DOCSLIB.ORG

MAP1LC3A Antibody (Pab)

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
MAP1LC3A Antibody (Pab) 21.10.2014MAP1LC3A antibody (pAb) Rabbit Anti-Human Microtubule-associated protein 1 light chain 3 alpha (MAP1A/MAP1B LC3A, MAP1ALC3, ATG8E) Instruction Manual Catalog Number PK-AB718-7579 Synonyms Microtubule-associated protein 1 light chain 3 alpha, LC3, LC3A, MAP1A/MAP1B LC3A, MAP1A/MAP1B light chain 3A, MAP1ALC3, ATG8E, Autophagy-related protein LC3A Description Microtubule-associated proteins (MAPs) regulate microtubule stability and play critical roles in neuronal development and plasticity. MAP1LC3A belongs to the MAP1 LC3 family of proteins that form mature complexes with MAP1A and MAP1B which are thought to be important in the formation and development of axons and dendrites. MAP1LC3A is one of three isoforms of MAP1LC3, the mammalian homolog of yeast ATG8, an essential autophagy protein. These isoforms exhibit distinct expression patterns and MAP1LC3A, like MAP1LC3A but not MAP1LC3B, is post-translationally modified, suggesting the three isoforms may have different physiological functions. Quantity 100 µg Source / Host Rabbit Immunogen MAP1LC3A antibody was raised against a 10 amino acid peptide near the amino terminus of human MAP1LC3A. Purification Method Affinity chromatography purified via peptide column. Clone / IgG Subtype Polyclonal antibody Species Reactivity Human Specificity MAP1LC3A antibody is human specific. At least two isoforms of MAP1LC3A are known to exist. MAP1LC3A antibody is predicted to not cross-react with MAP1LC3B or MAP1LC3C. Formulation Antibody is supplied in PBS containing 0.02% sodium azide. Reconstitution During shipment, small volumes of antibody will occasionally become entrapped in the seal of the product vial. For products with volumes of 200 μl or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container’s cap. Storage & Stability Antibody can be stored at 4ºC for three months and at -20°C for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Applications E, WB, IHC, IF |Note: Antibody might be suitable for other applications not tested so far. Optimal concentrations for each application have to be determined indivudually. MAP1LC3A antibody can be used for detection of MAP1LC3A by Western blot at 1 - 2 µg/ml. Antibody can also be used for Immunohistochemistry starting at 5 µg/mL. For immunofluorescence start at 20 µg/mL. Images Available upon request. References Mandelkow E and Mandelkow EM. Microtubules and microtubule-associated proteins. Curr. Opin. Cell Biol. 1995; 7:72-81. Halpain S and Dehmelt L. The MAP1 family of microtubule-associated proteins. Genome Biol. 2006; 7:224. He H, Dang Y, Dai F, et al. Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B. J. Biol. Chem. 2003; 278:29278-87. Images Available upon request. Related Products Cat. No. PK-AB718-7579P - MAP1LC3A Peptide Cat. No. PK-AB718-1201 - HeLa Cell Lysate FOR IN VITRO RESEARCH USE ONLY. NOT FOR DIAGNOSTIC OR THERAPE UTIC PROCEDURES. PromoCell GmbH North America 1 – 866 – 251 – 2860 (toll free) Email: [email protected] Sickingenstr. 63/65 Deutschland 0800 – 776 66 23 (gebührenfrei) www.promokine.info 69126 Heidelberg France 0800 90 93 32 (ligne verte) Germany United Kingdom 0800 – 96 03 33 (toll free) Other Countries +49 6221 – 649 34 0 09/2014 .
