto Encyclopedia of Genes and human leukocyte antigen B27, affecting children at ≤16 years Genomes pathway enrichment analyses of the DEGs were of age. -
Role and Regulation of the P53-Homolog P73 in the Transformation of Normal Human Fibroblasts
Role and regulation of the p53-homolog p73 in the transformation of normal human fibroblasts Dissertation zur Erlangung des naturwissenschaftlichen Doktorgrades der Bayerischen Julius-Maximilians-Universität Würzburg vorgelegt von Lars Hofmann aus Aschaffenburg Würzburg 2007 Eingereicht am Mitglieder der Promotionskommission: Vorsitzender: Prof. Dr. Dr. Martin J. Müller Gutachter: Prof. Dr. Michael P. Schön Gutachter : Prof. Dr. Georg Krohne Tag des Promotionskolloquiums: Doktorurkunde ausgehändigt am Erklärung Hiermit erkläre ich, dass ich die vorliegende Arbeit selbständig angefertigt und keine anderen als die angegebenen Hilfsmittel und Quellen verwendet habe. Diese Arbeit wurde weder in gleicher noch in ähnlicher Form in einem anderen Prüfungsverfahren vorgelegt. Ich habe früher, außer den mit dem Zulassungsgesuch urkundlichen Graden, keine weiteren akademischen Grade erworben und zu erwerben gesucht. Würzburg, Lars Hofmann Content SUMMARY ................................................................................................................ IV ZUSAMMENFASSUNG ............................................................................................. V 1. INTRODUCTION ................................................................................................. 1 1.1. Molecular basics of cancer .......................................................................................... 1 1.2. Early research on tumorigenesis ................................................................................. 3 1.3. Developing -
JNK and NF‑Κb Signaling Pathways Are Involved in Cytokine Changes in Patients with Congenital Heart Disease Prior to and After Transcatheter Closure
EXPERIMENTAL AND THERAPEUTIC MEDICINE 15: 1525-1531, 2018 JNK and NF‑κB signaling pathways are involved in cytokine changes in patients with congenital heart disease prior to and after transcatheter closure SHUNYANG FAN1*, KEFANG LI1*, DEYIN ZHANG2 and FUYUN LIU3 1Heart Center, The Third Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan 450052; 2Department of Internal Medicine, The Third People's Hospital of Henan Province, Zhengzhou, Henan 450000; 3Department of Pediatric Surgery, The Third Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan 450052, P.R. China Received December 15, 2016; Accepted August 26, 2017 DOI: 10.3892/etm.2017.5595 Abstract. Congenital heart disease (CHD) is a problem in the changes in cytokines, as well as their recovery following structure of the heart that is present at birth. Due to advances transcatheter closure treatment were associated with the in interventional cardiology, CHD may currently be without JNK and NF-κB signaling pathways. The present study may surgery. The present study aimed to explore the molecular provide further understanding of the underlying molecular mechanism underlying CHD. A total of 200 cases of CHD mechanisms in CHD and propose a potential novel target for treated by transcatheter closure as well as 200 controls were the treatment of CHD. retrospectively assessed. Serum cytokines prior to and after treatment were assessed by reverse-transcription quantitative Introduction polymerase chain reaction analysis. Furthermore, the levels of proteins associated with c-Jun N-terminal kinase (JNK) and Congenital heart disease (CHD), also known as a congenital nuclear factor (NF)-κB were assessed by western blot analysis heart anomaly, is a structural aberration of the heart that and immunohistochemistry. -
Bioinformatics Tools for the Analysis of Gene-Phenotype Relationships Coupled with a Next Generation Chip-Sequencing Data Processing Pipeline
Bioinformatics Tools for the Analysis of Gene-Phenotype Relationships Coupled with a Next Generation ChIP-Sequencing Data Processing Pipeline Erinija Pranckeviciene Thesis submitted to the Faculty of Graduate and Postdoctoral Studies in partial fulfillment of the requirements for the Doctorate in Philosophy degree in Cellular and Molecular Medicine Department of Cellular and Molecular Medicine Faculty of Medicine University of Ottawa c Erinija Pranckeviciene, Ottawa, Canada, 2015 Abstract The rapidly advancing high-throughput and next generation sequencing technologies facilitate deeper insights into the molecular mechanisms underlying the expression of phenotypes in living organisms. Experimental data and scientific publications following this technological advance- ment have rapidly accumulated in public databases. Meaningful analysis of currently avail- able data in genomic databases requires sophisticated computational tools and algorithms, and presents considerable challenges to molecular biologists without specialized training in bioinfor- matics. To study their phenotype of interest molecular biologists must