Search results for "HSP27"

showing 10 items of 43 documents

Targeting heat shock proteins in cancer

2010

Heat shock proteins (HSPs) HSP27, HSP70 and HSP90 are powerful chaperones. Their expression is induced in response to a wide variety of physiological and environmental insults including anti-cancer chemotherapy, thus allowing the cell to survive to lethal conditions. Different functions of HSPs have been described to account for their cytoprotective function, including their role as molecular chaperones as they play a central role in the correct folding of misfolded proteins, but also their anti-apoptotic properties. HSPs are often overexpressed in cancer cells and this constitutive expression is necessary for cancer cells' survival. HSPs may have oncogene-like functions and likewise mediat…

Protein Foldingendocrine systemCancer ResearchCell SurvivalProtein ConformationCellAntineoplastic AgentsApoptosisBreast NeoplasmsHsp27NeoplasmsHeat shock proteinmedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHeat-Shock ProteinsCell ProliferationbiologyCell growthCancermedicine.diseaseHsp90Hsp70Cell biologymedicine.anatomical_structureOncologyDrug Resistance NeoplasmCancer cellbiology.proteinMolecular ChaperonesCancer Letters
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Hsp27 and Hsp60 in human submandibular salivary gland: Quantitative patterns in healthy and cancerous tissues with potential implications for differe…

2021

Tumors of the submandibular salivary gland (SMG) are uncommon but sufficiently frequent for the physician to consider them in routine examinations and for the pathologist to be prepared to differentiate them from other tissue abnormalities. However, scarcity of specimens makes training difficult, a situation compounded by the lack of accepted universal diagnostic guidelines. Furthermore, there is little information on the chaperone system (CS) of the gland, despite the increasing evidence of its participation in carcinogenesis as a biomarker for diagnosis and patient follow up, and in the mechanisms by which the tumor cells thrive. We are investigating this aspect of various tumors, and her…

Settore BIO/17 - IstologiaMalePathologymedicine.medical_specialtyHistologyCarcinogenesisAdenoid cystic carcinomaSubmandibular GlandHsp27 Hsp60 Pleomorphic adenoma Submandibular salivary glandAdenoid cystic carcinomamedicine.disease_causeDiagnosis DifferentialMitochondrial ProteinsPleomorphic adenomaHsp27Biomarkers TumormedicineHumansHeat-Shock ProteinsSalivary glandbiologySettore BIO/16 - Anatomia Umanabusiness.industryChaperonin 60Cell BiologyGeneral Medicinemedicine.diseaseNeoplasm ProteinsSubmandibular Gland Neoplasmsmedicine.anatomical_structurebiology.proteinBiomarker (medicine)ImmunohistochemistryChaperone systemFemaleDifferential diagnosisbusinessCarcinogenesisMolecular ChaperonesActa Histochemica
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Molecular Approaches to Target Heat Shock Proteins for Cancer Treatment

2015

HSP90 was the first molecular target to inhibit the interaction of this heat shock protein (HSP) with client proteins in cancer cells and tissues. The HSP90 inhibition was attempted to liberate from this chaperone the oncogenic fusion proteins, mutated and activated serine/threonine protein kinases, tyrosine kinases, as well as transcription factors with oncogenic activity, in this manner, the free proteins could be recognized by the proteasome system to be degraded. We should remember here that many HSP family members are overexpressed in different kinds of cancer tissues, these molecules act as chaperones of tumorigenesis. In cancer patients, the first generation of HSP90 inhibitors showe…

Cancer Drug resistance Heat shock proteins HSP27 HSP60 HSP70 HSP90 Molecular targets New anticancer drugs Therapy.
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Hsp27 and Hsp70 in chronic obstructive pulmonary disease: certainties vs doubts

2015

Dear Editor, We read with great interest the work by Cui et al. (2015) in which they measured the levels of Hsp70 and Hsp27 in plasma and lymphocytes obtained from coal workers (CW) affected by chronic obstructive pulmonary disease (COPD) alone or associated with pneumoconiosis (CWP). They found that Hsp70 levels were higher in plasma of COPD subjects affected by CWP compared to COPD subjects without CWP and to controls. There was no difference in Hsp70 levels between COPD without CWP and controls. Hsp70 levels in lymphocytes did not show differences among the three groups. The authors found lower levels of Hsp27 in plasma from patients when comparing controls to both COPD with and without …