Load more

Recommended publications
  • Autophagy Patterns and Prognosis in Uveal Melanomas
    Modern Pathology (2011) 24, 1036–1045 1036 & 2011 USCAP, Inc. All rights reserved 0893-3952/11 $32.00 Autophagy patterns and prognosis in uveal melanomas Alexandra N Giatromanolaki1, Georgios St Charitoudis2, Nikolaos E Bechrakis3, Vassilios P Kozobolis4, Michael I Koukourakis5, Michael H Foerster2 and Efthimios L Sivridis1 1Department of Pathology, Democritus University of Thrace Medical School, Alexandroupolis, Greece; 2Department of Ophthalmology, Charite´ Medical University, Campus Benjamin Franklin, Berlin, Germany; 3Department of Ophthalmology, University of Innsbruck Medical School, Innsbruck, Austria; 4Department of Ophthalmology, Democritus University of Thrace Medical School, Alexandroupolis, Greece and 5Department of Radiotherapy/Oncology, Democritus University of Thrace Medical School, Alexandroupolis, Greece Autophagy is a self-degradation mechanism by which cells recycle their own cytoplasmic constituents. It has been claimed that, under certain conditions, such a process may be associated with tumor progression. In this study, the autophagic activity was investigated in a series of 99 uveal melanomas after immunohistochemical staining for the autophagy-associated proteins MAP1LC3A and BECN1, most commonly known as LC3A and Beclin 1, respectively. These were assessed in parallel with the hypoxia-inducible factor 1a (HIF1A) and its downstream protein lactate dehydrogenase 5 (composed by five LDHA subunits). Increased autophagic reactivity, detected by MAP1LC3A or BECN1, was associated with intense pigmentation and tumor hypoxia. Uveal melanomas with extensive overexpression of BECN1 or those with underexpression of this protein were associated with the worst prognosis, but the former manifested metastases much earlier than the latter; only 58% of patients with extensive BECN1 overexpression were alive at 4 years, compared with 80% of patients with underexpressed patterns.
    [Show full text]
  • MAP1LC3 Antibody Cat
    MAP1LC3 Antibody Cat. No.: 7951 MAP1LC3 Antibody Immunohistochemistry of MAP1LC3 in rat brain tissue with MAP1LC3 antibody at 5 μg/ml. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat HOMOLOGY: Predicted species reactivity based on immunogen sequence: Bovine: (100%) MAP1LC3 antibody was raised against a 12 amino acid peptide near the center of human MAP1LC3A. IMMUNOGEN: The immunogen is located within amino acids 20 - 70 of MAP1LC3. TESTED APPLICATIONS: ELISA, IHC-P, WB September 29, 2021 1 https://www.prosci-inc.com/map1lc3-antibody-7951.html MAP1LC3 antibody can be used for detection of MAP1LC3 by Western blot at 0.5 - 1 μg/ml. Antibody can also be used for Immunohistochemistry starting at 5 μg/mL. APPLICATIONS: Antibody validated: Western Blot in human samples and Immunohistochemistry in rat samples. All other applications and species not yet tested. MAP1LC3 antibody is human, mouse and rat reactive. Multiple isoforms MAP1LC3 are SPECIFICITY: known to exist. MAP1LC3 antibody is predicted to detect MAP1LC3A, MAP1LC3B, and MAP1LC3C. POSITIVE CONTROL: 1) Cat. No. 1303 - Human Brain Tissue Lysate Predicted: 13 kDa PREDICTED MOLECULAR WEIGHT: Observed: 18 kDa Properties PURIFICATION: MAP1LC3 antibody is affinity chromatography purified via peptide column. CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: MAP1LC3 antibody is supplied in PBS containing 0.02% sodium azide. CONCENTRATION: 1 mg/mL MAP1LC3 antibody can be stored at 4˚C for three months and -20˚C, stable for up to one STORAGE CONDITIONS: year. Additional Info OFFICIAL SYMBOL: MAP1LC3A MAP1LC3 Antibody: LC3, LC3A, ATG8E, MAP1ALC3, MAP1BLC3Autophagy-related protein ALTERNATE NAMES: LC3 A ACCESSION NO.: NP_115903 PROTEIN GI NO.: 14210522 GENE ID: 84557 USER NOTE: Optimal dilutions for each application to be determined by the researcher.
