Apoptosis Product List
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Computational Genome-Wide Identification of Heat Shock Protein Genes in the Bovine Genome [Version 1; Peer Review: 2 Approved, 1 Approved with Reservations]
F1000Research 2018, 7:1504 Last updated: 08 AUG 2021 RESEARCH ARTICLE Computational genome-wide identification of heat shock protein genes in the bovine genome [version 1; peer review: 2 approved, 1 approved with reservations] Oyeyemi O. Ajayi1,2, Sunday O. Peters3, Marcos De Donato2,4, Sunday O. Sowande5, Fidalis D.N. Mujibi6, Olanrewaju B. Morenikeji2,7, Bolaji N. Thomas 8, Matthew A. Adeleke 9, Ikhide G. Imumorin2,10,11 1Department of Animal Breeding and Genetics, Federal University of Agriculture, Abeokuta, Nigeria 2International Programs, College of Agriculture and Life Sciences, Cornell University, Ithaca, NY, 14853, USA 3Department of Animal Science, Berry College, Mount Berry, GA, 30149, USA 4Departamento Regional de Bioingenierias, Tecnologico de Monterrey, Escuela de Ingenieria y Ciencias, Queretaro, Mexico 5Department of Animal Production and Health, Federal University of Agriculture, Abeokuta, Nigeria 6Usomi Limited, Nairobi, Kenya 7Department of Animal Production and Health, Federal University of Technology, Akure, Nigeria 8Department of Biomedical Sciences, Rochester Institute of Technology, Rochester, NY, 14623, USA 9School of Life Sciences, University of KwaZulu-Natal, Durban, 4000, South Africa 10School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, 30032, USA 11African Institute of Bioscience Research and Training, Ibadan, Nigeria v1 First published: 20 Sep 2018, 7:1504 Open Peer Review https://doi.org/10.12688/f1000research.16058.1 Latest published: 20 Sep 2018, 7:1504 https://doi.org/10.12688/f1000research.16058.1 Reviewer Status Invited Reviewers Abstract Background: Heat shock proteins (HSPs) are molecular chaperones 1 2 3 known to bind and sequester client proteins under stress. Methods: To identify and better understand some of these proteins, version 1 we carried out a computational genome-wide survey of the bovine 20 Sep 2018 report report report genome. -
Stress-Responsive Regulation of Mitochondria Through the ER
TEM-969; No. of Pages 10 Review Stress-responsive regulation of mitochondria through the ER unfolded protein response T. Kelly Rainbolt, Jaclyn M. Saunders, and R. Luke Wiseman Department of Molecular and Experimental Medicine, Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA The endoplasmic reticulum (ER) and mitochondria form function is sensitive to pathologic insults that induce ER physical interactions involved in the regulation of bio- stress (defined by the increased accumulation of misfolded logic functions including mitochondrial bioenergetics proteins within the ER lumen). ER stress can be transmit- and apoptotic signaling. To coordinate these functions ted to mitochondria by alterations in the transfer of me- 2+ during stress, cells must coregulate ER and mitochon- tabolites such as Ca or by stress-responsive signaling dria through stress-responsive signaling pathways such pathways, directly influencing mitochondrial functions. as the ER unfolded protein response (UPR). Although the Depending on the extent of cellular stress, the stress UPR is traditionally viewed as a signaling pathway re- signaling from the ER to mitochondria can result in pro- sponsible for regulating ER proteostasis, it is becoming survival or proapoptotic adaptations in mitochondrial increasingly clear that the protein kinase RNA (PKR)-like function. endoplasmic reticulum kinase (PERK) signaling pathway During the early adaptive phase of ER stress, ER– 2+ within the UPR can also regulate mitochondria proteos- mitochondrial contacts increase, promoting Ca transfer 2+ tasis and function in response to pathologic insults that between these organelles [4]. This increase in Ca flux into induce ER stress. Here, we discuss the contributions of mitochondria stimulates mitochondrial metabolism 2+ PERK in coordinating ER–mitochondrial activities and through the activity of Ca -regulated dehydrogenases describe the mechanisms by which PERK adapts mito- involved in the tricarboxylic acid (TCA) cycle. -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
