Search results for "Proteasomal degradation"

showing 4 items of 4 documents

Characterization of a mutant form of human apolipoprotein B (Thr26_Tyr27del) associated with familial hypobetalipoproteinemia

2016

We have previously identified a deletion mutant of human apoB [apoB (Thr26_Tyr27del)] in a subject with primary hypobetalipoproteinemia. The present study determined the effect of Thr26_Tyr27del mutation on apoB secretion using transfected McA-RH7777 cells. Transient or stable transfection of apoB-48 containing the Thr26_Tyr27del mutation showed drastically reduced secretion of the mutant as compared to wild-type apoB-48. No lipoproteins containing the mutant apoB-48 were secreted into the medium. Incubation of transfected cells in a lipid-rich medium in the presence of cycloheximide showed rapid turnover of cell-associated mutant apoB-48 as compared to that of wild-type apoB-48. Immunofluo…

0301 basic medicineSettore MED/09 - Medicina InternaTime FactorsApolipoprotein B-48 secretionApolipoprotein BMutantDNA Mutational AnalysisApolipoprotein B mutation Apolipoprotein B-48 secretion Hypobetalipoproteinemia Proteasomal degradation030204 cardiovascular system & hematologymedicine.disease_causeEndoplasmic ReticulumHypobetalipoproteinemiaschemistry.chemical_compound0302 clinical medicineProteasomal degradationProteolysiSequence DeletionMutationbiologyMedicine (all)TransfectionProteasome InhibitorPhenotypeBiochemistryApolipoprotein B-100lipids (amino acids peptides and proteins)Proteasome InhibitorsHumanHeterozygoteProteasome Endopeptidase ComplexTime FactorCycloheximideTransfectiondigestive systemCell LineDNA Mutational Analysi03 medical and health sciencesmedicineHumansSecretionGenetic Predisposition to DiseaseMolecular BiologyEndoplasmic reticulumnutritional and metabolic diseasesCell Biologymedicine.diseaseMolecular biology030104 developmental biologychemistryProteolysisbiology.proteinHypobetalipoproteinemiaApolipoprotein B mutationApolipoprotein B-48Hypobetalipoproteinemia
researchProduct

The receptor protein tyrosine phosphatase PTPRJ negatively modulates the CD98hc oncoprotein in lung cancer cells.

2018

PTPRJ, a receptor protein tyrosine phosphatase strongly downregulated in human cancer, displays tumor suppressor activity by negatively modulating several proteins involved in proliferating signals. Here, through a proteomic-based approach, we identified a list of potential PTPRJ-interacting proteins and among them we focused on CD98hc, a type II glycosylated integral membrane protein encoded by SLC3A2, corresponding to the heavy chain of a heterodimeric transmembrane amino-acid transporter, including LAT1. CD98hc is widely overexpressed in several types of cancers and contributes to the process of tumorigenesis by interfering with cell proliferation, adhesion, and migration. We first valid…

0301 basic medicineCD98hcChemistryCell growthCellPTPRJProtein tyrosine phosphatasemedicine.disease_causeProtein tyrosine phosphatase03 medical and health scienceschemistry.chemical_compound030104 developmental biologymedicine.anatomical_structureProteasomal degradationOncologyMG132Cancer cellCancer researchmedicineProteasome inhibitorGene silencingLung cancerCarcinogenesismedicine.drugResearch Paper
researchProduct

Rôle des protéines de choc thermique dans la régulation du facteur de transcription HIF

2011

Both HIF1α and HIF2α proteins are highly involved in the development of pathologies, such as cancers, which are prime public health issues. These proteins are primarily controlled at the protein level by ubiquitin-dependant degradation, and regulate numerous cellular processes which are likely to favor the development of these diseases. A recent issue in therapeutic research is to identify partners that might regulate the expression and the activity of the HIFα proteins, with the aim to elaborate targeted therapies. Heat shock proteins (HSPs) form a family of proteins whose main function is to regulate protein homeostasis in cells, which they achieve through interaction with the ubiquitin-p…

[SDV.SA]Life Sciences [q-bio]/Agricultural sciences[SDV.SA] Life Sciences [q-bio]/Agricultural sciences[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyUbiquitinProtéine clienteDégradation protéasomaleHSP27UbiquitineClient proteinProteasomal degradation[ SDV.MHEP ] Life Sciences [q-bio]/Human health and pathologyHSP90Inhibiteurs d’HSP90HIF2α[ SDV.SA ] Life Sciences [q-bio]/Agricultural sciences[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyHSP90 inhibitors
researchProduct

Direct and indirect measurements of enhanced phenolic bioavailability from litchi pericarp procyanidins by Lactobacillus casei-01

2017

Litchi pericarp procyanidins (LPP) are dietary supplements with high antioxidant activity, but poor oral bioavailability and efficacy. Lactobacillus casei (L. casei-01) can transform flavan-3-ols from litchi pericarp and increase their antioxidant ability; thus, L. casei-01 with LPP was administered to rats for four and eight weeks to study the effect of such a combination on metabolic parameters and on phase II metabolism and detoxification pathways in the liver as an indirect measure for phenolic bioavailability. Our data indicated that the T-AOC of the plasma, the liver GSH-Px and GSH-ST activity, and the expression of UGT and SULT isoforms in the liver of the rats were all enhanced afte…

Male0301 basic medicineURINARY-EXCRETIONAntioxidantmedicine.medical_treatmentCHINENSIS PERICARPCatechinRats Sprague-DawleyBiotransformationIngestionFood scienceBiotransformationGENE-EXPRESSIONGlutathione TransferasebiologyChemistryfood and beverages04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceLacticaseibacillus caseiLiverBiochemistryUDP-GLUCURONOSYLTRANSFERASE; PROTEASOMAL DEGRADATION; ANTIOXIDANT ACTIVITY; PROBIOTIC BACTERIA; CHINENSIS PERICARP; URINARY-EXCRETION; GENE-EXPRESSION; IN-VITRO; NRF2; POLYPHENOLSPROTEASOMAL DEGRADATIONPROBIOTIC BACTERIALactobacillus caseiAbsorption (skin)NRF203 medical and health sciencesPOLYPHENOLS0404 agricultural biotechnologyLitchiPhenolsDetoxificationmedicineAnimalsBiflavonoidsProanthocyanidinsGlutathione PeroxidasePlant ExtractsUDP-GLUCURONOSYLTRANSFERASEIN-VITRObiology.organism_classificationRatsBioavailabilitybody regionsTransformation (genetics)030104 developmental biologyFruitANTIOXIDANT ACTIVITYFood ScienceFood & Function
researchProduct