    [Show full text]
  • De Novo EIF2AK1 and EIF2AK2 Variants Are Associated with Developmental Delay, Leukoencephalopathy, and Neurologic Decompensation
    bioRxiv preprint doi: https://doi.org/10.1101/757039; this version posted September 16, 2019. 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. De novo EIF2AK1 and EIF2AK2 variants are associated with developmental delay, leukoencephalopathy, and neurologic decompensation Dongxue Mao1,2, Chloe M. Reuter3,4, Maura R.Z. Ruzhnikov5,6, Anita E. Beck7, Emily G. Farrow8,9,10, Lisa T. Emrick1,11,12,13, Jill A. Rosenfeld12, Katherine M. Mackenzie5, Laurie Robak2,12,13, Matthew T. Wheeler3,14, Lindsay C. Burrage12,13, Mahim Jain15, Pengfei Liu12, Daniel Calame11,13, Sebastien Küry17,18, Martin Sillesen19, Klaus Schmitz-Abe20, Davide Tonduti21, Luigina Spaccini22, Maria Iascone23, Casie A. Genetti20, Madeline Graf16, Alyssa Tran12, Mercedes Alejandro12, Undiagnosed Diseases Network, Brendan H. Lee12,13, Isabelle Thiffault8,9,24, Pankaj B. Agrawal#,20, Jonathan A. Bernstein#,3,25, Hugo J. Bellen#,2,12,26,27,28, Hsiao- Tuan Chao#,1,2,11,12,13,28,27,29 #Correspondence should be addressed: [email protected] (P.A.), [email protected] (J.A.B.), [email protected] (H.J.B.), [email protected] (H.T.C.) 1Department of Pediatrics, Baylor College of Medicine (BCM), Houston, TX 2Jan and Dan Duncan Neurological Research Institute, Texas Children’s Hospital, Houston, TX 3Stanford Center for Undiagnosed Diseases, Stanford University, Stanford, CA 4Stanford Center for Inherited Cardiovascular Disease, Division of Cardiovascular Medicine,
    [Show full text]
  • Autophagy Is a New Protective Mechanism Against the Cytotoxicity
    www.nature.com/scientificreports OPEN Autophagy is a new protective mechanism against the cytotoxicity of platinum nanoparticles in human Received: 14 November 2018 Accepted: 11 February 2019 trophoblasts Published: xx xx xxxx Akitoshi Nakashima1, Kazuma Higashisaka2,3, Tae Kusabiraki1, Aiko Aoki1, Akemi Ushijima1, Yosuke Ono1, Sayaka Tsuda1, Tomoko Shima1, Osamu Yoshino1,7, Kazuya Nagano2, Yasuo Yoshioka2,4,5, Yasuo Tsutsumi2,6 & Shigeru Saito1 Nanoparticles are widely used in commodities, and pregnant women are inevitably exposed to these particles. The placenta protects the growing fetus from foreign or toxic materials, and provides energy and oxygen. Here we report that autophagy, a cellular mechanism to maintain homeostasis, engulfs platinum nanoparticles (nPt) to reduce their cytotoxicity in trophoblasts. Autophagy was activated by nPt in extravillous trophoblast (EVT) cell lines, and EVT functions, such as invasion and vascular remodeling, and proliferation were inhibited by nPt. These inhibitory efects by nPt were augmented in autophagy-defcient cells. Regarding the dynamic state of nPt, analysis using ICP-MS demonstrated a higher accumulation of nPt in the autophagosome-rich than the cytoplasmic fraction in autophagy- normal cells. Meanwhile, there were more nPt in the nuclei of autophagy-defcient cells, resulting in greater DNA damage at a lower concentration of nPt. Thus, we found a new protective mechanism against the cytotoxicity of nPt in human trophoblasts. Pregnant women and developing fetuses are very susceptible to foreign toxins, including air pollutants, microbes, and nanoparticles1–3. Smaller nanoparticles made of silica, titanium dioxide, cobalt and chromium, gold, or silver cross the fetal-maternal barrier more readily than larger particles4–7.