Mitochondrial Protein Quality Control Mechanisms
G C A T T A C G G C A T genes Review Mitochondrial Protein Quality Control Mechanisms Pooja Jadiya * and Dhanendra Tomar * Center for Translational Medicine, Lewis Katz School of Medicine, Temple University, Philadelphia, PA 19140, USA * Correspondence: [email protected] (P.J.); [email protected] (D.T.); Tel.: +1-215-707-9144 (D.T.) Received: 29 April 2020; Accepted: 15 May 2020; Published: 18 May 2020 Abstract: Mitochondria serve as a hub for many cellular processes, including bioenergetics, metabolism, cellular signaling, redox balance, calcium homeostasis, and cell death. The mitochondrial proteome includes over a thousand proteins, encoded by both the mitochondrial and nuclear genomes. The majority (~99%) of proteins are nuclear encoded that are synthesized in the cytosol and subsequently imported into the mitochondria. Within the mitochondria, polypeptides fold and assemble into their native functional form. Mitochondria health and integrity depend on correct protein import, folding, and regulated turnover termed as mitochondrial protein quality control (MPQC). Failure to maintain these processes can cause mitochondrial dysfunction that leads to various pathophysiological outcomes and the commencement of diseases. Here, we summarize the current knowledge about the role of different MPQC regulatory systems such as mitochondrial chaperones, proteases, the ubiquitin-proteasome system, mitochondrial unfolded protein response, mitophagy, and mitochondria-derived vesicles in the maintenance of mitochondrial proteome and health. The proper understanding of mitochondrial protein quality control mechanisms will provide relevant insights to treat multiple human diseases. Keywords: mitochondria; proteome; ubiquitin; proteasome; chaperones; protease; mitophagy; mitochondrial protein quality control; mitochondria-associated degradation; mitochondrial unfolded protein response 1. Introduction Mitochondria are double membrane, dynamic, and semiautonomous organelles which have several critical cellular functions. -
Mitochondrial Chaperone Trap1 and the Calcium Binding Protein Sorcin Interact and Protect Cells Against Apoptosis Induced by Antiblastic Agents
Published OnlineFirst July 20, 2010; DOI: 10.1158/0008-5472.CAN-10-1256 Published OnlineFirst on July 20, 2010 as 10.1158/0008-5472.CAN-10-1256 Therapeutics, Targets, and Chemical Biology Cancer Research Mitochondrial Chaperone Trap1 and the Calcium Binding Protein Sorcin Interact and Protect Cells against Apoptosis Induced by Antiblastic Agents Matteo Landriscina1, Gabriella Laudiero3, Francesca Maddalena1, Maria Rosaria Amoroso3, Annamaria Piscazzi1, Flora Cozzolino4,6, Maria Monti4,6, Corrado Garbi5, Alberto Fersini2, Piero Pucci4,6, and Franca Esposito3,6 Abstract TRAP1, a mitochondrial chaperone (Hsp75) with antioxidant and antiapoptotic functions, is involved in multidrug resistance in human colorectal carcinoma cells. Through a proteomic analysis of TRAP1 coimmu- noprecipitation complexes, the Ca2+-binding protein Sorcin was identified as a new TRAP1 interactor. This result prompted us to investigate the presence and role of Sorcin in mitochondria from human colon carci- noma cells. Using fluorescence microscopy and Western blot analysis of purified mitochondria and submito- chondrial fractions, we showed the mitochondrial localization of an isoform of Sorcin with an electrophoretic motility lower than 20 kDa that specifically interacts with TRAP1. Furthermore, the effects of overexpressing or downregulating Sorcin and/or TRAP1 allowed us to demonstrate a reciprocal regulation between these two proteins and to show that their interaction is required for Sorcin mitochondrial localization and TRAP1 sta- bility. Indeed, the depletion of TRAP1 by short hairpin RNA in colorectal carcinoma cells lowered Sorcin levels in mitochondria, whereas the depletion of Sorcin by small interfering RNA increased TRAP1 degradation. We also report several lines of evidence suggesting that intramitochondrial Sorcin plays a role in TRAP1 cytopro- tection. -
