Search results for "Endoplasm"

showing 10 items of 323 documents

Oxidative Stress and Endoplasmic Reticulum Stress in Rare Respiratory Diseases

2021

Several studies have shown that some rare respiratory diseases, such as alpha-1 antitrypsin deficiency (AATD), idiopathic pulmonary fibrosis (IPF), cystic fibrosis (CF), and primary ciliary dyskinesia (PCD) present oxidative stress (OS) and endoplasmic reticulum (ER) stress. Their involvement in these pathologies and the use of antioxidants as therapeutic agents to minimize the effects of OS are discussed in this review.

0301 basic medicinePathologymedicine.medical_specialtylcsh:Medicineprimary ciliary dyskinesiaReviewrare respiratory diseasesmedicine.disease_causeCystic fibrosiscystic fibrosis03 medical and health sciencesIdiopathic pulmonary fibrosis0302 clinical medicineotorhinolaryngologic diseasesmedicineoxidative stressRespiratory systemPrimary ciliary dyskinesiaAlpha 1-antitrypsin deficiencybusiness.industryEndoplasmic reticulumlcsh:RGeneral Medicineidiopathic pulmonary fibrosismedicine.diseaserespiratory tract diseases030104 developmental biologyAlpha-1 antitrypsin deficiency030220 oncology & carcinogenesisendoplasmic reticulum stressantioxidant therapiesbusinessOxidative stressJournal of Clinical Medicine
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Lon protease: a novel mitochondrial matrix protein in the interconnection between drug-induced mitochondrial dysfunction and endoplasmic reticulum st…

2017

Background and Purpose Mitochondria-associated membranes (MAMs) are specific endoplasmic reticulum (ER) domains that enable it to interact directly with mitochondria and mediate metabolic flow and Ca2+ transfer. A growing list of proteins have been identified as MAMs components, but how they are recruited and function during complex cell stress situations is still not understood, while the participation of mitochondrial matrix proteins is largely unrecognized. Experimental Approach This work compares mitochondrial/ER contact during combined ER stress/mitochondrial dysfunction using a model of human hepatoma cells (Hep3B cell line) treated for 24 h with classic pharmacological inducers of ER…

0301 basic medicinePharmacologyMitochondrial DNAChemistryEndoplasmic reticulumMitochondrionmedicine.diseaseCarbonyl cyanide m-chlorophenyl hydrazoneCell biology03 medical and health sciencesMitofusin-2chemistry.chemical_compound030104 developmental biology0302 clinical medicineMitochondrial matrixUnfolded protein responsemedicineOptic Atrophy 1030217 neurology & neurosurgeryBritish Journal of Pharmacology
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Activin Receptor Ligand Blocking and Cancer Have Distinct Effects on Protein and Redox Homeostasis in Skeletal Muscle and Liver

2019

Muscle wasting in cancer cachexia can be alleviated by blocking activin receptor type 2 (ACVR2) ligands through changes in protein synthesis/degradation. These changes in cellular and protein metabolism may alter protein homeostasis. First, we elucidated the acute (1–2 days) and 2-week effects of blocking ACVR2 ligands by soluble activin receptor 2B (sACVR2B-Fc) on unfolded protein response (UPR), heat shock proteins (HSPs) and redox balance in a healthy mouse skeletal muscle. Second, we examined UPR, autophagy and redox balance with or without sACVR2B-Fc administration in muscle and liver of C26 tumor-bearing mice. The indicators of UPR and HSPs were not altered 1–2 days after a single sAC…

0301 basic medicinePhysiologyProtein metabolismlihaksetMyostatinlcsh:PhysiologyMuscle hypertrophyACTIVATIONchemistry.chemical_compound0302 clinical medicineENDOPLASMIC-RETICULUM STRESSCACHEXIAglutathioneta315Original ResearchIIB RECEPTORbiologylcsh:QP1-981Chemistry1184 Genetics developmental biology physiologyactivinActivin receptorMOUSE MODELunfolded protein response3. Good healthmedicine.anatomical_structure030220 oncology & carcinogenesismyostatinsyöpätauditautofagiacancer cachexiamedicine.medical_specialtyendocrine systemautophagyoxidative stress/redoxta3111liverCachexia03 medical and health sciencesPhysiology (medical)Internal medicinemedicineHEAT-SHOCK PROTEINSskeletal muscleglutationioksidatiivinen stressiECCENTRIC EXERCISEmaksaSkeletal muscleGlutathionemedicine.diseaseMUSCULAR-DYSTROPHY030104 developmental biologyEndocrinologybiology.proteinOXIDATIVE DAMAGE3111 BiomedicineproteiinitlihassurkastumasairaudetACVR2BFrontiers in Physiology
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BAX inhibitor-1 is a Ca(2+) channel critically important for immune cell function and survival.