    [Show full text]
  • The Association of ATG16L1 Variations with Clinical Phenotypes of Adult-Onset Still’S Disease
    G C A T T A C G G C A T genes Article The Association of ATG16L1 Variations with Clinical Phenotypes of Adult-Onset Still’s Disease Wei-Ting Hung 1,2, Shuen-Iu Hung 3 , Yi-Ming Chen 4,5,6 , Chia-Wei Hsieh 6,7, Hsin-Hua Chen 6,7,8 , Kuo-Tung Tang 5,6,7 , Der-Yuan Chen 9,10,11,* and Tsuo-Hung Lan 1,5,12,13,* 1 Institute of Clinical Medicine, National Yang-Ming Chiao Tung University, Taipei 11221, Taiwan; [email protected] 2 Department of Medical Education, Taichung Veterans General Hospital, Taichung 40705, Taiwan 3 Cancer Vaccine and Immune Cell Therapy Core Laboratory, Chang Gung Immunology Consortium, Chang Gung Memorial Hospital, Linkou, Taoyuan 33305, Taiwan; [email protected] 4 Department of Medical Research, Taichung Veterans General Hospital, Taichung 40705, Taiwan; [email protected] 5 School of Medicine, College of Medicine, National Yang Ming Chiao Tung University, Taipei 11221, Taiwan; [email protected] 6 Rong Hsing Research Center for Translational Medicine & Ph.D. Program in Translational Medicine, National Chung Hsing University, Taichung 40227, Taiwan; [email protected] (C.-W.H.); [email protected] (H.-H.C.) 7 Division of Allergy, Immunology, and Rheumatology, Taichung Veterans General Hospital, Taichung 40705, Taiwan 8 Department of Industrial Engineering and Enterprise Information, Tunghai University, Taichung 40705, Taiwan 9 Translational Medicine Laboratory, Rheumatology and Immunology Center, China Medical University Hospital, Taichung 40447, Taiwan 10 Rheumatology and Immunology Center, China Medical University Hospital, Taichung 40447, Taiwan Citation: Hung, W.-T.; Hung, S.-I.; 11 School of Medicine, China Medical University, Taichung 40447, Taiwan Chen, Y.-M.; Hsieh, C.-W.; Chen, 12 Tsao-Tun Psychiatric Center, Ministry of Health and Welfare, Nantou 54249, Taiwan H.-H.; Tang, K.-T.; Chen, D.-Y.; Lan, 13 Center for Neuropsychiatric Research, National Health Research Institutes, Miaoli 35053, Taiwan T.-H.
    [Show full text]
  • Spermatozoal Gene KO Studies for the Highly Present Paternal Transcripts
    Spermatozoal gene KO studies for the highly present paternal Potential maternal interactions Conclusions of the KO studies on the maternal gene transcripts detected by GeneMANIA candidates for interaction with the paternal Fbxo2 Selective cochlear degeneration in mice lacking Cul1, Fbxl2, Fbxl3, Fbxl5, Cul-1 KO causes early embryonic lethality at E6.5 before Fbxo2 Fbxo34, Fbxo5, Itgb1, Rbx1, the onset of gastrulation http://www.jneurosci.org/content/27/19/5163.full Skp1a http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3641602/. Loss of Cul1 results in early embryonic lethality and Another KO study showed the following: Loss of dysregulation of cyclin E F-box only protein 2 (Fbxo2) disrupts levels and http://www.ncbi.nlm.nih.gov/pubmed/10508527?dopt=Abs localization of select NMDA receptor subunits, tract. and promotes aberrant synaptic connectivity http://www.ncbi.nlm.nih.gov/pubmed/25878288. Fbxo5 (or Emi1): Regulates early mitosis. KO studies shown lethal defects in preimplantation embryo A third KO study showed that Fbxo2 regulates development http://mcb.asm.org/content/26/14/5373.full. amyloid precursor protein levels and processing http://www.jbc.org/content/289/10/7038.long#fn- Rbx1/Roc1: Rbx1 disruption results in early embryonic 1. lethality due to proliferation failure http://www.pnas.org/content/106/15/6203.full.pdf & Fbxo2 has been found to be involved in http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2732615/. neurons, but it has not been tested for potential decreased fertilization or pregnancy rates. It Skp1a: In vivo interference with Skp1 function leads to shows high expression levels in testis, indicating genetic instability and neoplastic transformation potential other not investigated functions http://www.ncbi.nlm.nih.gov/pubmed/12417738?dopt=Abs http://biogps.org/#goto=genereport&id=230904 tract.