MaleHSP27 Heat-Shock ProteinLymphocytemedicine.medical_treatmentPopulationHSP27 Heat-Shock ProteinsBiochemistryPathogenesisPulmonary Disease Chronic ObstructiveOccupational ExposureBiopsymedicineHumansHSP70 Heat-Shock ProteinsLymphocytesAnthracosieducationLetter to the EditorAnthracosisHSP70 Heat-Shock ProteinLamina propriaCOPDeducation.field_of_studyLungmedicine.diagnostic_testbusiness.industryCell Biologymedicine.diseaseCoal Miningrespiratory tract diseasesCoalmedicine.anatomical_structureCytokineImmunologyLymphocytebusinessHumanCell Stress and Chaperones
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Chaperone patterns in vernal keratoconjunctivitis are distinctive of cell and Hsp type and are modified by inflammatory stimuli

2016

Background Vernal keratoconjunctivitis (VKC) is a severe ocular allergy with pathogenic mechanism poorly understood and no efficacious treatment. The aims of the study were to determine quantities and distribution of Hsp chaperones in the conjunctiva of VKC patients and assess their levels in conjunctival epithelial and fibroblast cultures exposed to inflammatory stimuli. Methods Hsp10, Hsp27, Hsp40, Hsp60, Hsp70, Hsp90, Hsp105, and Hsp110 were determined in conjunctiva biopsies from nine patients and nine healthy age-matched normal subjects, using immunomorphology and qPCR. Conjunctival epithelial cells and fibroblasts were cultured and stimulated with IL-1β, histamine, IL-4, TNF-α, or UV-…

Male0301 basic medicinequantitative Hsp patternschemistry.chemical_compoundChaperonesHspchaperoneImmunology and AllergyChildCells CulturedHeat-Shock ProteinsConjunctivitis AllergicCulturedbiologyCD68conjunctival cells Hspconjunctival cellsImmunohistochemistrychaperones; conjunctival cells Hsp; quantitative Hsp patterns; vernal keratoconjunctivitis; Immunology; Immunology and Allergymedicine.anatomical_structureFemaleHistaminequantitative Hsp patternConjunctivaAdolescentCellsImmunologyTryptasevernal keratoconjunctivitiNO03 medical and health sciencesAllergicImmune systemHsp27Heat shock proteinmedicineHumansvernal keratoconjunctivitischaperones; conjunctival cells Hsp; quantitative Hsp patterns; vernal keratoconjunctivitis; Adolescent; Cells Cultured; Child; Conjunctivitis Allergic; Epithelial Cells; Female; Fibroblasts; Heat-Shock Proteins; Humans; Immunohistochemistry; Male; Molecular Chaperones; Immunology and Allergy; ImmunologyEpithelial CellsFibroblastsConjunctivitismedicine.diseaseeye diseases030104 developmental biologychemistryImmunologybiology.proteinChaperones; conjunctival cells Hsp; quantitative Hsp patterns; vernal keratoconjunctivitisVernal keratoconjunctivitisMolecular Chaperones
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Heat shock protein-27 protects human bronchial epithelial cells against oxidative stress-mediated apoptosis: possible implication in asthma.

2002

Inflammation of the human bronchial epithelium, as observed in asthmatics, is characterized by the selective death of the columnar epithelial cells, which desquamate from the basal cells. Tissue repair initiates from basal cells that resist inflammation. Here, we have evaluated the extent of apoptosis as well as the Hsp27 level of expression in epithelial cells from bronchial biopsy samples taken from normal and asthmatic subjects. Hsp27 is a chaperone whose expression protects against oxidative stress. We report that in asthmatic subjects the basal epithelium cells express a high level of Hsp27 but no apoptotic morphology. In contrast, apoptotic columnar cells are devoid of Hsp27 expressio…

Adultendocrine systemanimal structuresHSP27 Heat-Shock ProteinsInflammationApoptosisBronchiColumnar CellRespiratory MucosaBiologymedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicHsp27Heat shock proteinmedicineBronchial BiopsyHumansHeat-Shock ProteinsEpithelial CellsCell BiologyHydrogen PeroxideOriginal ArticlesMiddle AgedOxidantsEpitheliumAsthmaCell biologyNeoplasm ProteinsOxidative Stressmedicine.anatomical_structureApoptosisImmunologybiology.proteinmedicine.symptomOxidative stressMolecular ChaperonesCell stresschaperones
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SFRR-E Young Investigator AwardeeαB-crystallin modulation after acute exercise in skeletal muscle: the role of oxidative stress and fiber composition.