prioritize large lists of poorly characterized genes generated in high-throughput experiments. To date, prioritization tools have primarily been designed to work with phenotypes of human diseases as defined by the genes known to be associated with those diseases. There is therefore a need for more prioritiza- tion tools for phenotypes which are not related with diseases generally or diseases with which no genes have yet been associated in particular. Chromatin immunoprecipitation followed by next generation sequencing (ChIP-Seq) is a method of choice to study the gene regulation processes responsible for the expression of cellular phenotypes. Among publicly available computational pipelines for the processing of ChIP-Seq data, there is a lack of tools for the downstream analysis of composite motifs and preferred binding distances of the DNA binding proteins. -
Activation of NIX-Mediated Mitophagy by an Interferon Regulatory Factor Homologue of Human Herpesvirus
ARTICLE https://doi.org/10.1038/s41467-019-11164-2 OPEN Activation of NIX-mediated mitophagy by an interferon regulatory factor homologue of human herpesvirus Mai Tram Vo 1, Barbara J. Smith2, John Nicholas1 & Young Bong Choi 1 Viral control of mitochondrial quality and content has emerged as an important mechanism for counteracting the host response to virus infection. Despite the knowledge of this crucial 1234567890():,; function of some viruses, little is known about how herpesviruses regulate mitochondrial homeostasis during infection. Human herpesvirus 8 (HHV-8) is an oncogenic virus causally related to AIDS-associated malignancies. Here, we show that HHV-8-encoded viral interferon regulatory factor 1 (vIRF-1) promotes mitochondrial clearance by activating mitophagy to support virus replication. Genetic interference with vIRF-1 expression or targeting to the mitochondria inhibits HHV-8 replication-induced mitophagy and leads to an accumulation of mitochondria. Moreover, vIRF-1 binds directly to a mitophagy receptor, NIX, on the mito- chondria and activates NIX-mediated mitophagy to promote mitochondrial clearance. Genetic and pharmacological interruption of vIRF-1/NIX-activated mitophagy inhibits HHV-8 pro- ductive replication. Our findings uncover an essential role of vIRF-1 in mitophagy activation and promotion of HHV-8 lytic replication via this mechanism. 1 Department of Oncology, Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA. 2 Department of Cell Biology, Institute -
BNIP3 and NIX Mediate Mieap-Induced Accumulation of Lysosomal Proteins Within Mitochondria
BNIP3 and NIX Mediate Mieap-Induced Accumulation of Lysosomal Proteins within Mitochondria Yasuyuki Nakamura, Noriaki Kitamura, Daisuke Shinogi, Masaki Yoshida, Olga Goda, Ryuya Murai, Hiroki Kamino, Hirofumi Arakawa* Division of Cancer Biology, National Cancer Center Research Institute, Tokyo, Japan Abstract Mieap, a p53-inducible protein, controls mitochondrial quality by repairing unhealthy mitochondria. During repair, Mieap induces the accumulation of intramitochondrial lysosomal proteins (designated MALM for Mieap-induced accumulation of lysosome-like organelles within mitochondria) by interacting with NIX, leading to the elimination of oxidized mitochondrial proteins. Here, we report that an additional mitochondrial outer membrane protein, BNIP3, is also involved in MALM. BNIP3 interacts with Mieap in a reactive oxygen species (ROS)-dependent manner via the BH3 domain of BNIP3 and the coiled-coil domains of Mieap. The knockdown of endogenous BNIP3 expression severely inhibited MALM. Although the overexpression of either BNIP3 or NIX did not cause a remarkable change in the mitochondrial membrane potential (MMP), the co- expression of all three exogenous proteins, Mieap, BNIP3 and NIX, caused a dramatic reduction in MMP, implying that the physical interaction of Mieap, BNIP3 and NIX at the mitochondrial outer membrane may regulate the opening of a pore in the mitochondrial double membrane. This effect was not related to cell death. These results suggest that two mitochondrial outer membrane proteins, BNIP3 and NIX, mediate MALM in order to maintain mitochondrial integrity. The physical interaction of Mieap, BNIP3 and NIX at the mitochondrial outer membrane may play a critical role in the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. -
A Cluster of Cooperating Tumor-Suppressor Gene Candidates in Chromosomal Deletions