Characterization of the Cellular Network of Ubiquitin Conjugating and Ligating Enzymes Ewa Katarzyna Blaszczak
Characterization of the cellular network of ubiquitin conjugating and ligating enzymes Ewa Katarzyna Blaszczak To cite this version: Ewa Katarzyna Blaszczak. Characterization of the cellular network of ubiquitin conjugating and ligating enzymes. Cellular Biology. Université Rennes 1, 2015. English. NNT : 2015REN1S116. tel-01547616 HAL Id: tel-01547616 https://tel.archives-ouvertes.fr/tel-01547616 Submitted on 27 Jun 2017 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ANNÉE 2015 THÈSE / UNIVERSITÉ DE RENNES 1 sous le sceau de l’Université Européenne de Bretagne pour le grade de DOCTEUR DE L’UNIVERSITÉ DE RENNES 1 Mention : BIOLOGIE École doctorale Vie-Agro-Santé présentée par Ewa Katarzyna Blaszczak Préparée à l’unité de recherche UMR 6290, IGDR Institut de Génétique et Développement de Rennes Université Rennes 1 Thèse soutenue à Rennes le 26.06.2015 Characterization of devant le jury composé de : Aude ECHALIER-GLAZER the cellular network Maître de conférence University of Leicester / rapporteur of ubiquitin Lionel PINTARD Directeur de recherche -
Oncoprotein MDM2 Is a Ubiquitin Ligase E3 for Tumor Suppressor P53
View metadata,FEBS 19628 citation and similar papers at core.ac.uk FEBS Letters 420brought (1997) to you 25^27 by CORE provided by Elsevier - Publisher Connector Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53 Reiko Honda, Hirofumi Tanaka, Hideyo Yasuda* School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, 1432-1 Horinouchi, Tokyo 192-03, Japan Received 20 October 1997; revised version received 12 November 1997 the ubiquitin activating enzyme, E1, the ubiquitin conjugating Abstract The tumor suppressor p53 is degraded by the ubiquitin-proteasome system. p53 was polyubiquitinated in the enzyme, E2 and the ubiquitin ligase, E3. E1 is a common presence of E1, UbcH5 as E2 and MDM2 oncoprotein. A enzyme involved in all kinds of ubiquitination. The speci¢city ubiquitin molecule bound MDM2 through sulfhydroxy bond of the targeted protein is dependent on the E2 and E3 used in which is characteristic of ubiquitin ligase (E3)-ubiquitin binding. the reaction. The resultant ubiquitinated protein is degraded The cysteine residue in the carboxyl terminus of MDM2 was by proteasome. essential for the activity. These data suggest that the MDM2 protein, which is induced by p53, functions as a ubiquitin ligase, 2. Materials and methods E3, in human papillomavirus-uninfected cells which do not have E6 protein. 2.1. Expression of proteins z 1997 Federation of European Biochemical Societies. Human MDM2 [15], E6-AP [16], UbcH7 [17], E2-C/UbcH10 [18], EFP [19], cdc34 [20] and UbcH5 [21] cDNAs were obtained by RT- Key words: MDM2; p53; Ubiquitin ligase; E6AP; HECT PCR using RNA from HeLa S3 cells. -
TRAP1 Regulates Wnt/-Catenin Pathway Through LRP5/6 Receptors
International Journal of Molecular Sciences Article TRAP1 Regulates Wnt/β-Catenin Pathway through LRP5/6 Receptors Expression Modulation 1, 1, 1 1 Giacomo Lettini y, Valentina Condelli y, Michele Pietrafesa , Fabiana Crispo , Pietro Zoppoli 1 , Francesca Maddalena 1, Ilaria Laurenzana 1 , Alessandro Sgambato 1, Franca Esposito 2,* and Matteo Landriscina 1,3,* 1 Laboratory of Pre-Clinical and Translational Research, IRCCS, Referral Cancer Center of Basilicata, 85028 Rionero in Vulture, PZ, Italy; [email protected] (G.L.); [email protected] (V.C.); [email protected] (M.P.); [email protected] (F.C.); [email protected] (P.Z.); [email protected] (F.M.); [email protected] (I.L.); [email protected] (A.S.) 2 Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, 80131 Naples, Italy 3 Medical Oncology Unit, Department of Medical and Surgical Sciences, University of Foggia, 71100 Foggia, Italy * Correspondence: [email protected] (F.E.); [email protected] (M.L.); Tel.: +39-081-7463-145 (F.E.); +39-0881-736-426 (M.L.) These authors have contributed equally to this work. y Received: 