Search results for "Hsp27"

showing 10 items of 43 documents

Heat shock proteins as danger signals for cancer detection

2011

First discovered in 1962, heat shock proteins (HSPs) are highly studied with about 35,500 publications on the subject to date. HSPs are highly conserved, function as molecular chaperones for a large panel of “client” proteins and have strong cytoprotective properties. Induced by many different stress signals, they promote cell survival in adverse conditions. Therefore, their roles have been investigated in several conditions and pathologies where HSPs accumulate, such as in cancer. Among the diverse mammalian HSPs, some members share several features that may qualify them as cancer biomarkers. This review focuses mainly on three inducible HSPs: HSP27, HPS70, and HSP90. Our survey of recent …

Cancer Researchendocrine systemdetectionchemical and pharmacologic phenomenaCancer detectionReview ArticleBioinformaticsdanger signallcsh:RC254-28203 medical and health sciencesstress0302 clinical medicineHsp27Heat shock proteinMedicine030304 developmental biologyCancer0303 health sciencesbiologyHeat shock proteinbusiness.industryCancerhemic and immune systemsmedicine.diseaselcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensHsp903. Good healthBiomarker (cell)Oncology030220 oncology & carcinogenesisbiological sciencesbiology.proteinbiomarkerCancer biomarkersbusinessFunction (biology)Frontiers in Oncology
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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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Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity?

2012

Abstract The cytoskeleton is a highly complex network of three major intracellular filaments, microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs). This network plays a key role in the control of cell shape, division, functions and interactions in animal organs and tissues. Dysregulation of the network can contribute to numerous human diseases. Although small HSPs (sHSPs) and in particular HSP27 (HSPB1) or αB-crystallin (HSPB5) display a wide range of cellular properties, they are mostly known for their ability to protect cells under stress conditions. Mutations in some sHSPs have been found to affect their ability to interact with cytoskeleton proteins, leading to IF a…

Epithelial-Mesenchymal TransitionIntermediate FilamentsVimentinmacromolecular substancesMicrofilamentBiochemistry03 medical and health sciences0302 clinical medicineHsp27MicrotubuleStress PhysiologicalHeat shock proteinNeoplasmsAnimalsHumansCytoskeletonIntermediate filament030304 developmental biology0303 health sciencesbiologyGenetic Diseases InbornCell BiologyFibrosisCell biologyHeat-Shock Proteins SmallMutationbiology.proteinDesmin030217 neurology & neurosurgeryThe international journal of biochemistrycell biology
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Cellular responses and HSP70 expression during wound healing in Holothuria tubulosa (Gmelin, 1788).

2014

Wound repair is a key event in the regeneration mechanisms of echinoderms. We studied, at the behavioural, cellular and molecular levels, the wound healing processes in Holothuria tubulosa after injuries to the body wall. The experiments were performed for periods of up to 72 h, and various coelomocyte counts, as well as the expression of heat shock proteins (HS27, HSP70 and HSP90), were recorded. Dermal wound healing was nearly complete within 72 h. In the early stages, we observed the injured animals twisting their bodies to keep their injuries on the surface of the water for the extrusion of the buccal pedicles. At the cellular level, we found time-dependent variations in the circulating…

HolothurianStreImmunoblottingSettore BIO/05 - ZoologiaHSP27 Heat-Shock ProteinsAquatic ScienceAndrologyWestern blotHeat shock proteinmedicineHSPEnvironmental ChemistryAnimalsHolothuriaHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsSettore BIO/06 - Anatomia Comparata E CitologiaCoelomocyteWound Healingmedicine.diagnostic_testbiologyRegeneration (biology)Holothuria tubulosaGeneral Medicinebiology.organism_classificationHsp70Organ SpecificityImmunologyCoelomocyteWound healingHolothuriaFishshellfish immunology
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HSP27 controls GATA-1 protein level during erythroid cell differentiation.

2010

AbstractHeat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific proteins. Here, we show that globin transcription factor 1 (GATA-1) is a client protein of HSP27. In 2 models of erythroid differentiation; that is, in the human erythroleukemia cell line, K562 induced to differentiate into erythroid cells on hemin exposure and CD34+ human cells ex vivo driven to erythroid differentiation in liquid culture, depletion of HSP27 provokes an accumulation of GATA-1 and impairs terminal maturation. More spec…

LeupeptinsPyridines[SDV]Life Sciences [q-bio]Cellular differentiationCellHSP27 Heat-Shock ProteinsAntigens CD34Biochemistryp38 Mitogen-Activated Protein Kinases0302 clinical medicineTransforming Growth Factor betahemic and lymphatic diseasesChlorocebus aethiopsGATA1 Transcription FactorPhosphorylationComputingMilieux_MISCELLANEOUSCells CulturedHeat-Shock Proteins0303 health sciencesbiologyImidazolesCell DifferentiationHematology[SDV] Life Sciences [q-bio]medicine.anatomical_structure030220 oncology & carcinogenesisembryonic structuresCOS CellsRNA InterferenceSignal transductionProteasome InhibitorsProtein BindingProteasome Endopeptidase ComplexImmunologyImmunoblotting03 medical and health sciencesHsp27Erythroid CellsHeat shock proteinmedicineAnimalsHumansTranscription factor030304 developmental biologyCell NucleusInterleukin-6UbiquitinationCell BiologyTransforming growth factor betaMolecular biologyChaperone (protein)biology.proteinK562 CellsHeLa CellsMolecular ChaperonesBlood
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Immunomorphological Pattern of Molecular Chaperones in Normal and Pathological Thyroid Tissues and Circulating Exosomes: Potential Use in Clinics

