Search results for " Post-Translational"

showing 10 items of 148 documents

The histone deacetylase inhibitor SAHA induces HSP60 nitration and its extracellular release by exosomal vesicles in human lung-derived carcinoma cel…

2015

// Claudia Campanella 1, 2, * , Antonella D'Anneo 3, * , Antonella Marino Gammazza 1, 2, * , Celeste Caruso Bavisotto 1, 2 , Rosario Barone 1, 2 , Sonia Emanuele 4 , Filippa Lo Cascio 1 , Emanuele Mocciaro 1 , Stefano Fais 5 , Everly Conway De Macario 6 , Alberto J.L. Macario 2, 6 , Francesco Cappello 1, 2 , Marianna Lauricella 4 1 Department of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy “Emerico Luna”, University of Palermo, Palermo, Italy 2 Euro-Mediterranean Institute of Science and Technology, Palermo, Italy 3 Department of Biological, Chemical and Pharmaceutical Sciences and Technologies, Laboratory of Biochemistry, University of Palermo, Palermo, Ita…

0301 basic medicineanimal structuresLung Neoplasmsmedicine.drug_classCell SurvivalNitrosationExosomes; Histone deacetylase inhibitor; HSP60; Oxidative stress; SAHAchemical and pharmacologic phenomenaAntineoplastic AgentsApoptosisexosomesBiologyHydroxamic Acidscomplex mixturesMitochondrial Proteins03 medical and health sciencesCell Line TumorSettore BIO/10 - BiochimicamedicineHumansoxidative stressSecretionViability assayCell ProliferationVorinostatHistone deacetylase inhibitorCell growthSettore BIO/16 - Anatomia UmanaHistone deacetylase inhibitorfungiSAHAChaperonin 60MicrovesiclesHistone Deacetylase InhibitorsExosome030104 developmental biologyOncologyApoptosisImmunologyCancer researchOxidative streHSP60Histone deacetylaseProtein Processing Post-TranslationalHSP60Research Paper
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Obesogenic Diets Cause Alterations on Proteins and Theirs Post-Translational Modifications in Mouse Brains

2021

Obesity constitutes a major global health threat and is associated with a variety of diseases ranging from metabolic and cardiovascular disease, cancer to neurodegeneration. The hallmarks of neurodegeneration include oxidative stress, proteasome impairment, mitochondrial dysfunction and accumulation of abnormal protein aggregates as well as metabolic alterations. As an example, in post-mortem brain of patients with Alzheimer’s disease (AD), several studies have reported reduction of insulin, insulin-like growth factor 1 and insulin receptor and an increase in tau protein and glycogen-synthase kinase-3β compared to healthy controls suggesting an impairment of metabolism in the AD patient’s …

0301 basic medicinemedicine.medical_specialtyRC620-627Endocrinology Diabetes and Metabolismmedicine.medical_treatmentTau proteinObesity nutrition brain impairment proteomics post-translational modificationsBrain damageMitochondrionProteomicsmedicine.disease_causeSettore BIO/09 - Fisiologia03 medical and health sciencesproteomics0302 clinical medicineInternal medicinepost-translational modificationsmedicineTX341-641ObesityNutritional diseases. Deficiency diseasesOriginal ResearchSettore MED/04 - Patologia GeneraleNutrition and DieteticsbiologyNutrition. Foods and food supplyInsulinNeurodegenerationmedicine.diseasebrain impairmentInsulin receptornutrition030104 developmental biologyEndocrinologybiology.proteinmedicine.symptom030217 neurology & neurosurgeryOxidative stressFood ScienceNutrition and Metabolic Insights
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Down-regulation of Endogenous Amyloid Precursor Protein Processing due to Cellular Aging