    [Show full text]
  • Photodynamic Therapy Induces Autophagy-Mediated Cell Death In
    Song et al. Cell Death and Disease (2020) 11:938 https://doi.org/10.1038/s41419-020-03136-y Cell Death & Disease ARTICLE Open Access Photodynamic therapy induces autophagy- mediated cell death in human colorectal cancer cells via activation of the ROS/JNK signaling pathway Changfeng Song1,WenXu1,HongkunWu2,XiaotongWang1,QianyiGong1,ChangLiu2,JianwenLiu1 and Lin Zhou2 Abstract Evidence has shown that m-THPC and verteporfin (VP) are promising sensitizers in photodynamic therapy (PDT). In addition, autophagy can act as a tumor suppressor or a tumor promoter depending on the photosensitizer (PS) and the cancer cell type. However, the role of autophagy in m-THPC- and VP-mediated PDT in in vitro and in vivo models of human colorectal cancer (CRC) has not been reported. In this study, m-THPC-PDT or VP-PDT exhibited significant phototoxicity, inhibited proliferation, and induced the generation of large amounts of reactive oxygen species (ROS) in CRC cells. From immunoblotting, fluorescence image analysis, and transmission electron microscopy, we found extensive autophagic activation induced by ROS in cells. In addition, m-THPC-PDT or VP-PDT treatment significantly induced apoptosis in CRC cells. Interestingly, the inhibition of m-THPC-PDT-induced autophagy by knockdown of ATG5 or ATG7 substantially inhibited the apoptosis of CRC cells. Moreover, m-THPC- PDT treatment inhibited tumorigenesis of subcutaneous HCT116 xenografts. Meanwhile, antioxidant treatment 1234567890():,; 1234567890():,; 1234567890():,; 1234567890():,; markedly inhibited autophagy and apoptosis induced by PDT in CRC cells by inactivating JNK signaling. In conclusion, inhibition of autophagy can remarkably alleviate PDT-mediated anticancer efficiency in CRC cells via inactivation of the ROS/JNK signaling pathway.
    [Show full text]
  • MAP1LC3A Antibody [E2F7] Cat
    MAP1LC3A Antibody [E2F7] Cat. No.: 14-019 MAP1LC3A Antibody [E2F7] Immunohistochemistry of paraffin-embedded mouse Immunohistochemistry of paraffin-embedded human liver brain using MAP1LC3A antibody (14-019) at dilution of using MAP1LC3A antibody (14-019) at dilution of 1:100 (40x 1:100 (40x lens). lens). Immunohistochemistry of paraffin-embedded mouse Immunofluorescence analysis of HeLa cells using MAP1LC3A liver using MAP1LC3A antibody (14-019) at dilution of antibody (14-019). 1:100 (40x lens). Immunofluorescence analysis of PC-12 cells using MAP1LC3A antibody (14-019). Immunofluorescence analysis of HUVEC cells using MAP1LC3A antibody (14-019). September 24, 2021 1 https://www.prosci-inc.com/map1lc3a-antibody-e2f7-14-019.html Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat IMMUNOGEN: Recombinant protein of human MAP1LC3A TESTED APPLICATIONS: IF, IHC, IP, WB WB: ,1:500 - 1:2000 IHC: ,1:50 - 1:200 APPLICATIONS: IF: ,1:50 - 1:200 IP: ,1:20 - 1:50 POSITIVE CONTROL: 1) SHG-44 2) Mouse brain 3) Mouse liver 4) Mouse skeletal muscle PREDICTED MOLECULAR Observed: 14kDa WEIGHT: Properties PURIFICATION: Affinity purification CLONALITY: Monoclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. STORAGE CONDITIONS: Store at -20˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: MAP1LC3A MAP1LC3A Antibody: LC3, LC3A, ATG8E, MAP1ALC3, MAP1BLC3Autophagy-related protein ALTERNATE NAMES: LC3 A GENE ID: 84557 USER NOTE: Optimal dilutions for each application to be determined by the researcher. September 24, 2021 2 https://www.prosci-inc.com/map1lc3a-antibody-e2f7-14-019.html Background and References MAP1A and MAP1B are microtubule-associated proteins which mediate the physical interactions between microtubules and components of the cytoskeleton.
