Search results for "Hsp40"

showing 10 items of 13 documents

Hsp40 Is Involved in Cilia Regeneration in Sea Urchin Embryos

2003

In a previous paper we demonstrated that, in Paracentrotus lividus embryos, deciliation represents a specific kind of stress that induces an increase in the levels of an acidic protein of about 40 kD (p40). Here we report that deciliation also induces an increase in Hsp40 chaperone levels and enhancement of its ectodermal localization. We suggest that Hsp40 might play a chaperoning role in cilia regeneration.

0301 basic medicineEmbryo NonmammalianHistologyParacentrotus lividus03 medical and health sciences0302 clinical medicineStress PhysiologicalCulture Techniquesbiology.animalEctodermBotanyAnimalsRegenerationElectrophoresis Gel Two-DimensionalCiliaSettore BIO/06 - Anatomia Comparata E CitologiaSea urchinHeat-Shock ProteinsCentrosomebiologyCiliumEmbryoHSP40 Heat-Shock ProteinsSea urchin embryobiology.organism_classificationHsp40 deciliation sea urchinCell biology030104 developmental biologySea UrchinsAnatomy030217 neurology & neurosurgeryMolecular Chaperones
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Assessment of Targeted Next-Generation Sequencing as a Tool for the Diagnosis of Charcot-Marie-Tooth Disease and Hereditary Motor Neuropathy

2016

Charcot-Marie-Tooth disease is characterized by broad genetic heterogeneity with >50 known disease-associated genes. Mutations in some of these genes can cause a pure motor form of hereditary motor neuropathy, the genetics of which are poorly characterized. We designed a panel comprising 56 genes associated with Charcot-Marie-Tooth disease/hereditary motor neuropathy. We validated this diagnostic tool by first testing 11 patients with pathological mutations. A cohort of 33 affected subjects was selected for this study. The DNAJB2 c.352+1G>A mutation was detected in two cases; novel changes and/or variants with low frequency (50 known disease-associated genes. Mutations in some of these gene…

0301 basic medicineMaleDiseaseBioinformaticsDNA sequencingPathology and Forensic Medicine03 medical and health sciences0302 clinical medicineCharcot-Marie-Tooth DiseaseMedicineHumansGeneGeneticsbusiness.industryGenetic heterogeneityHaplotypeCase-control studyHigh-Throughput Nucleotide SequencingReproducibility of ResultsHSP40 Heat-Shock Proteins030104 developmental biologyHaplotypesCase-Control StudiesMutation (genetic algorithm)MutationMolecular MedicineFemalebusinessHereditary Sensory and Motor Neuropathy030217 neurology & neurosurgeryFounder effectMolecular Chaperones
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Overexpression of human homologs of the bacterial DnaJ chaperone in the synovial tissue of patients with rheumatoid arthritis

1999

Objective To study the expression of the chaperone family of J proteins in the synovial tissue of patients with rheumatoid arthritis (RA) or osteoarthritis. Methods Rabbit antibodies specific for a synthetic peptide (pHSJ1: EAYEVLSDKHKREIYD), representing the most conserved part of all J domains thus far identified—among them the Drosophila tumor suppressor Tid56—were used in immunohistochemical analyses of frozen sections of synovial tissue and immunoblotting of protein extracts of adherent synovial cells. IgG specific for Tid56 was also used. Results Both antisera predominantly and intensely stained synovial lining cells from RA patients; other cells did not stain or stained only faintly.…

AdultMalePathologymedicine.medical_specialtyMolecular Sequence DataImmunologyEnzyme-Linked Immunosorbent Assaymedicine.disease_causeAutoimmunityArthritis RheumatoidImmunoenzyme TechniquesMiceBacterial ProteinsRheumatologyAntibody SpecificityOsteoarthritismedicineAnimalsHumansImmunology and AllergyPharmacology (medical)Amino Acid SequenceCells CulturedHeat-Shock ProteinsAgedAntiserumFrozen section procedurebiologybusiness.industrySynovial MembraneHSP40 Heat-Shock ProteinsMiddle AgedIn vitromedicine.anatomical_structureSynovial Cellbiology.proteinImmunohistochemistryFemaleSynovial membraneAntibodybusinessArthritis & Rheumatism
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Endoplasmic reticulum‐resident chaperones modulate the inflammatory and angiogenic responses of endothelial cells

2015

SummaryBackground Wound healing depends on a well-balanced regulation of inflammation and angiogenesis. In chronic wounds the healing process is disturbed and inflammation persists. Regulation of wound closure is controlled by transmembrane and extracellular proteins, the folding and maturation of which occur in the endoplasmic reticulum (ER) by ER-resident chaperone machinery. Objectives To study the role of the ER-resident chaperones BiP/Grp78, its cochaperone Mdg1/ERdJ4, and Grp94 in chronic, nonhealing wounds. Methods Immunohistochemical staining of these chaperones in individual human biopsies and investigation of the possible role of BiP and Mdg1 in endothelial cells, focusing on thei…

