Search results for "Secretor"

showing 10 items of 159 documents

Histo-blood group antigens in children with symptomatic rotavirus infection

2019

Group A rotaviruses are a major cause of acute gastroenteritis in children. The diversity and unequal geographical prevalence of rotavirus genotypes have been linked to histo-blood group antigens (HBGAs) in different human populations. In order to evaluate the role of HBGAs in rotavirus infections in our population, secretor status (FUT2+), ABO blood group, and Lewis antigens were determined in children attended for rotavirus gastroenteritis in Valencia, Spain. During three consecutive years (2013&ndash

0301 basic medicineMaleSalivaviruseslcsh:QR1-502medicine.disease_causelcsh:MicrobiologysusceptibilityBlood group antigensFecesfluids and secretionsRotavirusGenotypeChildGastroenterologiaeducation.field_of_studyvirus diseaseshisto-blood group antigens (HBGAs)Rotavirus infectionInfectious DiseasesChild PreschoolBlood Group AntigensFemalegastroenteritisGenotypeVirus RNA030106 microbiologyPopulationRotavirus InfectionsArticlesecretor03 medical and health sciencesAntigenVirologyABO blood group systemmedicineHumansGenetic Predisposition to DiseaseABO group antigenseducationSalivabusiness.industryInfant NewbornInfantVirology030104 developmental biologyrotavirusLewisSpainbusiness
researchProduct

Identification of Cysteine Ubiquitylation Sites on the Sec23A Protein of the COPII Complex Required for Vesicle Formation from the ER

2017

Background COPII is a multiprotein complex that surrounds carrier vesicles budding from the Endoplasmic Reticulum and allows the recruitment of secretory proteins. The Sec23a protein plays a crucial role in the regulation of the dynamics of COPII formation ensuring the proper function of the secretory pathway. Objective Since few evidences suggest that ubiquitylation could have a role in the COPII regulation, the present study was aimed to establish whether the Sec23a component of the vesicular envelope COPII could be ubiquitylated. Method Sec23a ubiquitylation was revealed by co-immunoprecipitation experiments. Recombinant Sec23a was gel-purified and analyzed by mass spectrometry subjected…

0301 basic medicineMultiprotein complexUbiquitylationbiologyVescicular transportEndoplasmic reticulumVesicleSEC23AArticleSec23aGeneral Biochemistry Genetics and Molecular BiologyCell biology03 medical and health sciences030104 developmental biologySecretory proteinUbiquitinERESbiology.proteinCOPIICOPIISecretory pathwayThe Open Biochemistry Journal
researchProduct

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
researchProduct

The interactions between host glycobiology, bacterial microbiota, and viruses in the gut

2018

Rotavirus (RV) and norovirus (NoV) are the major etiological agents of viral acute gastroenteritis worldwide. Host genetic factors, the histo-blood group antigens (HBGA), are associated with RV and NoV susceptibility and recent findings additionally point to HBGA as a factor modulating the intestinal microbial composition. In vitro and in vivo experiments in animal models established that the microbiota enhances RV and NoV infection, uncovering a triangular interplay between RV and NoV, host glycobiology, and the intestinal microbiota that ultimately influences viral infectivity. Studies on the microbiota composition in individuals displaying different RV and NoV susceptibilities allowed th…

0301 basic medicineRotavirus030106 microbiologylcsh:QR1-502MicrobiologiaReviewBiologymedicine.disease_causelcsh:MicrobiologyMicrobiology03 medical and health sciencesSecretorAntigenstomatognathic systemVirologyRotavirusHisto-blood group antigens (HBGAs)medicineAnimalsHumansGlycomicsInfectivityGlycobiologyHost (biology)MicrobiotaNorovirusAcute gastroenteritisGastroenteritisVirusGastrointestinal Tract030104 developmental biologyInfectious DiseasesHost susceptibilityHost-Pathogen InteractionsFucosyltransferase-2 gene (FUT2)NorovirusReceptors VirusMicrobiota composition
researchProduct

