0000000000744897

AUTHOR

Gustavo Egea

0000-0001-5242-150x

showing 4 related works from this author

alpha GalNAc is essential for recognition of Exo-1 epithelial antigen by mouse monoclonal antibody Pa-G-14.

1993

Mouse monoclonal antibody Pa-G-14 detects Exo-1, an antigen whose expression is regulated in the processes of epithelial-cell differentiation and transformation. The epitope recognized by Pa-G-14 is present both in glycosphingolipids and in mucin glycoproteins. To characterize the specificity of Pa-G-14, immuno-thin-layer chromatography, biochemical, and enzymatic treatment of glycosphingolipid extracts from human pancreas were used. The antibody bound to all blood-group-A substances; alpha GalNAc, but not fucose, was essential for reactivity. In ELISA, Pa-G-14 also reacted with ovine and bovine submaxillary mucins but not with porcine submaxillary mucin. Binding to ovine submaxillary mucin…

Cancer ResearchAcetylgalactosaminemedicine.drug_classMolecular Sequence DataSubmandibular GlandMonoclonal antibodyFucoseEpitopeGlycosphingolipidschemistry.chemical_compoundEpitopesMiceAntigenAntibody SpecificityAntigens NeoplasmmedicineAnimalsHumansPancreasGlycoproteinschemistry.chemical_classificationSheepbiologyMucinMucinsOvine Submaxillary MucinAntibodies MonoclonalMolecular biologycarbohydrates (lipids)OncologychemistryBiochemistryCarbohydrate SequenceAntigens Surfacebiology.proteinCattleAntibodyGlycoproteinInternational journal of cancer
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Autophagy

2012

Klionsky, Daniel J. et al.

autophagy assays[SDV]Life Sciences [q-bio]AutolysosomeAutophagosome maturationautophagosomeBioinformaticsstressChaperone-mediated autophagyModelsLC3MESH: Animalsguidelinesautolysosome autophagosome flux LC3 lysosome phagophore stress vacuoleSettore BIO/06 - Anatomia Comparata E CitologiaComputingMilieux_MISCELLANEOUSSettore BIO/17Autophagy databaseautolysosome3. Good healthddc:540lysosomeEnergy and redox metabolism Mitochondrial medicine [NCMLS 4]methods [Biological Assay]Biological AssaySettore BIO/17 - ISTOLOGIANeuroniMAP1LC3BHumanautophagygenetics [Autophagy]AutofagiaMESH: Autophagy*/genetics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyAutofagia; Neuroni; istologiaBiologyModels BiologicalLC3; autolysosome; autophagosome; flux; lysosome; phagophore; stress; vacuoleddc:570AutophagyAnimalsHumansAutophagy-Related Protein 7[SDV.BC] Life Sciences [q-bio]/Cellular BiologyBiological Assay/methodsMolecular BiologyBiologyAutophagy; guidelines; autophagy assaysistologiaphagophoreMESH: HumansAnimals; Biological Assay; Humans; Models Biological; AutophagyvacuoleAnimal[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH: Models BiologicalPathogenesis and modulation of inflammation Infection and autoimmunity [N4i 1]Cell BiologyBiologicalAutophagy/geneticsfluxAutophagosome membraneAutophagy Protein 5Human medicineMESH: Biological Assay/methods*Neuroscienceautolysosome; autophagosome; flux; LC3; lysosome; phagophore; stress; vacuoleAutophagy
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ALLOPURINOL BLOCKS AORTIC ANEURYSM IN A MOUSE MODEL OF MARFAN SYNDROME VIA REDUCING AORTIC OXIDATIVE STRESS

2022

ABSTRACTBackgroundIncreasing evidence indicates that redox stress participates in MFS aortopathy, though its mechanistic contribution is little known. We reported elevated reactive oxygen species (ROS) formation and NADPH oxidase NOX4 upregulation in MFS patients and mouse aortae. Here we address the contribution of xanthine oxidoreductase (XOR), which catabolizes purines into uric acid and ROS in MFS aortopathy.Methods and ResultsIn aortic samples from MFS patients, XOR protein expression, revealed by immunohistochemistry, increased in both the tunicae intima and media of the dilated zone. In MFS mice (Fbn1C1041G/+), aortic XOR mRNA transcripts and enzymatic activity of the oxidase form (X…

Marfan syndromemedicine.medical_specialtyEstrès oxidatiuAortic aneurysmsAllopurinolAllopurinolBiochemistryMarfan SyndromeMicechemistry.chemical_compoundAortic aneurysmMetal·loproteïnasesPhysiology (medical)medicine.arteryInternal medicinemedicineAnimalsAortaAortaNADPH oxidasebiologybusiness.industryConnective tissues diseasesNOX4Enzyme inhibitorsHydrogen Peroxidemedicine.diseaseMetalloproteinasesAortic AneurysmÀcid úricDisease Models AnimalOxidative StressEndocrinologyInhibidors enzimàticschemistryXanthine dehydrogenaseOxidative stressbiology.proteinUric acidMalalties del teixit connectiuAneurismes aòrticsReactive Oxygen SpeciesbusinessOxidation-ReductionUric acidmedicine.drug
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Actin Filaments Are Involved in the Coupling of V0-V1 Domains of Vacuolar H+-ATPase at the Golgi Complex*

2016

We previously reported that actin-depolymerizing agents promote the alkalization of the Golgi stack and the trans-Golgi network. The main determinant of acidic pH at the Golgi is the vacuolar-type H+-translocating ATPase (V-ATPase), whose V1 domain subunits B and C bind actin. We have generated a GFP-tagged subunit B2 construct (GFP-B2) that is incorporated into the V1 domain, which in turn is coupled to the V0 sector. GFP-B2 subunit is enriched at distal Golgi compartments in HeLa cells. Subcellular fractionation, immunoprecipitation, and inversal FRAP experiments show that the actin depolymerization promotes the dissociation of V1-V0 domains, which entails subunit B2 translocation from Go…

0301 basic medicineVacuolar Proton-Translocating ATPasesGolgi ApparatusBiologyMicrofilamentBiochemistry03 medical and health sciencessymbols.namesakeCytosolHumansActin-binding proteinMolecular BiologyLipid raftActinGolgi membraneCell BiologyIntracellular MembranesGolgi apparatusHydrogen-Ion ConcentrationActin cytoskeletonCell biologyProtein Structure TertiaryCytosolActin Cytoskeleton030104 developmental biologysymbolsbiology.proteinHeLa Cells
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