Chronic woundChemokineAngiogenesisDown-RegulationNeovascularization PhysiologicInflammationDermatologyEndoplasmic ReticulumProinflammatory cytokinemedicineHumansEndoplasmic Reticulum Chaperone BiPCells CulturedHeat-Shock ProteinsInflammationWound HealingMembrane GlycoproteinsbiologyTumor Necrosis Factor-alphaEndoplasmic reticulumEndothelial CellsMembrane ProteinsHSP40 Heat-Shock ProteinsCell biologyChaperone (protein)Chronic Diseasebiology.proteinmedicine.symptomWound healingMolecular ChaperonesBritish Journal of Dermatology
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Tumor suppression inDrosophila is causally related to the function of thelethal(2)tumorous imaginal discs gene, adnaJ homolog

1995

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) causes in homozygotes malignant growth of cells of the imaginal discs and the death of the mutant larvae at the time of puparium formation. We describe the molecular cloning of the l(2)tid+ gene and its temporal expression pattern in the wild-type and mutant alleles. Germ line rescue of the tumor phenotype was achieved with a 7.0 kb Hindlll-fragment derived from the polytene chromosome band 59F5. The l(2)tid+ gene spans approximately 2.5 kb of genomic DNA. The protein coding region, 1,696 bps long, is divided by an intron into two exons. The predicted Tid56 protein contains 518 amino acids and posse…

DNA ComplementarySaccharomyces cerevisiae ProteinsTumor suppressor geneMolecular Sequence DataMutantGenes InsectSaccharomyces cerevisiaeAnimals Genetically ModifiedFungal ProteinsMitochondrial ProteinsSpecies SpecificityEscherichia coliGeneticsAnimalsDrosophila ProteinsHumansGenes Tumor SuppressorAmino Acid SequenceCloning MolecularGeneAllelesHeat-Shock ProteinsPolytene chromosome bandBase SequenceSequence Homology Amino AcidbiologyEscherichia coli ProteinsPupaChromosome MappingExonsNeoplasms ExperimentalCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyImaginal discDrosophila melanogasterLarvaDNAJA2Drosophila melanogasterSequence AlignmentDrosophila ProteinDevelopmental BiologyDevelopmental Genetics
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Mitochondrial localization and temporal expression of the Drosophila melanogaster DnaJ homologous tumor suppressor Tid50

1998

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (tid) was identified as a homolog of all dnaJ-like genes known to date which have been well preserved in evolution. Homozygous D. melanogaster l(2)tid mutants l(2)tid1, l(2)tid2 and l(2)tid3 are characterized by neoplastic transformation of the adult integumental primordia, the imaginal discs, and the death at the time of puparium formation. The first part of this study is concerned with the identification and subcellular localization of the l(2)tid-encoded protein, Tid50. The second part examines its tissue specific expression during wild-type development and in tumorous imaginal discs. To specify the functi…

Embryo NonmammalianTumor suppressor geneMutantGenes InsectCell FractionationBiochemistryCell LineMitochondrial ProteinsMelanogasterAnimalsDrosophila ProteinsGenes Tumor SuppressorNeoplastic transformationRNA MessengerGeneHeat-Shock ProteinsbiologyPupaGene Expression Regulation DevelopmentalRNANeoplasms ExperimentalSequence Analysis DNAOriginal ArticlesCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyMitochondriaGene Expression Regulation NeoplasticImaginal discDrosophila melanogasterOrgan SpecificityLarvaRabbitsDrosophila melanogasterCell Stress & Chaperones
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High levels of the molecular chaperone Mdg1/ERdj4 reflect the activation state of endothelial cells

2003

Mdg1/ERdj4, a mammalian chaperone that belongs to the HSP40 protein family, has been reported to be located in the endoplasmic reticulum (ER), is induced by ER stress, and protects ER stressed cells from apoptosis. Here we show that under normal physiological conditions, Mdg1/ERdj4 is expressed at various levels in the vasculature due to different activation states of the endothelium. To elucidate the stimuli that induce ER stress and thus upregulate Mdg1/ERdj4, we investigated the effect of several endothelium specific stressors on its expression. Mdg1/ERdj4 mRNA is induced by activated macrophages, by nitric oxide (NO) and heat shock, and during terminal cell differentiation, whereas shea…