2015

The endoplasmic reticulum (ER) serves as the major intracellular Ca(2+) store and has a role in the synthesis and folding of proteins. BAX (BCL2-associated X protein) inhibitor-1 (BI-1) is a Ca(2+) leak channel also implicated in the response against protein misfolding, thereby connecting the Ca(2+) store and protein-folding functions of the ER. We found that BI-1-deficient mice suffer from leukopenia and erythrocytosis, have an increased number of splenic marginal zone B cells and higher abundance and nuclear translocation of NF-κB (nuclear factor-κ light-chain enhancer of activated B cells) proteins, correlating with increased cytosolic and ER Ca(2+) levels. When put into culture, purifie…

0301 basic medicineProgrammed cell deathCytoplasmEncephalomyelitis Autoimmune ExperimentalCell SurvivalT-LymphocytesActive Transport Cell NucleusApoptosisBiologyEndoplasmic Reticulum03 medical and health sciencesAnimalsCalcium SignalingObesityMolecular BiologyCalcium signalingMice KnockoutOriginal PaperB-LymphocytesBAX inhibitor 1Endoplasmic reticulumNF-kappa BMembrane ProteinsCell BiologyLeukopeniaNFKB1Acquired immune systemCell biologyEnzyme ActivationMice Inbred C57BLCytosol030104 developmental biologyApoptosisCaspasesCalciumFemaleSpleen
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Anticancer metal drugs and immunogenic cell death

2016

Conventional chemotherapeutics, but also innovative precision anticancer compounds, are commonly perceived to target primarily the cancer cell compartment. However, recently it was discovered that some of these compounds can also exert immunomodulatory activities which might be exploited to synergistically enhance their anticancer effects. One specific phenomenon of the interplay between chemotherapy and the anticancer immune response is the so-called “immunogenic cell death” (ICD). ICD was discovered based on a vaccination effect exerted by cancer cells dying from pretreatment with certain chemotherapeutics, termed ICD inducers, in syngeneic transplantation mouse models. Interestingly, onl…

0301 basic medicineProgrammed cell deathOrganoplatinum Compoundsmedicine.medical_treatmentAntineoplastic AgentsPharmacologyBiochemistryAntineoplastic AgentInorganic ChemistryMice03 medical and health sciences0302 clinical medicineImmune systemCancer immunotherapyNeoplasmsmedicineAnimalsHumansEndoplasmic Reticulum StreCisplatinChemotherapyCell DeathAnimalChemistryOrganoplatinum CompoundEndoplasmic Reticulum Stress3. Good healthOxaliplatin030104 developmental biologyAnticancer metal drugSettore CHIM/03 - Chimica Generale E Inorganica030220 oncology & carcinogenesisCancer cellUnfolded protein responseImmunogenic cell deathCisplatinReactive Oxygen SpecieReactive Oxygen SpeciesImmunogenic cell deathHumanmedicine.drugJournal of Inorganic Biochemistry
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Pekinenin E Inhibits the Growth of Hepatocellular Carcinoma by Promoting Endoplasmic Reticulum Stress Mediated Cell Death.

2017

Hepatocellular carcinoma (HCC) is a malignant primary liver cancer with poor prognosis. In the present study, we report that pekinenin E (PE), a casbane diterpenoid derived from the roots of Euphorbia pekinensis, has a strong antitumor activity against human HCC cells both in vitro and in vivo. PE suppressed the growth of human HCC cells Hep G2 and SMMC-7721. In addition, PE-mediated endoplasmic reticulum (ER) stress caused increasing expressions of C/EBP homologous protein (CHOP), leading to apoptosis in HCC cells both in vitro and in vivo. Inhibition of ER stress with CHOP small interfering RNA or 4-phenyl-butyric acid partially reversed PE-induced cell death. Furthermore, PE induced S ce…

0301 basic medicineProgrammed cell deathSmall interfering RNAPathologymedicine.medical_specialtyCell cycle checkpointCHOP03 medical and health sciencesmedicinePharmacology (medical)Original ResearchPharmacologybusiness.industryEndoplasmic reticulumlcsh:RM1-950apoptosisdigestive system diseasesHep G2030104 developmental biologylcsh:Therapeutics. PharmacologyApoptosishepatocarcinomacell cycle arrestUnfolded protein responseCancer researchbusinessER stresspekinenin EFrontiers in pharmacology
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The endoplasmic reticulum unfolded protein response in neurodegenerative disorders and its potential therapeutic significance

2017

In eukaryotic cells, the endoplasmic reticulum (ER) is the cell compartment involved in secretory protein translocation and quality control of secretory protein folding. Different conditions can alter ER function, resulting in the accumulation of unfolded or misfolded proteins within the ER lumen. Such a condition, known as ER stress, elicits an integrated adaptive response known as the unfolded protein response (UPR) that aims to restore proteostasis within the secretory pathway. Conversely, in prolonged cell stress or insufficient adaptive response, UPR signaling causes cell death. ER dysfunctions are involved and contribute to neuronal degeneration in several human diseases, including Al…

