Search results for "Intracellular Membranes"

showing 7 items of 47 documents

Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with α-actinin—Analysis of patient mutations

2005

Z-band alternatively spliced PDZ-containing protein (ZASP/Cypher) has an important role in maintaining Z-disc stability in striated and cardiac muscle. ZASP/Cypher interacts through its PDZ domain with the major Z-disc actin cross-linker, alpha-actinin. ZASP/Cypher also has a conserved sequence called the ZM-motif, and it is found in two alternatively spliced exons 4 and 6. We have shown earlier that the ZM-motif containing internal regions of two related proteins ALP and CLP36 interact with alpha-actinin rod region, and that the ZM-motif is important in targeting ALP to the alpha-actinin containing structures in cell. Here, we show that the ZASP/Cypher internal fragments containing either …

SarcomeresAmino Acid MotifsPDZ domainCHO Cellsmacromolecular substancesBiologyConserved sequenceStress fiber assemblyMyoblastsMiceExonCricetinaeStress FibersmedicineAnimalsHumansMyocyteActininMuscle SkeletalActinAdaptor Proteins Signal TransducingOrganellesGeneticsMyocardiumPoint mutationCardiac muscleExonsIntracellular MembranesCell BiologyLIM Domain Proteinsmusculoskeletal systemPeptide FragmentsCell biologymedicine.anatomical_structureMutationCardiomyopathiesProtein BindingExperimental Cell Research
researchProduct

Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis

2004

The tumor suppressor p53 exerts its anti-neoplastic activity primarily through the induction of apoptosis. We found that cytosolic localization of endogenous wild-type or trans-activation–deficient p53 was necessary and sufficient for apoptosis. p53 directly activated the proapoptotic Bcl-2protein Bax in the absence of other proteins to permeabilize mitochondria and engage the apoptotic program. p53 also released both proapoptotic multidomain proteins and BH3-only proteins [Proapoptotic Bcl-2family proteins that share only the third Bcl-2homology domain (BH3)] that were sequestered by Bcl-xL. The transcription-independent activation of Bax by p53 occurred with similar kinetics and concentra…

Tumor suppressor geneProtein ConformationUltraviolet RaysWheat Germ AgglutininsRecombinant Fusion Proteinsbcl-X ProteinApoptosisEndogenyMitochondrionBiologyPermeabilityHomology (biology)law.inventionMiceCytosollawProto-Oncogene ProteinsMitochondrial membrane permeabilizationAnimalsHumansCells CulturedCell Line Transformedbcl-2-Associated X ProteinCell NucleusMultidisciplinaryCytochromes cIntracellular MembranesGenes p53MitochondriaCell biologyCytosolGene Expression RegulationProto-Oncogene Proteins c-bcl-2ApoptosisLiposomesMutationSuppressorTumor Suppressor Protein p53biological phenomena cell phenomena and immunityCarrier ProteinsBH3 Interacting Domain Death Agonist ProteinHeLa CellsScience
researchProduct

Vitamin A deficiency causes oxidative damage to liver mitochondria in rats.

2000

Mitochondrial damage in rat liver induced by chronic vitamin A-deficiency was studied using three different groups of rats: (i) control rats, (ii) rats fed a vitamin A-free diet until 50 d after birth and (iii) vitamin A-deficient rats re-fed a control diet for 30 d. No statistical difference in body weight and food intake was found between control and vitamin A-deficient rats. Liver GSH concentration was similar in both groups. However, in vitamin A-deficient rats, the mitochondrial GSH/GSSG ratio was significantly lower and the levels of malondialdehyde (MDA) and 8-oxo-7, 8-dihydro-2'-deoxyguanosine (oxo8dG) were higher when compared to control rats. These values were partially restored i…

Vitaminmedicine.medical_specialtyAgingPopulationMitochondria LiverBiologyMitochondrionmedicine.disease_causeWeight GainBiochemistryMembrane Potentialschemistry.chemical_compoundMembrane LipidsPhysiology (medical)Internal medicineMalondialdehydemedicineDeoxyguanosineAnimalseducationVitamin Aeducation.field_of_studyGlutathione DisulfideVitamin A DeficiencyDeoxyguanosineGlutathioneIntracellular Membranesmedicine.diseaseMalondialdehydeFlow CytometryGlutathioneRatsVitamin A deficiencyEndocrinologychemistry8-Hydroxy-2'-DeoxyguanosineFemaleEnergy IntakeOxidative stressFree radical biologymedicine
researchProduct

Proteins and enzymes of the peroxisomal membrane in mammals.