2005

Processing of amyloid precursor protein (APP) is a well acknowledged central pathogenic mechanism in Alzheimer disease. However, influences of age-associated cellular alterations on the biochemistry of APP processing have not been studied in molecular detail so far. Here, we report that processing of endogenous APP is down-regulated during the aging of normal human fibroblasts (IMR-90). The generation of intracellular APP cleavage products C99, C83, and AICD gradually declines with increasing life span and is accompanied by a reduced secretion of soluble APP (sAPP) and sAPPalpha. Further, the maturation of APP was reduced in senescent cells, which has been shown to be directly mediated by a…

ADAM10NicastrinEndogenyBiochemistryCell LineAmyloid beta-Protein PrecursorMembrane MicrodomainsDownregulation and upregulationEndopeptidasesmental disordersPresenilin-1Amyloid precursor proteinAspartic Acid EndopeptidasesHumansSecretionMolecular BiologyCellular SenescenceMembrane GlycoproteinsbiologyChemistryMembrane ProteinsCell BiologyFibroblastsCholesterolBiochemistrybiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAmyloid precursor protein secretaseIntracellularJournal of Biological Chemistry
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Novel mutations of the MET proto-oncogene in papillary renal carcinomas.

1999

Hereditary papillary renal carcinoma (HPRC) is characterized by multiple, bilateral papillary renal carcinomas. Previously, we demonstrated missense mutations in the tyrosine kinase domain of the MET proto-oncogene in HPRC and a subset of sporadic papillary renal carcinomas. In this study, we screened a large panel of sporadic papillary renal carcinomas and various solid tumors for mutations in the MET proto-oncogene. Summarizing these and previous results, mutations of the MET proto-oncogene were detected in 17/129 sporadic papillary renal carcinomas but not in other solid tumors. We detected five novel missense mutations; three of five mutations were located in the ATP-binding region of t…

AdenomaModels MolecularCancer ResearchProtein ConformationDNA Mutational AnalysisMolecular Sequence DataHereditary Papillary Renal Cell CarcinomaBiologymedicine.disease_causeTransfectionProto-Oncogene MasReceptor tyrosine kinaseMiceAdenosine TriphosphateNeoplastic Syndromes HereditaryProto-OncogenesGeneticsCarcinomamedicineMissense mutationAnimalsHumansPoint MutationAmino Acid SequencePhosphorylationCodonMolecular BiologyKidneyMutationBinding SitesSequence Homology Amino AcidPoint mutation3T3 CellsDNA NeoplasmProto-Oncogene Proteins c-metmedicine.diseaseCarcinoma PapillaryKidney NeoplasmsNeoplasm Proteinsmedicine.anatomical_structureCell Transformation NeoplasticCancer researchbiology.proteinMutagenesis Site-DirectedTyrosine kinaseProtein Processing Post-TranslationalSequence AlignmentOncogene
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Regulation of ISWI chromatin remodelling activity.

2013

The packaging of the eukaryotic genome into chromatin facilitates the storage of the genetic information within the nucleus, but prevents the access to the underlying DNA sequences. Structural changes in chromatin are mediated by several mechanisms. Among them, ATP-dependent remodelling complexes belonging to ISWI family provides one of the best examples that eukaryotic cells evolved to finely regulate these changes. ISWI-containing complexes use the energy derived from ATP hydrolysis to rearrange nucleosomes on chromatin in order to favour specific nuclear reactions. The combination of regulatory nuclear factors associated with the ATPase subunit as well as its modulation by specific histo…

Adenosine TriphosphatasesISWI chromatinBiologyChromatin Assembly and DisassemblyChromatin remodelingCell biologyChromatinProtein Structure TertiaryHistoneHistone H1Nucleic AcidsProtein Interaction MappingGeneticsbiology.proteinHistone codeNucleosomeAnimalsHumansScaffold/matrix attachment regionProtein Processing Post-TranslationalGenetics (clinical)ChIA-PETTranscription FactorsChromosoma
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Topographic heterogeneity of amyloid B-protein epitopes in brains with various forms of neuronal ceroid lipofuscinoses suggesting defective processin…

