Search results for "Hsp"

showing 10 items of 557 documents

HSP110 : role in colorectal cancer development and immunogenicity

2015

Our team studies HSPs, including HSP110. HSPs are chaperones involved in the folding of newly synthesized and denatured proteins. HSPs are overexpressed under stress conditions and are involved in cell survival thanks to their anti-apoptotic and anti-aggregation functions. HSP110 is overexpressed in colorectal cancer and is associated with a poor prognosis. The expression of a mutant HSP110, named HSP110DE9, has been shown in MSI colorectal cancer. This one was shown to act there as a dominant negative, by binding HSP110 and inhibiting its functions. Its expression sensitizes cancer cells to chemotherapy and is associated with a better prognosis for patients.I was first interested in HSP110…

STAT3Cancer colorectal[SDV.MHEP] Life Sciences [q-bio]/Human health and pathologyMacrophage polarizationHSP110DE9Colorectal cancerHSP110
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Localization of HSP70, Cdc2, and cyclin B in sea urchin oocytes in non-stressed conditions.

2003

In Paracentrotus lividus embryos, a Mediterranean sea urchin species, HSP70 is present in all the cells. During cell division it localizes under normal growth conditions on the centrosomes and on the whole isolated mitotic apparatus. Now, in situ hybridization, Western blot analyses, and immunohistochemistry show that the HSP70 mRNA is present in both small and large P. lividus oocytes, that all four isoforms of HSP70 can be found also in the oocytes, and that a certain amount of HSP70 localizes on asters and spindles during polar body formation. Moreover, two representative cell-cycle related proteins, cyclin B, and Cdc2, are present both in small and large oocytes, concentrating in the ge…

Sea urchinCell divisionBlotting WesternBiophysicsCyclin BCdc2In situ hybridizationCyclin BBiochemistryParacentrotus lividusPolar bodybiology.animalCDC2 Protein KinaseAnimalsProtein IsoformsHSP70 Heat-Shock ProteinsRNA MessengerSea urchinMolecular BiologyHSP70In Situ HybridizationCyclin-dependent kinase 1biologyOvaryCell Biologybiology.organism_classificationMolecular biologyImmunohistochemistryCell biologyOogenesiBiophysicCytoplasmSea Urchinsbiology.proteinOocytesElectrophoresis Polyacrylamide GelFemaleCell DivisionBiochemical and biophysical research communications
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Hsp60 and human aging: Les liaisons dangereuses 

2013

Stressors can cause abnormal intracellular accumulation of Hsp60 and its localization in extramitochondrial sites, secretion, and circulation, with immune system activation. Dysfunction of chaperones associated with their quantitative and qualitative decline with aging (chaperonopathies of aging) characterizes senescence and is a potential causal factor in the physiological deterioration that occurs with it. The role of Hsp60 in aging is not easy to elucidate, because aging is accompanied by pathologies (e.g., cardiovascular and neurodegenerative disorders, osteoporosis, diabetes, cancer, etc.) in which Hsp60 has been implicated but, although those disorders are more frequent in the elderly…

SenescenceAginganimal structuresOsteoporosischemical and pharmacologic phenomenaInflammationDiseaseBiologycomplex mixturesMitochondrial ProteinsPathogenesisImmune systemDiabetes mellitusmedicineHumansCellular SenescenceAutoantibodiesHeart FailurefungiHSP 60 AGING CHAPERONES.Neurodegenerative DiseasesChaperonin 60Atherosclerosismedicine.diseaseMitochondriaImmune SystemImmunologyHSP60Arthropathy Neurogenicmedicine.symptomFrontiers in Bioscience
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Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems

2010

Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging ha…

SenescencebiologyGeneral NeuroscienceGeneral Biochemistry Genetics and Molecular BiologyCell biologyCo-chaperoneImmune systemHistory and Philosophy of ScienceChaperone (protein)biology.proteinProtein foldingHSP60Functional declineReceptorAnnals of the New York Academy of Sciences
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Is chlamydial heat shock protein 60 a risk factor for oncogenesis?