4 September 2020; Accepted: 10 October 2020; Published: 13 October 2020 Abstract: Wnt/β-Catenin signaling is involved in embryonic development, regeneration, and cellular differentiation and is responsible for cancer stemness maintenance. The HSP90 molecular chaperone TRAP1 is upregulated in 60–70% of human colorectal carcinomas (CRCs) and favors stem cells maintenance, modulating the Wnt/β-Catenin pathway and preventing β-Catenin phosphorylation/degradation. The role of TRAP1 in the regulation of Wnt/β-Catenin signaling was further investigated in human CRC cell lines, patient-derived spheroids, and CRC specimens. -
Structure-Function Relationship and Their Role in Protein Folding
Chapter 8 1 Molecular Chaperones: Structure-Function 2 Relationship and their Role in Protein Folding 3 Bhaskar K. Chatterjee, Sarita Puri, Ashima Sharma, Ashutosh Pastor, 4 and Tapan K. Chaudhuri 5 Abstract During heat shock conditions a plethora of proteins are found to play a 6 role in maintaining cellular homeostasis. They play diverse roles from folding of 7 non-native proteins to the proteasomal degradation of harmful aggregates. A few 8 out of these heat shock proteins (Hsp) help in the folding of non-native substrate 9 proteins and are termed as molecular chaperones. Various structural and functional 10 adaptations make them work efficiently under both normal and stress conditions. 11 These adaptations involve transitions to oligomeric structures, thermal stability, 12 efficient binding affinity for substrates and co-chaperones, elevated synthesis during 13 shock conditions, switching between ‘holding’ and ‘folding’ functions etc. Their 14 ability to function under various kinds of stress conditions like heat shock, cancers, 15 neurodegenerative diseases, and in burdened cells due to recombinant protein pro- 16 duction makes them therapeutically and industrially important biomolecules. 17 Keywords Chaperone assisted folding · Heat shock · Molecular chaperones · 18 Protein folding · Structure-function of chaperones 19 Abbreviations 20 ACD α-crystallin domain 21 ADP Adenosine di-phosphate 22 ATP Adenosine tri-phosphate 23 CCT Chaperonin containing TCP-1 24 CIRCE Controlling inverted repeat of chaperone expression 25 Bhaskar K. Chatterjee, Sarita Puri, Ashima Sharma, and Ashutosh Pastor authors are equally contributed. B. K. Chatterjee · S. Puri · A. Sharma · A. Pastor · T. K. Chaudhuri (*) Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, HauzKhas, New Delhi, India e-mail: [email protected] © Springer International Publishing AG 2018 181 A. -
Cell Surface GRP94 As a Novel Emerging Therapeutic Target for Monoclonal Antibody Cancer Therapy
cells Review Cell Surface GRP94 as a Novel Emerging Therapeutic Target for Monoclonal Antibody Cancer Therapy Ji Woong Kim † , Yea Bin Cho † and Sukmook Lee * Biopharmaceutical Chemistry Major, School of Applied Chemistry, Kookmin University, Seoul 02707, Korea; [email protected] (J.W.K.); [email protected] (Y.B.C.) * Correspondence: [email protected]; Tel.: +82-2-910-6763 † These authors contributed equally to this work. Abstract: Glucose-regulated protein 94 (GRP94) is an endoplasmic reticulum (ER)-resident member of the heat shock protein 90 (HSP90) family. In physiological conditions, it plays a vital role in regulating biological functions, including chaperoning cellular proteins in the ER lumen, maintaining calcium homeostasis, and modulating immune system function.‘Recently, several reports have shown the functional role and clinical relevance of GRP94 overexpression in the progression and metastasis of several cancers. Therefore, the current review highlights GRP94’s physiological and pathophysiological roles in normal and cancer cells. Additionally, the unmet medical needs of small chemical inhibitors and the current development status of monoclonal antibodies specifically targeting GRP94 will be discussed to emphasize the importance of cell surface GRP94 as an emerging therapeutic target in monoclonal antibody therapy for cancer. Keywords: GRP94; cancer; therapeutic target; therapy; monoclonal antibody Citation: Kim, J.W.; Cho, Y.B.; Lee, S. Cell Surface GRP94 as a Novel 1. Introduction Emerging Therapeutic Target for Cancer, the second leading cause of death behind cardiovascular disease, remains a Monoclonal Antibody Cancer major global public health problem [1]. Overall, the burden of cancer incidence and mortal- Therapy. Cells 2021, 10, 670. -