1993

Proteins of the peroxisomal membrane can be schematically divided into two groups, one being made up of more or less characterized proteins with generally unknown functions and the other consisting of enzyme activities of which the corresponding proteins have not been characterized. In the present report, these proteins and enzymes are described with the addition of unpublished results regarding their induction by peroxisome proliferators at the post-transcriptional level. Integral membrane proteins (IMPs) can be isolated using an alkaline solution of sodium carbonate. A dozen of preponderant IMPs can be seen on sodium dodecyl sulfate polyacrylamide gel electrophoresis, and the major band c…

chemistry.chemical_classificationMammalsEndoplasmic reticulumMembrane ProteinsCell BiologyGeneral MedicineIntracellular MembranesPeroxisomeBiologyMicrobodieschemistry.chemical_compoundMembrane LipidsEnzymechemistryMembrane proteinBiochemistryBiosynthesisAcyltransferaseAnimalsHumansElectrophoresis Polyacrylamide GelIntegral membrane proteinPolyacrylamide gel electrophoresisBiology of the cell
researchProduct

Monoclonal antibody TeM 106 reacts with a tonoplast intrinsic protein of 106 kDa from Brassica oleracea L

1995

A monoclonal antibody, designated TeM 106, that recognizes an intrinsic protein from the vacuole membrane (tonoplast) of cauliflower (Brassica oleracea L. var. botrytis) is described. Mice were immunized with a tonoplast fraction that had been purified from differentiating meristematic cells from the cauliflower head. Hybridomas were generated and screened by means of Enzyme Linked Immuno Sorbent Assays for differential reactivity to tonoplast over non-related proteins (bovine serum albumin). One out of 14 reactive murine clones was selected on the basis of its stability, secretory efficiency, and high affinity of the secreted antibodies. TeM 106 is an IgM which was shown by indirect immuno…

medicine.drug_classBlotting WesternFluorescent Antibody TechniqueMannoseEnzyme-Linked Immunosorbent AssayBrassicaVacuoleMonoclonal antibodyEpitopeMicechemistry.chemical_compoundAntigenAntibody SpecificityConcanavalin AmedicineAnimalsElectrophoresis Gel Two-DimensionalBovine serum albuminPlant ProteinsGel electrophoresisbiologyAntibodies MonoclonalMembrane ProteinsSerum Albumin BovineIntracellular MembranesCell BiologyMolecular biologyMolecular WeightKineticsBiochemistrychemistryVacuolesbiology.proteinElectrophoresis Polyacrylamide GelPlant LectinsAntibodyJournal of Cell Science
researchProduct

Lysosomal trafficking in rat cardiac myocytes.

1990

By immunolabeling of cryosections, we have characterized in rat cardiac myocytes the cation-independent mannose-6-phosphate receptor (MPR), a lysosomal membrane glycoprotein, lgp120, and a lysosomal enzyme, MEP (homologous to cathepsin L). Most of the MPR label was located in large membrane-filled structures (MPR structures) in large clusters of mitochondria adjacent to but distinct from the Golgi complex. Lpg120 and MEP showed typical lysosomal localization throughout the cell, often associated with regions that appeared to contain autophagosome-like structures. In addition, MEP and lgp120 co-localized within MPR structures. MEP and MPR were localized inside the lumen of MPR structures. M…

medicine.medical_specialtyHistologyCathepsin LImmunoblottingFluorescent Antibody TechniqueReceptors Cell SurfaceMitochondrionMitochondria HeartReceptor IGF Type 2Cathepsin LImmunolabelingsymbols.namesakeAntigens CDLysosomal-Associated Membrane Protein 1Internal medicineLysosomeEndopeptidasesmedicineAnimalsFrozen SectionsMyocyteReceptorchemistry.chemical_classificationMembrane GlycoproteinsbiologyMyocardiumLysosome-Associated Membrane GlycoproteinsIntracellular MembranesGolgi apparatusCathepsinsRatsCell biologyCysteine EndopeptidasesMicroscopy ElectronEndocrinologymedicine.anatomical_structureAnimals NewbornLiverchemistrybiology.proteinsymbolsCattleAnatomyLysosomesGlycoproteinJournal of Histochemistry & Cytochemistry
researchProduct

In vitro studies on the activation of the hepatitis C virus NS3 proteinase by the NS4A cofactor.

1996

AbstractProteolytic processing of the nonstructural proteins of the hepatitis C virus (HCV) is mediated by two viral proteinases: the NS2-3 proteinase cleaving at the NS2/3 junction and the NS3 serine-type proteinase responsible for processing at the NS3/4A, NS4A/B, NS4B/5A, and NS5A/B sites. Activity of the NS3 proteinase is modulated by NS4A. In the absence of this cofactor processing at the NS3-dependent sites does not occur or, in the case of the NS5A/B junction, is poor but increased when NS4A is present. Although recent studies demonstrated that proteinase activation requires direct interaction between NS3 and NS4A, the mechanism by which NS4A exerts the activation function is not kno…

virusesMolecular Sequence DataHepacivirusBiologyViral Nonstructural ProteinsCell LineEnzyme activatorProteinase 3VirologyCricetinaeMicrosomesAnimalsHumansAmino Acid SequenceBinding siteNS5APeptide sequenceSequence Deletionchemistry.chemical_classificationNS3Binding SitesBase Sequencevirus diseasesIntracellular Membranesbiochemical phenomena metabolism and nutritionMolecular biologyIn vitrodigestive system diseasesAmino acidEnzyme ActivationBiochemistrychemistryDNA ViralPeptidesHeLa CellsVirology
researchProduct