0301 basic medicineProgrammed cell deathTherapeutic targetReviewBiologytherapeutic targetsNeurodegenerative diseaselcsh:RC321-571Unfolded protein response03 medical and health sciencesCellular and Molecular NeuroscienceProtein misfolding disordermedicineneurodegenerative diseasesprotein misfolding disorderslcsh:Neurosciences. Biological psychiatry. NeuropsychiatryMolecular BiologySecretory pathwayEndoplasmic reticulumNeurodegenerationmedicine.diseaseCell biology030104 developmental biologyProteostasisSecretory proteinUnfolded protein responseER streSignal transductionER stressNeuroscience
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Mcl-1 and Bok transmembrane domains : Unexpected players in the modulation of apoptosis

2020

The Bcl-2 protein family comprises both proand antiapoptotic members that control the permeabilization of the mitochondrial outer membrane, a crucial step in the modulation of apoptosis. Recent research has demonstrated that the carboxyl-terminal transmembrane domain (TMD) of some Bcl-2 protein family mem-bers can modulate apoptosis; however, the transmembrane interactome of the antiapoptotic protein Mcl-1 remains largely unexplored. Here, we demonstrate that the Mcl-1 TMD forms homooligomers in the mitochondrial membrane, competes with full-length Mcl-1 protein with regards to its antiapoptotic function, and induces cell death in a Bok-dependent manner. While the Bok TMD oligomers locate p…

0301 basic medicineProtein familyMitochondrionBCL-X(L)Endoplasmic ReticulumInteractome114 Physical sciences03 medical and health sciencesBok0302 clinical medicineProtein DomainsMITOCHONDRIAhemic and lymphatic diseasesAnimalsHumansBcl-2Inner mitochondrial membraneMultidisciplinaryCell DeathChemistryEndoplasmic reticulumapoptosisMcl-1PATHWAYSLOCALIZATIONBiological SciencesTransmembrane protein3. Good healthCell biologytransmembraneTransmembrane domainstomatognathic diseasesGLYCOPHORIN-A DIMERIZATION030104 developmental biologyHELIX PACKINGProto-Oncogene Proteins c-bcl-2BAX030220 oncology & carcinogenesisMitochondrial MembranesPROSURVIVAL BCL-2 PROTEINSMOTIFSURVIVALMyeloid Cell Leukemia Sequence 1 Protein1182 Biochemistry cell and molecular biologyBacterial outer membraneHeLa Cells
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RPGR protein complex regulates proteasome activity and mediates store-operated calcium entry

2018

Ciliopathies are a group of genetically heterogeneous disorders, characterized by defects in cilia genesis or maintenance. Mutations in the RPGR gene and its interacting partners, RPGRIP1 and RPGRIP1L, cause ciliopathies, but the function of their proteins remains unclear. Here we show that knockdown (KD) of RPGR, RPGRIP1 or RPGRIP1L in hTERT-RPE1 cells results in abnormal actin cytoskeleton organization. The actin cytoskeleton rearrangement is regulated by the small GTPase RhoA via the planar cell polarity (PCP) pathway. RhoA activity was upregulated in the absence of RPGR, RPGRIP1 or RPGRIP1L proteins. In RPGR, RPGRIP1 or RPGRIP1L KD cells, we observed increased levels of DVl2 and DVl3 pr…

0301 basic medicineRMRHOAactin cytoskeletonbiologyChemistryEndoplasmic reticulumCiliumSTIM1RPGR complex030105 genetics & heredityActin cytoskeletonStore-operated calcium entryActin cytoskeleton organizationeye diseasesCell biology03 medical and health sciencesendoplasmic reticulum030104 developmental biologyciliopathyOncologybiology.proteinSmall GTPasestore-operated Ca2+ entryResearch PaperOncotarget
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Oxidative modification impairs SERCA activity in Drosophila and human cell models of Parkinson's disease

2021

DJ-1 is a causative gene for familial Parkinson's disease (PD) with different functions, standing out its role against oxidative stress (OS). Accordingly, PD model flies harboring a mutation in the DJ-1β gene (the Drosophila ortholog of human DJ-1) show high levels of OS markers like protein carbonylation, a common post-translational modification that may alter protein function. To increase our understanding of PD pathogenesis as well as to discover potential therapeutic targets for pharmacological intervention, we performed a redox proteomic assay in DJ-1β mutant flies. Among the proteins that showed increased carbonylation levels in PD model flies, we found SERCA, an endoplasmic reticulum…

0301 basic medicineSERCAProteomeProtein CarbonylationProtein Deglycase DJ-1MutantOxidative phosphorylationmedicine.disease_causeSarcoplasmic Reticulum Calcium-Transporting ATPasesAnimals Genetically ModifiedProtein CarbonylationNeuroblastoma03 medical and health sciences0302 clinical medicinemedicineAnimalsDrosophila ProteinsHumansMolecular BiologyMutationActivator (genetics)ChemistryEndoplasmic reticulumfungiParkinson DiseaseCell biologyDisease Models AnimalOxidative StressDrosophila melanogasterPhenotype030104 developmental biologyMutationMolecular MedicineCalciumOxidation-Reduction030217 neurology & neurosurgeryOxidative stressBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
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