Molecular Chaperone TRAP1 Regulates a Metabolic Switch Between Mitochondrial Respiration and Aerobic Glycolysis
Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis Soichiro Yoshidaa,1, Shinji Tsutsumia,1, Guillaume Muhlebachb,1, Carole Sourbiera, Min-Jung Leec, Sunmin Leec, Evangelia Vartholomaioub, Manabu Tatokoroa,d, Kristin Beebea, Naoto Miyajimaa, Robert P. Mohneye, Yang Chene, Hisashi Hasumia, Wanping Xua, Hiroshi Fukushimad, Ken Nakamuraf, Fumitaka Kogad, Kazunori Kiharad, Jane Trepelc, Didier Picardb, and Leonard Neckersa,2 aUrologic Oncology Branch and cMedical Oncology Branch, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892; bDepartment of Cell Biology, University of Geneva, CH-1211 Geneva 4, Switzerland; eMetabolon, Durham, NC 27560; dDepartment of Urology, Tokyo Medical and Dental University, Tokyo 113-8510, Japan; and fGladstone Institute of Neurological Disease, University of California at San Francisco School of Medicine, San Francisco, CA 94158 Edited* by Sue Wickner, National Cancer Institute, National Institutes of Health, Bethesda, MD, and approved March 12, 2013 (received for review November 27, 2012) TRAP1 (TNF receptor-associated protein), a member of the HSP90 HSP90 comprises as much as 5% of a cancer cell’sproteincom- chaperone family, is found predominantly in mitochondria. TRAP1 is plement (12). Indeed, some cancers express less TRAP1 than do broadly considered to be an anticancer molecular target. However, their normal tissue counterparts (13). Thus, the functions of TRAP1 current inhibitors cannot distinguish between HSP90 and TRAP1, in mitochondria of normal and transformed cells are likely more making their utility as probes of TRAP1-specific function question- complex than previously appreciated and, in the absence of TRAP1- able. Some cancers express less TRAP1 than do their normal tissue specific inhibitors, other approaches are necessary to investigate counterparts, suggesting that TRAP1 function in mitochondria of TRAP1-specific cellular effects. -
Cloning of the Human Homolog of the CDC34 Cell Cycle Gene by Complementation in Yeast SHARON E
Proc. Natl. Acad. Sci. USA Vol. 90, pp. 10484-10488, November 1993 Genetics Cloning of the human homolog of the CDC34 cell cycle gene by complementation in yeast SHARON E. PLON*tt, KATHLEEN A. LEPPIG§, HONG-NHUNG Do*, AND MARK GROUDINE*¶ *Fred Hutchinson Cancer Research Center, Seattle, WA 98104; and Departments of tMedicine, §Pathology and fRadiation Oncology, University of Washington, Seattle, WA 98195 Communicated by Leland Hartwell, August 9, 1993 ABSTRACT In a screen designed to isolate human cDNAs During initial screening for human cDNAs that would that complement a yeast G2 phase checkpoint mutation (mecl), complement the mecl checkpoint mutation, we obtained a we isolated a cDNA homologous to the Saccharomyces cerevi- partially active cDNA that further analysis reveals is the siae CDC34 gene. The human CDC34 cDNA can functionally human homolog of S. cerevisiae CDC34. We report here the substitute for the yeast CDC34 gene and represents a mam- cloning and functional and physical characterization of this malian homolog ofthe group ofyeast genes required for the late human gene. 11 G- S phase transition. The human CDC34 gene is expressed in multiple cell lines as a unique species and Southern blot MATERIALS AND METHODS analysis reveals evidence for a single gene that is highly conserved in higher eukaryotes. The human gene is located on Yeast and Bacterial Strains. The S. cerevisiae strains de- the far telomeric region of 19p13.3 in a location that defmes a scribed in these experiments were isogenic with A364a. region of homology between human chromosome 19p and Source of the strain other than this laboratory are indicated: mouse chromosome 11.