Drosophila and humans share similar mechanisms of insulin secretion

2017

Drosophila and humans share similar mechanisms of insulin secretion

0301 basic medicineanimal structures[SDV]Life Sciences [q-bio][SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/NeurobiologyfungiGeneral MedicineBiologybiology.organism_classificationSomatomedinGeneral Biochemistry Genetics and Molecular Biology3. Good healthCell biology03 medical and health sciences030104 developmental biologyFeeding behavior[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]LeucineDrosophila melanogasterInsulin secretion[SDV.AEN]Life Sciences [q-bio]/Food and NutritionSecretory pathwayDrosophila ProteinComputingMilieux_MISCELLANEOUS
researchProduct

Avoided motifs: short amino acid strings missing from protein datasets.

2020

Abstract According to the amino acid composition of natural proteins, it could be expected that all possible sequences of three or four amino acids will occur at least once in large protein datasets purely by chance. However, in some species or cellular context, specific short amino acid motifs are missing due to unknown reasons. We describe these as Avoided Motifs, short amino acid combinations missing from biological sequences. Here we identify 209 human and 154 bacterial Avoided Motifs of length four amino acids, and discuss their possible functionality according to their presence in other species. Furthermore, we determine two Avoided Motifs of length three amino acids in human proteins…

0301 basic medicinechemistry.chemical_classificationProtein functionAmino Acid Motifs030102 biochemistry & molecular biologyClinical BiochemistryComputational BiologyProteinsContext (language use)Computational biologyBiologyBiochemistryAmino acid03 medical and health sciences030104 developmental biologySecretory proteinchemistryAmino acid compositionCytoplasmMolecular BiologyHuman proteinsSequence AlignmentBiological chemistryReferences
researchProduct

The Unfolded Protein Response Plays a Predominant Homeostatic Role in Response to Mitochondrial Stress in Pancreatic Stellate Cells.

2016

Activated pancreatic stellate cells (PaSC) are key participants in the stroma of pancreatic cancer, secreting extracellular matrix proteins and inflammatory mediators. Tumors are poorly vascularized, creating metabolic stress conditions in cancer and stromal cells that necessitate adaptive homeostatic cellular programs. Activation of autophagy and the endoplasmic reticulum unfolded protein response (UPR) have been described in hepatic stellate cells, but the role of these processes in PaSC responses to metabolic stress is unknown. We reported that the PI3K/mTOR pathway, which AMPK can regulate through multiple inputs, modulates PaSC activation and fibrogenic potential. Here, using primary a…

0301 basic medicinelcsh:MedicineApoptosisMitochondrionAMP-Activated Protein KinasesEndoplasmic ReticulumBiochemistrychemistry.chemical_compoundMiceeIF-2 KinasePhosphatidylinositol 3-Kinases0302 clinical medicineFluorescence MicroscopyCell SignalingTumor Microenvironment2.1 Biological and endogenous factorsSmall interfering RNAsAetiologylcsh:ScienceEnergy-Producing OrganellesCancerMice KnockoutMicroscopyMultidisciplinarySecretory PathwayCell DeathTOR Serine-Threonine KinasesLight MicroscopySignaling CascadesCell biologyMitochondriaNeoplasm ProteinsUp-RegulationNucleic acidsCell Processes030220 oncology & carcinogenesisCellular Structures and OrganellesResearch ArticleSignal TransductionProgrammed cell deathCell PhysiologyGeneral Science & TechnologyAutophagic Cell DeathKnockoutBiologyBioenergeticsResearch and Analysis MethodsStress Signaling Cascade03 medical and health sciencesGeneticsAutophagyAnimalsNon-coding RNAPancreasPI3K/AKT/mTOR pathwaylcsh:RAutophagyAMPKBiology and Life SciencesCell BiologyCell MetabolismGene regulationPancreatic NeoplasmsEnzyme Activation030104 developmental biologychemistryHepatic stellate cellUnfolded protein responseUnfolded Protein ResponseRNAlcsh:QGene expressionInterleukin-4Digestive DiseasesRottlerinTranscription Factor CHOP
researchProduct

alpha 2-COP is involved in early secretory traffic in Arabidopsis and is required for plant growth