2015

αB-crystallin (CRYAB) is a member of the small heat shock proteins implicated in various biological functions, particularly in skeletal muscle where it is involved in adaptive remodelling processes, activation of gene transcription and stabilization of nascent proteins.In this research we analysed αB-crystallin' response in mouse gastrocnemius at 15' and 30' of recovery from an acute aerobic exercise (1hour), correlating its modulation with oxidative stress level and fiber composition, red (RG) and white gastrocnemius (WG).We found for the first time that the acute exercise lead to a short term, specific increase of phospho-αB-crystallin level (pCRYAB) in the RG, while no changes were obser…

medicine.medical_specialtybiologySkeletal muscleOxidative phosphorylationmedicine.disease_causeBiochemistryHsp70medicine.anatomical_structureEndocrinologyHsp27BiochemistryCrystallinPhysiology (medical)Internal medicinemedicinebiology.proteinPhosphorylationAerobic exerciseOxidative stressFree radical biologymedicine
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Molecular Chaperones and Thyroid Cancer

2021

Thyroid cancers are the most common of the endocrine system malignancies and progress must be made in the areas of differential diagnosis and treatment to improve patient management. Advances in the understanding of carcinogenic mechanisms have occurred in various fronts, including studies of the chaperone system (CS). Components of the CS are found to be quantitatively increased or decreased, and some correlations have been established between the quantitative changes and tumor type, prognosis, and response to treatment. These correlations provide the basis for identifying distinctive patterns useful in differential diagnosis and for planning experiments aiming at elucidating the role of t…

QH301-705.5thyroid tumorsHsp90Reviewmedicine.disease_causeCatalysisChaperoninHsp70Inorganic ChemistryHsp27chaperone systemdifferential diagnosismedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsThyroid NeoplasmsBiology (General)Physical and Theoretical ChemistryHsp27QD1-999Molecular BiologyThyroid cancerSpectroscopychaperonotherapybiologychaperonopathies by mistakeOrganic ChemistryThyroidmolecular chaperonesChaperonin 60General Medicinemedicine.diseaseHsp60Hsp90Computer Science ApplicationsChemistrymedicine.anatomical_structureChaperone (protein)biology.proteinCancer researchHSP60CarcinogenesisInternational Journal of Molecular Sciences
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JNK and AP-1 mediate apoptosis induced by bortezomib in HepG2 cells via FasL/caspase-8 and mitochondria-dependent pathways

2006

The proteasome inhibitor bortezomib is an efficacious apoptotic agent in many tumor cells. This paper shows that bortezomib induced apoptosis in human hepatoma HepG2 cells associated with many modifications in the expression of survival or death factors. Although bortezomib increased the level of the protective factors HSP70 and HSP27, the effects of the drug that favour cell death were predominant. These events include accumulation of c-Jun, phospho-c-Jun and p53; increase in FasL level with activation of caspase-8; changes related to members of Bcl-2 family with increase in the level of pro-apoptotic members and decrease in that of anti-apoptotic ones; dissipation of mitochondrial potenti…

Cancer ResearchProgrammed cell deathFas Ligand ProteinProto-Oncogene Proteins c-junClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentsApoptosisCaspase 8Cell LineBortezomibHsp27Cell Line TumormedicineHumansMitogen-Activated Protein Kinase 8Protease InhibitorsAP1Heat-Shock ProteinsPharmacologyCaspase 8Membrane GlycoproteinsbiologyJNK.Bortezomibc-JunLiver NeoplasmsBiochemistry (medical)c-junhepatomaCell BiologyapoptosiBoronic AcidsMitochondriaCell biologyTranscription Factor AP-1AP-1 transcription factorLiverProto-Oncogene Proteins c-bcl-2ApoptosisCaspasesPyrazinesTumor Necrosis Factorsbiology.proteinCancer researchProteasome inhibitorSignal Transductionmedicine.drugApoptosis
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MDMA Administration and Heat Shock Proteins Response: Foreseeing a Molecular Link

2010

Molecular and cellular mechanisms of MDMA-induced toxicity have been extensively studied in a number of experimental models. Nevertheless, only few studies investigated the involvement of HSPs ("molecular chaperones") in MDMA organs toxicity. In the present minireview we highlight this subject analysing the results of these studies conducted especially on brain tissue. Despite of it seems obvious that HSPs overexpression is a protective reaction against MDMA treatment, the molecular mechanisms for exerting their action are far to be undiscovered. At the same time, we need of comprehensive studies concerning the whole range of Hsps/chaperones expressions in all organs after acute and chronic…

N-Methyl-34-methylenedioxyamphetamineModels NeurologicalBrainPharmaceutical ScienceMDMABrain tissuePharmacologyBiologyHeat shock proteinmental disordersToxicityHallucinogensmedicineAnimalsHumans34-Methylenedioxy-N-methylamphetamine brain toxicity Hsp27 Hsp32 Hsp60 Hsp70.Heat-Shock ProteinsHeat-Shock Responsepsychological phenomena and processesBiotechnologymedicine.drugCurrent Pharmaceutical Biotechnology
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