1990

To verify our hypothesis of defective protease inhibitor domains that are encoded by abnormal processing of amyloid precursor protein (APP) in brains of patients with neuronal ceroid lipofuscinoses (NCL), immunohistochemical and cytochemical studies were performed with monoclonal antibodies (mAbs) directed against various domains of APP. For the studies, 22 autopsy brains were used: 12 with different forms of NCL, and 10 control brains. The staining procedure for the avidin-biotin complex (ABC) technique and the postembedding gold-labelled procedure for electron microscopy (EM) were employed. Of all mAbs used for the study, only mAbs generated against amyloid B-protein bound to neural tissu…

AdultAmyloidPathologymedicine.medical_specialtyBatten diseaseAdolescentAmyloidImmunocytochemistryPathology and Forensic MedicineLipofuscinEpitopes03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineNeuronal Ceroid-LipofuscinosesAmyloid precursor proteinmedicineHumansSenile plaquesChildAged030304 developmental biology0303 health sciencesAmyloid beta-PeptidesbiologyAntibodies MonoclonalBrainInfantMiddle Agedmedicine.diseaseImmunohistochemistryMolecular biology3. Good healthChild Preschoolbiology.proteinNeuronal ceroid lipofuscinosisNeurology (clinical)Protein Processing Post-Translational030217 neurology & neurosurgeryImmunostainingActa Neuropathologica
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Posttranslationally modified proteins as mediators of sustained intestinal inflammation.

2006

Oxidative and carbonyl stress leads to generation of N(epsilon)-carboxymethyllysine-modified proteins (CML-mps), which are known to bind the receptor for advanced glycation end products (RAGE) and induce nuclear factor (NF)-kappaB-dependent proinflammatory gene expression. To determine the impact of CML-mps in vivo, RAGE-dependent sustained NF-kappaB activation was studied in resection gut specimens from patients with inflammatory bowel disease. Inflamed gut biopsy tissue demonstrated a significant up-regulation of RAGE and increased NF-kappaB activation. Protein extracts from the inflamed zones, but not from noninflamed resection borders, caused perpetuated NF-kappaB activation in cultured…

AdultCell ExtractsMaleReceptor for Advanced Glycation End ProductsInflammationBiologyInflammatory bowel diseasep38 Mitogen-Activated Protein KinasesPathology and Forensic MedicineProinflammatory cytokineRAGE (receptor)MiceGlycationhemic and lymphatic diseasesGene expressionmedicineAnimalsCalgranulin BHumansCalgranulin AIntestinal MucosaReceptors ImmunologicReceptorProtein Kinase InhibitorsMice KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3LysineNF-kappa Bnutritional and metabolic diseasesEndothelial Cellsmedicine.diseaseNFKB1Inflammatory Bowel DiseasesIntestinesDisease Models AnimalImmunologyCancer researchFemalemedicine.symptomProtein Processing Post-TranslationalRegular ArticlesThe American journal of pathology
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Molecular characterisation and expression analysis of SEREX-defined antigen NUCB2 in gastric epithelium, gastritis and gastric cancer.

2009

NUCB2 is an EF-hand Ca2+ binding protein that has been implicated in various physiological processes like calcium homeostasis, hypothalamic regulation of feeding and TNF receptor shedding. In our previous study we identified NUCB2 as a potential tumour antigen eliciting autoantibody responses in 5.4% of gastric cancer patients but not in the healthy individuals.The current study aimed to elucidate the molecular mechanism underlying NUCB2 immunogenicity and to gain an insight into the physiological functions of NUCB2 in the stomach. mRNA expression analysis demonstrated that NUCB2 is ubiquitously expressed in normal tissues, including lymphoid tissues, and downregulated in gastric tumours wh…