2004

Heat shock protein 60 (HSP60) plays an important role in the protein folding of prokaryotic and eukaryotic cells. Most of the papers published on chlamydial HSP60 concern its role in immune response during infection. In the last decade, exposure to Chlamydia trachomatis has been consistently associated with the development of cervical and ovarian cancer. Moreover, it has been suggested that chlamydial HSP60 may have an anti- apoptotic effect during persistent infection. We hypothesize that the accumulation of exogenous chlamydial HSP60 in the cytoplasm of actively replicating eukaryotic cells may interfere with the regulation of the apoptotic pathway. The concomitant expression of viral onc…

Senescencechlamydia hsp60Genital Neoplasms Femalechemical and pharmacologic phenomenaApoptosisChlamydia trachomatisBiologymedicine.disease_causeCellular and Molecular NeuroscienceImmune systemBacterial ProteinsRisk FactorsHeat shock proteinmedicineHumansNeoplastic transformationMolecular BiologyPharmacologyCell BiologyChaperonin 60Chlamydia InfectionsCell biologyCell Transformation NeoplasticApoptosisImmunologyMolecular MedicineHSP60FemaleCarcinogenesisChlamydia trachomatis
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A comparative analysis of the products of GROEL-1 gene fromChlamydia trachomatisserovar D and the HSP60 var1 transcript fromHomo sapienssuggests a po…

2009

Summary Chlamydia trachomatis serovar D produces large quantities of HSP60-1 during infections, which accumulate inside the host cell inducing autoimmunity. We compare the aminoacid sequences of the human HSP60 with the bacterial counterpart to better elucidate how CTHSP60 may simulate HSP60 from human origin during infection and may induce an autoimmune response. As a result of the comparison we suggest several possible epitopes of the CTHSP60, which may induce autoimmunity.

Serotypeanimal structuresTranscription GeneticMolecular Sequence DataImmunologyAutoimmunityChlamydia trachomatischemical and pharmacologic phenomenaBiologymedicine.disease_causecomplex mixturesEpitopeAutoimmunityGeneticsmedicineHumansAmino Acid SequenceMolecular BiologyGeneGenetics (clinical)GeneticsBase SequencefungiChaperonin 60General MedicineChlamydia InfectionsHsp60 Chlamydia trachomatisGroELHomo sapiensHSP60Chlamydia trachomatisSequence AlignmentInternational Journal of Immunogenetics
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An alternative set of test to bioassay for bioinsecticides

2010

The development of an assay to determine insecticidal properties for either biological and conventional plant protection products plays an important role on the early screening of potential pathogens or derived toxins candidates. The standard methods for the evaluation it has been by bioassay, especially determination of LD50 or LC 50 requiring the use of relatively large numbers of insects and toxin tests. There are several problems connected with these bioassays: availability of insects and in the right life stage, mass producing the candidate species, preparation, reproducibly and costs relative to intensive manpower. These aspects are really important especially when bio-insectides shou…

Settore AGR/11 - Entomologia Generale E ApplicataBacillus thuringiensis Rhynchophorous ferrugineus screening entomopathogens HSP 70 growth inhibition.Settore BIO/05 - Zoologia
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Bacillus thuringiensis treatment alters larval growth, hemocytes and modulation of Hsp70 in Rhynchophorus ferrugineus

2011

To study the pathogen-host relationship, we used the model of the entomopathogenic bacterium Bacillus thuringiensis (Bt) and Rhynchophorus ferrugineus, a quarantine pest that attacks the palm trees. In particular, we focused on the Bt stress-induced infections. We studied the effect of Bt on larval growth, on hemocytes and on the expression of the heat shock proteins (Hsp70). HSPs are rapidly synthesized in the cells after a stress exposition including pathogens. The Hsp70 was evaluated in the supernatant of the hemocyte lysate (HLS) obtained from larvae fed with Bt. This is the first time that the presence of Hsp70 has been recorded in R. ferrugineus. Bt has negative effects on larval grow…

Settore AGR/11 - Entomologia Generale E ApplicataSettore BIO/05 - ZoologiaRed Palm Weevil pests diseases stress response Bacillus thuringiensis Hsp70
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In vivo modulation of Hsp70 in Rhynchophorus ferrugineus hemocytes after Bacillus thuringiensis treatment

2010

Heat shock proteins (Hsps) are rapidly synthesized within stressed cells after exposure to an environmental stressor. A variety of environmental stresses, including heat, cold, trace-metal exposure, xenobiotics have been reported to modulate Hsps expression in various organisms. Hsps are grouped into several families based on their protein size. Most organisms have several genes encoding members of this Hsp family. In particularly Hsp70 can be induced quickly under stressful conditions, but return to a normal expression level under non-stressful conditions. Few studies have been done to detect the Hsp70 expression in phytophagous insects towards pathogens. Since a preliminary research discl…

Settore AGR/11 - Entomologia Generale E ApplicataSettore BIO/05 - ZoologiaRed Palm weevil HSP 70 Stress entomopathogenic bacteria Bt screening
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Ku factor is responsible of Hsp70 basal transcription in mouse mesoangioblasts

2008

Settore BIO/06 - Anatomia Comparata E CitologiaKu factor Hsp70 mesoangioblasts
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