2017

[EN] COP (coat protein) I-coated vesicles mediate intra-Golgi transport and retrograde transport from the Golgi to the endoplasmic reticulum. These vesicles form through the action of the small GTPase ADP-ribosylation factor 1 (ARF1) and the COPI heptameric protein complex (coatomer), which consists of seven subunits (alpha-, beta-, beta' -, gamma-, delta-, epsilon- and xi-COP). In contrast to mammals and yeast, several isoforms for coatomer subunits, with the exception of gamma and delta, have been identified in Arabidopsis. To understand the role of COPI proteins in plant biology, we have identified and characterized a loss-of-function mutant of alpha 2-COP, an Arabidopsis alpha-COP isofo…

0301 basic medicineα2-COPPhysiologyUbiquitin-Protein LigasesProtein subunitMutantSEC31ArabidopsisPlant ScienceEndoplasmic ReticulumCoatomer ProteinP24 family protein03 medical and health sciencessymbols.namesakeBotanyBIOQUIMICA Y BIOLOGIA MOLECULARCOPIICOPIISecretory pathwayCOPICoat proteinArabidopsis ProteinsChemistryEndoplasmic reticulumAlpha 2-COPBiological TransportCOPIGolgi apparatusSEC31.Cell biologyAlpha 1-COPα1-COP030104 developmental biologyCoatomerGolgi apparatussymbolsCOPII Golgi apparatusResearch Paper
researchProduct

OSIP1 is a self‐assembling DUF3129 protein required to protect fungal cells from toxins and stressors

2021

International audience; Secreted proteins are key players in fungal physiology and cell protection against external stressing agents and antifungals. Oak stress-induced protein 1 (OSIP1) is a fungal-specific protein with unknown function. By using Podospora anserina and Phanerochaete chrysosporium as models, we combined both in vivo functional approaches and biophysical characterization of OSIP1 recombinant protein. The P. anserina OSIP1(Delta) mutant showed an increased sensitivity to the antifungal caspofungin compared to the wild type. This correlated with the production of a weakened extracellular exopolysaccharide/protein matrix (ECM). Since the recombinant OSIP1 from P. chrysosporium …

0303 health sciencesAntifungal Agentsbiology030306 microbiologyMutantWild typePhanerochaetebiology.organism_classificationMicrobiologyPodospora anserinalaw.inventionCell biologyFungal Proteins03 medical and health sciencesChaotropic agentSecretory proteinPodosporalawRecombinant DNAExtracellular[PHYS.COND.CM-MS]Physics [physics]/Condensed Matter [cond-mat]/Materials Science [cond-mat.mtrl-sci]PhanerochaeteEcology Evolution Behavior and SystematicsSignal Transduction030304 developmental biology
researchProduct

Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29

2002

Abstract ERp29 is a soluble protein localized in the endoplasmic reticulum (ER) of eukaryotic cells, which is conserved in all mammalian species. The N-terminal domain of ERp29 displays sequence and structural similarity to the protein disulfide isomerase despite the lack of the characteristic double cysteine motif. Although the exact function of ERp29 is not yet known, it was hypothesized that it may facilitate folding and/or export of secretory proteins in/from the ER. ERp29 is induced by ER stress, i.e. accumulation of unfolded proteins in the ER. To gain an insight into the mechanisms regulating ERp29 expression we have cloned and characterized the rat ERp29 gene and studied in details …

5' Flanking RegionRecombinant Fusion ProteinsMolecular Sequence DataCHO CellsBiologyCell LineMiceCricetinaeSequence Homology Nucleic AcidGene expressionTumor Cells CulturedGeneticsAnimalsHumansRNA MessengerLuciferasesPromoter Regions GeneticProtein disulfide-isomeraseGeneHeat-Shock ProteinsPhylogenyBase SequenceGene Expression ProfilingEndoplasmic reticulumPromoter3T3 CellsDNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsRatsHousekeeping geneSecretory proteinGenesUnfolded protein responseFemaleTranscription Initiation SiteSequence AlignmentHeLa CellsGene
researchProduct