    [Show full text]
  • And Inflammation-Related Gene Expression in White Blood
    cells Article Post-Effort Changes in Autophagy- and Inflammation-Related Gene Expression in White Blood Cells of Healthy Young Men Dorota Kostrzewa-Nowak 1,* , Alicja Trzeciak-Ryczek 2,3, Paweł Wityk 4 , Danuta Cembrowska-Lech 2,3 and Robert Nowak 1 1 Centre for Human Structural and Functional Research, Institute of Physical Culture Sciences, University of Szczecin, 17C Narutowicza St., 70-240 Szczecin, Poland; [email protected] 2 Institute of Biology, University of Szczecin, 13 W ˛askaSt., 71-415 Szczecin, Poland; [email protected] (A.T.-R.); [email protected] (D.C.-L.) 3 The Centre for Molecular Biology and Biotechnology, University of Szczecin, 13 W ˛askaSt., 71-415 Szczecin, Poland 4 Faculty of Chemistry, Gda´nskUniversity of Technology, 11/12 Narutowicza St., 80-233 Gda´nsk,Poland; [email protected] * Correspondence: [email protected] Abstract: Acute, strenuous physical exertion requiring high levels of energy production induces the production of reactive oxygen species and metabolic disturbances that can damage the mitochondria. Thus, selective autophagic elimination of defective mitochondria may improve resistance to oxidative stress and potentially to inflammation. The main goal of this study was to evaluate the impacts of intense effort on changes in the expression of select genes related to post-effort inflammation and autophagy. Thirty-five men aged 16–21 years were recruited to the study. The impacts of both aerobic Citation: Kostrzewa-Nowak, D.; (endurance) and anaerobic (speed) efforts on selected genes encoding chemokines (CXCL5, 8–12) Trzeciak-Ryczek, A.; Wityk, P.; were analyzed.
    [Show full text]
  • Identification of a Novel Autophagy-Related Gene Signature
    Identication of a novel autophagy-related gene signature for predicting metastasis and survival in patients with osteosarcoma Guangzhi Zhang Lanzhou University Second Hospital https://orcid.org/0000-0003-3193-0297 Yajun Deng Lanzhou University Second Hospital Zuolong Wu Lanzhou University Second Hospital Enhui Ren Lanzhou University Second Hospital Wenhua Yuan Lanzhou University Second Hospital Qiqi Xie ( [email protected] ) Lanzhou University Second Hospital https://orcid.org/0000-0003-4099-5287 Primary research Keywords: osteosarcoma, autophagy-related genes, signature, survival, metastasis Posted Date: March 26th, 2020 DOI: https://doi.org/10.21203/rs.3.rs-19384/v1 License: This work is licensed under a Creative Commons Attribution 4.0 International License. Read Full License Page 1/20 Abstract Background: Osteosarcoma (OS) is a bone malignant tumor that occurs in children and adolescents. Due to a lack of reliable prognostic biomarkers, the prognosis of OS patients is often uncertain. This study aimed to construct an autophagy-related gene signature to predict the prognosis of OS patients. Methods: The gene expression prole data of OS and normal muscle tissue samples were downloaded separately from the Therapeutically Applied Research To Generate Effective Treatments (TARGET) and Genotype-Tissue Expression (GTEx) databases . The differentially expressed autophagy-related genes (DEARGs) in OS and normal muscle tissue samples were screened using R software, before being subjected to Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analysis. A protein-protein interaction (PPI) network was constructed and hub autophagy-related genes were screened. Finally, the screened autophagy-related genes were subjected to univariate Cox regression, Lasso Cox regression, survival analysis, and clinical correlation analysis.