2019

The thyroid is a major component of the endocrine system and its pathology can cause serious diseases, e.g., papillary carcinoma (PC). However, the carcinogenic mechanisms are poorly understood and clinical useful biomarkers are scarce. Therefore, we determined if there are quantitative patterns of molecular chaperones in the tumor tissue and circulating exosomes that may be useful in diagnosis and provide clues on their participation in carcinogenesis. Hsp27, Hsp60, Hsp70, and Hsp90 were quantified by immunohistochemistry in PC, benign goiter (BG), and normal peritumoral tissue (PT). The same chaperones were assessed in plasma exosomes from PC and BG patients before and after ablative surg…

Male0301 basic medicineGoiterdiagnosismedicine.disease_causelcsh:Chemistry0302 clinical medicinelcsh:QH301-705.5Heat-Shock ProteinsSpectroscopygoiterbiologyThyroidmolecular chaperonesGeneral MedicineMiddle Agedmolecular chaperone3. Good healthComputer Science ApplicationsBlotdiagnosimedicine.anatomical_structure030220 oncology & carcinogenesisheat shock proteins (Hsp)ImmunohistochemistryFemalethyroid gland; papillary carcinoma; molecular chaperones; heat shock proteins (Hsp); goiter; exosomes; diagnosiendocrine systemanimal structuresexosomesArticleCatalysisInorganic Chemistry03 medical and health sciencesHsp27medicineHumansEndocrine systemexosomePhysical and Theoretical ChemistryMolecular Biologythyroid glandbusiness.industryOrganic Chemistrymedicine.diseaseCarcinoma PapillaryMicrovesicles030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Cancer researchbiology.proteinCarcinogenesisbusinesspapillary carcinomaInternational Journal of Molecular Sciences
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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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The expression of HSP27 is associated with poor clinical outcome in intrahepatic cholangiocarcinoma.

2007

Abstract Background The heat shock proteins (HSPs) 27-kDa (HSP27) and 72-kDa (HSP72), are ubiquitous chaperone molecules inducible in cells exposed to different stress conditions. Increased level of HSPs are reported in several human cancers, and found to be associated with the resistance to some anticancer treatments and poor prognosis. However, there is no study of the relationship between HSPs expression and patient's prognosis in intrahepatic cholangiocarcinoma (IHCCA). In this exploratory retrospective study, we investigated the expressions of HSP27 and HSP72 as potential prognostic factors in IHCCA. Methods Thirty-one paraffin-embedded samples were analyzed by immunohistochemical meth…

MaleCancer ResearchHSP27 Heat-Shock ProteinsMitosisHSP72 Heat-Shock ProteinsBile Duct Neoplasmlcsh:RC254-282CholangiocarcinomaImmunoenzyme TechniquesNecrosisLymphocytes Tumor-InfiltratingHsp27Surgical oncologyHeat shock proteinGeneticsBiomarkers TumorMedicineHumansNeoplasm InvasivenessSurvival rateIntrahepatic CholangiocarcinomaHeat-Shock ProteinsAgedCell ProliferationRetrospective Studiesbiologybusiness.industryRetrospective cohort studyMiddle Agedlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensPrognosisNeoplasm ProteinsSurvival RateBile Ducts IntrahepaticOncologyBile Duct NeoplasmsImmunologybiology.proteinCancer researchFemaleStem cellbusinessMolecular ChaperonesResearch ArticleBMC cancer
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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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Upregulation of antibody response to heat shock proteins and tissue antigens in an ocular ischemia model.

2011

PURPOSE. The aim of this study was to characterize the serum antibody reactivities occurring after ocular ischemia reperfusion. The time course of serum antibody responses was examined. METHODS. Wistar rats were exposed to transient ocular ischemia by elevating intraocular pressure to 130 mm Hg for 60 minutes. Axonal damage was evaluated on optic-nerve sections 2 and 4 weeks later. Blood samples collected before and several times after ischemia were used for antibody detection via customized protein microarrays. Different tissue antigens, including heat shock proteins (HSPs) and crystallins, were selected based on previous identification of antibody reactivities in studies on ischemic event…

MalePathologymedicine.medical_specialtyIschemiaHSP27 Heat-Shock ProteinsProtein Array AnalysisVimentinBiologyAutoantigensDownregulation and upregulationAntigenRetinal DiseasesHeat shock proteinGlial Fibrillary Acidic ProteinmedicineAnimalsRats WistarEye ProteinsIntraocular PressureAutoantibodiesGlial fibrillary acidic proteinRetinal VesselsSpectrinMyelin Basic ProteinOptic Nervemedicine.diseaseAxonsRatsUp-RegulationMyelin-Associated GlycoproteinShock (circulatory)Immunoglobulin GReperfusion Injurybiology.proteinMyelin-Oligodendrocyte Glycoproteinmedicine.symptomAntibodyMyelin ProteinsInvestigative ophthalmologyvisual science
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