AdultMalePathologymedicine.medical_specialtyHistologyNUCB2BiophysicsDown-RegulationNerve Tissue ProteinsBiologyAntigenWestern blotchief cellsParietal Cells GastricStomach NeoplasmsGastric glandsGastric mucosamedicineHumansNucleobindinsEnterochromaffin-like celllcsh:QH301-705.5AgedAutoantibodiesAged 80 and overOriginal Papermedicine.diagnostic_testReverse Transcriptase Polymerase Chain ReactionStomachgastric cancerCalcium-Binding Proteinsparietal cellsCell BiologySEREXMiddle AgedMolecular biologyGastric chief cellDNA-Binding Proteinsmedicine.anatomical_structurelcsh:Biology (General)Gastric MucosaGastritisCancer cellpepsinogen secretion.Femaletumour-associated antigensProtein Processing Post-TranslationalEuropean journal of histochemistry : EJH
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Elevated serum levels of IGF-binding protein 2 in patients with non-seminomatous germ cell cancer: correlation with tumor markers alpha-fetoprotein a…

2008

Background/aimsAlterations of the IGF system have been described in several different types of cancer. However, no information is available about the role of the IGF system in patients with non-seminomatous germ cell cancer.MethodsFree IGF-I, IGF-II, acid-labile subunit, and IGF-binding proteins (IGFBPs) 1–4 were analyzed by specific RIAs in 32 patients with untreated non-seminomas and compared with IGFBP levels of 38 healthy controls. Serum IGFBPs were analyzed by western ligand blotting (WLB) and immunoblotting. In 16 patients, IGFBP profiles were measured before, during, and after treatment.ResultsIn patients with testicular cancer, IGF-II levels were on average 1.44-fold higher than in …

AdultMalemedicine.medical_specialtyEndocrinology Diabetes and MetabolismProtein subunitBiologyChorionic GonadotropinInsulin-like growth factor-binding proteinHuman chorionic gonadotropinEndocrinologyTesticular NeoplasmsInsulin-Like Growth Factor IIRecurrenceInternal medicinemedicineBiomarkers TumorHumansIn patientTesticular cancerBinding proteinCancerGeneral MedicineMiddle AgedNeoplasms Germ Cell and Embryonalmedicine.diseaseUp-RegulationInsulin-Like Growth Factor Binding ProteinsInsulin-Like Growth Factor Binding Protein 2EndocrinologyInsulin-Like Growth Factor Binding Protein 3Case-Control Studiesbiology.proteinalpha-FetoproteinsOncofetal antigenProtein Processing Post-TranslationalEuropean journal of endocrinology
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Soluble Interleukin-2 Receptor Secretion Defectin Vitroin HLA-B8, DR3 Positive Subjects

1990

Several studies have shown that HLA-B8,DR3 positive subjects may display T cell dysfunctions. Recently, a soluble form of the receptor for IL-2 (sIL-2R) has been demonstrated in human sera and in vitro-stimulated culture supernatant from human T lymphocytes. In the present paper we report sIL-2R serum levels and sIL-2R production from peripheral blood mononuclear cells in HLA-B8,DR3 positive subjects. We found that HLA-B8,DR3 positive subjects have the highest values of serum sIL-2R, but comparing the values of these subjects with those of negative ones no significant difference was observed. As regards the in vitro production of sIL-2R, no difference exists for unstimulated cultures, where…

AdultMalemusculoskeletal diseasesInterleukin 2medicine.medical_specialtyAdolescentT cellImmunologyStimulationHuman leukocyte antigenBiologyLymphocyte Activationmedicine.disease_causePeripheral blood mononuclear cellAutoimmune DiseasesHLA-B8 AntigenAutoimmunityHLA-DR3 AntigenT-Lymphocyte Subsetsimmune system diseasesInternal medicinemedicineHumansImmunology and AllergyGenetic Predisposition to DiseaseReceptorSicilyCells CulturedImmunologic Deficiency SyndromesReceptors Interleukin-2Middle AgedIn vitroDiabetes Mellitus Type 1medicine.anatomical_structureEndocrinologySolubilityImmunologyLeukocytes MononuclearFemaleDisease SusceptibilityProtein Processing Post-Translationalmedicine.drugAutoimmunity
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