    [Show full text]
  • The Mtorc1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4
    The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4 The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Csibi, Alfred, Sarah-Maria Fendt, Chenggang Li, George Poulogiannis, Andrew Y. Choo, Douglas J. Chapski, Seung Min Jeong, et al. “The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4.” Cell 153, no. 4 (May 2013): 840–854. © 2013 Elsevier Inc. As Published http://dx.doi.org/10.1016/j.cell.2013.04.023 Publisher Elsevier Version Final published version Citable link http://hdl.handle.net/1721.1/91506 Terms of Use Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. The mTORC1 Pathway Stimulates Glutamine Metabolism and Cell Proliferation by Repressing SIRT4 Alfred Csibi,1 Sarah-Maria Fendt,2,6 Chenggang Li,3,5 George Poulogiannis,4,5 Andrew Y. Choo,1 Douglas J. Chapski,1 Seung Min Jeong,1 Jamie M. Dempsey,1 Andrey Parkhitko,3 Tasha Morrison,3 Elizabeth P. Henske,3 Marcia C. Haigis,1 Lewis C. Cantley,4 Gregory Stephanopoulos,2 Jane Yu,3 and John Blenis1,* 1Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA 2Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA 3Division of Pulmonary and Critical Care Medicine, Department of Medicine, Brigham and Women’s Hospital, Boston, MA 02115, USA 4Division of Signal Transduction,
    [Show full text]
  • Identification of Protein Features Encoded by Alternative Exons Using Exon Ontology
    Downloaded from genome.cshlp.org on October 2, 2021 - Published by Cold Spring Harbor Laboratory Press Resource Identification of protein features encoded by alternative exons using Exon Ontology Léon-Charles Tranchevent,1 Fabien Aubé,1 Louis Dulaurier,1 Clara Benoit-Pilven,1 Amandine Rey,1 Arnaud Poret,1 Emilie Chautard,2 Hussein Mortada,1 François-Olivier Desmet,1 Fatima Zahra Chakrama,1 Maira Alejandra Moreno-Garcia,1 Evelyne Goillot,3 Stéphane Janczarski,1 Franck Mortreux,1 Cyril F. Bourgeois,1,4 and Didier Auboeuf1,4 1Université Lyon 1, ENS de Lyon, CNRS UMR 5239, INSERM U1210, Laboratory of Biology and Modelling of the Cell, F-69007, Lyon, France; 2Laboratoire de Biométrie et Biologie Évolutive, Université Lyon 1, UMR CNRS 5558, INRIA Erable, Villeurbanne, F-69622, France; 3Institut NeuroMyoGène, CNRS UMR 5310, INSERM U1217, Université Lyon 1, Lyon, F-69007 France Transcriptomic genome-wide analyses demonstrate massive variation of alternative splicing in many physiological and pathological situations. One major challenge is now to establish the biological contribution of alternative splicing var- iation in physiological- or pathological-associated cellular phenotypes. Toward this end, we developed a computational approach, named Exon Ontology, based on terms corresponding to well-characterized protein features organized in an ontology tree. Exon Ontology is conceptually similar to Gene Ontology-based approaches but focuses on exon-encod- ed protein features instead of gene level functional annotations. Exon Ontology describes the protein features encoded by a selected list of exons and looks for potential Exon Ontology term enrichment. By applying this strategy to exons that are differentially spliced between epithelial and mesenchymal cells and after extensive experimental validation, we demonstrate that Exon Ontology provides support to discover specific protein features regulated by alternative splic- ing.
    [Show full text]