EndotheliumCell SurvivalCellular differentiationApoptosisCell CommunicationEndoplasmic ReticulumNitric OxideMiceStress PhysiologicalmedicineAnimalsHumansRNA MessengerHeat shockEndoplasmic Reticulum Chaperone BiPbiologyMacrophagesEndoplasmic reticulumMembrane ProteinsProteinsCell BiologyHSP40 Heat-Shock ProteinsCoculture TechniquesUp-RegulationHsp70Cell biologyProtein Transportmedicine.anatomical_structureApoptosisChaperone (protein)biology.proteinUnfolded protein responseEndothelium VascularStress MechanicalCarrier ProteinsCell NucleolusHeat-Shock ResponseHeLa CellsMolecular ChaperonesExperimental Cell Research
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Specific and promiscuous functions of multiple DnaJ proteins in Synechocystis sp. PCC 6803

2011

Cyanobacterial genomes typically encode multiple Hsp70 (DnaK) and Hsp40 (DnaJ) chaperones, and in the genome of the cyanobacteriumSynechocystisPCC 6803, three DnaK proteins are encoded together with seven DnaJ proteins. While only two of the DnaJ proteins can complement the growth defect of anEscherichia coliΔdnaJstrain, only disruption of thednaJgenesll0897resulted in a growth defect at elevated temperatures. Based on the domain structure and the phenotype observed following disruption of the encoding gene, Sll0897 can be classified as a canonical heat-shock protein inSynechocystis. Furthermore, mostdnaJgenes could be deleted individually, whereas disruption of the gene encoding the DnaJ S…

Geneticsendocrine systembiologySynechocystisSynechocystisHSP40 Heat-Shock Proteinsbiology.organism_classificationDNAJ ProteinMicrobiologyGenomePhenotypeProtein Structure TertiaryProtein structureBacterial ProteinsMultigene FamilyDNAJA2DNAJB1GeneMicrobiology
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Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.

2008

AbstractThe hepatitis B virus L protein forms a dual topology in the endoplasmic reticulum (ER) via a process involving cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain. Here, we show that preS posttranslocation depends on the action of the ER chaperone BiP. To modulate the in vivo BiP activity, we designed an approach based on overexpressing its positive and negative regulators, ER-localized DnaJ-domain containing protein 4 (ERdj4) and BiP-associated protein (BAP), respectively. The feasibility of this approach was confirmed by demonstrating that BAP, but not ERdj4, destabilizes the L/BiP complex. Overexpressing BAP or ERdj4 inhibits…

Hepatitis B virusgenetic structuresBiPBiophysicsHemagglutinin (influenza)Chromosomal translocationmacromolecular substancesmedicine.disease_causeEndoplasmic ReticulumBiochemistryCell LineAdenosine TriphosphateViral Envelope ProteinsStructural BiologyIn vivoCalnexinHBVGeneticsmedicineHumansMolecular BiologyEndoplasmic Reticulum Chaperone BiPTranslocational regulationHeat-Shock ProteinsHepatitis B virusbiologyEndoplasmic reticulumMembrane ProteinsCell BiologyHSP40 Heat-Shock ProteinsMolecular biologyProtein Structure TertiaryProtein TransportDual topologyMembrane topologyProtein BiosynthesisMembrane topologybiology.proteinPosttranslational translocationMolecular ChaperonesFEBS letters
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Molecular Cloning and mRNA Expression of Heat Shock Protein Genes and Their Response to Cadmium Stress in the Grasshopper Oxya chinensis

2015

Heat shock proteins (Hsps) are highly conserved molecular chaperones that are synthesized in response to stress. In this study, we cloned the full-length sequences of the Grp78 (glucose-regulated protein 78), Hsp70, Hsp90, and Hsp40 genes from the Chinese rice grasshopper Oxya chinensis. The full-length cDNA sequences of OcGrp78, OcHsp70, OcHsp90, and OcHsp40 contain open reading frames of 1947, 1920, 2172, and 1042 bp that encode proteins of 649, 640, 724, and 347 amino acids, respectively. Fluorescent real-time quantitative PCR (RT-qPCR) was performed to quantify the relative transcript levels of these Hsp genes in different tissues and developmental stages. The mRNAs encoding these four …

MaleZygotelcsh:MedicineGrasshoppersOpen Reading FramesStress PhysiologicalComplementary DNAHeat shock proteinGene expressionAnimalsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsRNA MessengerCloning Molecularlcsh:ScienceEndoplasmic Reticulum Chaperone BiPGeneHeat-Shock ProteinsRegulation of gene expressionMultidisciplinarybiologylcsh:RHSP40 Heat-Shock ProteinsHsp90Molecular biologyHsp70Real-time polymerase chain reactionGene Expression RegulationLarvabiology.proteinInsect ProteinsFemalelcsh:QResearch ArticleCadmiumSignal TransductionPLOS ONE
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