A cluster of cooperating tumor-suppressor gene candidates in chromosomal deletions Wen Xuea,1,2, Thomas Kitzinga,1,3, Stephanie Roesslerb, Johannes Zubera, Alexander Krasnitza, Nikolaus Schultzc, Kate Revilla, Susann Weissmuellerd,3, Amy R. Rappaporta, Janelle Simona,e,3, Jack Zhanga, Weijun Luoa, James Hicksa, Lars Zendera,4, Xin Wei Wangb, Scott Powersa, Michael Wiglera,5, and Scott W. Lowea,e,3,5 aCold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724; bLaboratory of Human Carcinogenesis, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892; cComputational Biology Center, Memorial Sloan-Kettering Cancer Center, New York, NY 10065; dWatson School of Biological Sciences, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724; and eHoward Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10065 Contributed by Michael Wigler, April 12, 2012 (sent for review January 13, 2012) The large chromosomal deletions frequently observed in cancer the extent of chromosome 8p deletions from cancer genome genomes are often thought to arise as a “two-hit” mechanism in the datasets derived from array-based comparative genomic hybrid- process of tumor-suppressor gene (TSG) inactivation. Using a murine ization (aCGH) performed at Cold Spring Harbor Laboratory and model system of hepatocellular carcinoma (HCC) and in vivo RNAi, the Cancer Genome Atlas (TCGA) project, totaling 1411 primary we test an alternative hypothesis, that such deletions can arise from tumor samples and cell lines of HCC and breast, colon, and lung selective pressure to attenuate the activity of multiple genes. By cancers (Fig. 1A and Materials and Methods). According to these targeting the mouse orthologs of genes frequently deleted on hu- data, approximately half of these tumors harbor heterozygous man 8p22 and adjacent regions, which are lost in approximately deletions of human chromosome 8p, often encompassing a large half of several other major epithelial cancers, we provide evidence portion of or even the entire chromosome arm (Fig. -
HYPOXIA MEDIATED DOWNREGULATION of MIRNA BIOGENESIS LEADS to INCREASED TUMOR PROGRESSION Rajesha Rupaimoole
The Texas Medical Center Library DigitalCommons@TMC The University of Texas MD Anderson Cancer Center UTHealth Graduate School of The University of Texas MD Anderson Cancer Biomedical Sciences Dissertations and Theses Center UTHealth Graduate School of (Open Access) Biomedical Sciences 12-2014 HYPOXIA MEDIATED DOWNREGULATION OF MIRNA BIOGENESIS LEADS TO INCREASED TUMOR PROGRESSION rajesha rupaimoole Follow this and additional works at: https://digitalcommons.library.tmc.edu/utgsbs_dissertations Part of the Medicine and Health Sciences Commons Recommended Citation rupaimoole, rajesha, "HYPOXIA MEDIATED DOWNREGULATION OF MIRNA BIOGENESIS LEADS TO INCREASED TUMOR PROGRESSION" (2014). The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access). 527. https://digitalcommons.library.tmc.edu/utgsbs_dissertations/527 This Dissertation (PhD) is brought to you for free and open access by the The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences at DigitalCommons@TMC. It has been accepted for inclusion in The University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences Dissertations and Theses (Open Access) by an authorized administrator of DigitalCommons@TMC. For more information, please contact [email protected]. HYPOXIA MEDIATED DOWNREGULATION OF MIRNA BIOGENESIS LEADS TO INCREASED TUMOR PROGRESSION By Rajesha Rupaimoole, M.S. APPROVED: ______________________________ Anil K. Sood, -
Oxidized Phospholipids Regulate Amino Acid Metabolism Through MTHFD2 to Facilitate Nucleotide Release in Endothelial Cells
ARTICLE DOI: 10.1038/s41467-018-04602-0 OPEN Oxidized phospholipids regulate amino acid metabolism through MTHFD2 to facilitate nucleotide release in endothelial cells Juliane Hitzel1,2, Eunjee Lee3,4, Yi Zhang 3,5,Sofia Iris Bibli2,6, Xiaogang Li7, Sven Zukunft 2,6, Beatrice Pflüger1,2, Jiong Hu2,6, Christoph Schürmann1,2, Andrea Estefania Vasconez1,2, James A. Oo1,2, Adelheid Kratzer8,9, Sandeep Kumar 10, Flávia Rezende1,2, Ivana Josipovic1,2, Dominique Thomas11, Hector Giral8,9, Yannick Schreiber12, Gerd Geisslinger11,12, Christian Fork1,2, Xia Yang13, Fragiska Sigala14, Casey E. Romanoski15, Jens Kroll7, Hanjoong Jo 10, Ulf Landmesser8,9,16, Aldons J. Lusis17, 1234567890():,; Dmitry Namgaladze18, Ingrid Fleming2,6, Matthias S. Leisegang1,2, Jun Zhu 3,4 & Ralf P. Brandes1,2 Oxidized phospholipids (oxPAPC) induce endothelial dysfunction and atherosclerosis. Here we show that oxPAPC induce a gene network regulating serine-glycine metabolism with the mitochondrial methylenetetrahydrofolate dehydrogenase/cyclohydrolase (MTHFD2) as a cau- sal regulator using integrative network modeling and Bayesian network analysis in human aortic endothelial cells. The cluster is activated in human plaque material and by atherogenic lipo- proteins isolated from plasma of patients with coronary artery disease (CAD). Single nucleotide polymorphisms (SNPs) within the MTHFD2-controlled cluster associate with CAD. The MTHFD2-controlled cluster redirects metabolism to glycine synthesis to replenish purine nucleotides. Since endothelial cells secrete purines in response to oxPAPC, the MTHFD2- controlled response maintains endothelial ATP. Accordingly, MTHFD2-dependent glycine synthesis is a prerequisite for angiogenesis. Thus, we propose that endothelial cells undergo MTHFD2-mediated reprogramming toward serine-glycine and mitochondrial one-carbon metabolism to compensate for the loss of ATP in response to oxPAPC during atherosclerosis.