Search results for "Shock proteins"

showing 10 items of 347 documents

Role of heat shock proteins in the pathogenesis of myasthenia gravis.

2010

Settore BIO/16 - Anatomia Umanaheat shock proteins myasthenia gravis
researchProduct

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
researchProduct

Chaperonin Hsp60 and Cancer Therapies

2020

The heat shock protein 60 (Hsp60) is a chaperonin belonging to the chaperoning (chaperone) system that typically contributes to protein homeostasis inside mitochondria, but also plays various non-canonical roles unrelated to protein quality control beyond the organelle. Chaperonopathies are disorders in which chaperones play an etiologic-pathogenic role and contribute to the onset/progression of disease. Hsp60 chaperonopathies by mistake are diseases in which the chaperonin is apparently normal (as far as it can be determined with current methodologies) but it actively contributes to pathology, for example in certain types of cancer, and autoimmune and chronic inflammatory disorders. In cer…

Settore BIO/17 - Istologiabiologybusiness.industryfungiDiseaseTumor initiationMitochondrionMicrovesiclesChaperoninAnticancer chaperonotherapy Biomarker Cancer Chaperonin Chaperoning (chaperone) system Chaperonopathies Exosomes Heat shock proteins Hsp60 Immune response Therapy Tumor VaccineChaperone (protein)Heat shock proteinbiology.proteinCancer researchMedicineHSP60business
researchProduct

THE GUT-BRAIN AXIS: EFFECTS OF THE PROBIOTIC LACTOBACILLUS FERMENTUM INTRODUCED IN THE DIET OF ETHANOL-FED MICE

2022

Settore BIO/17 - Istologiagut microbiotaheat shock proteinsLactobacillus fermentumgut-brain axiethanol
researchProduct

Tumor protein 53-induced nuclear protein 1 expression is repressed by miR-155, and its restoration inhibits pancreatic tumor development.

2007

Pancreatic cancer is a disease with an extremely poor prognosis. Tumor protein 53-induced nuclear protein 1 ( TP53INP1 ) is a proapoptotic stress-induced p53 target gene. In this article, we show by immunohistochemical analysis that TP53INP1 expression is dramatically reduced in pancreatic ductal adenocarcinoma (PDAC) and this decrease occurs early during pancreatic cancer development. TP53INP1 reexpression in the pancreatic cancer-derived cell line MiaPaCa2 strongly reduced its capacity to form s.c., i.p., and intrapancreatic tumors in nude mice. This anti-tumoral capacity is, at least in part, due to the induction of caspase 3-mediated apoptosis. In addition, TP53INP1 −/− mouse embryonic…

Settore MED/06 - Oncologia MedicaTransplantation HeterologousGene ExpressionMice NudeMicePancreatic tumorPancreatic cancerCell Line TumormicroRNAGene expressionmedicineAnimalsHumansRNA NeoplasmNuclear proteinCaspaseHeat-Shock ProteinsMice KnockoutMultidisciplinarybiologyBase Sequenceapoptosis pancreatic cancer ponasterone A tumor suppressor micro RNANuclear ProteinsBiological Sciencesmedicine.diseaseTransplantationPancreatic NeoplasmsMicroRNAsCell Transformation NeoplasticApoptosisCancer researchbiology.proteinTumor Suppressor Protein p53Carrier ProteinsNeoplasm TransplantationCarcinoma Pancreatic DuctalProceedings of the National Academy of Sciences of the United States of America
researchProduct

HEAT SHOCK PROTEINS AND ULCERATIVE COLITIS: THE START OF A NEW ERA?

2015

We read with great interest the article written by Abou El Azm and coworkers, published in the last issue of the Arab Journal of Gastroenterology [1]. In this article, the authors investigated the molecular expression of heat shock proteins (HSP) 70 and 90 in relation to the grades of inflammation and dysplasia in patients with ulcerative colitis (UC) before and after treatment. In this study, in agreement with other published studies [2–4], the authors not only found a potential role for HSP 70 and HSP 90 for assessment of the activity and prognosis of UC, but also such markers predicted the presence of dysplasia and differentiated it from reactive atypia [1]. HSP had been found not only a…

Settore MED/12 - GastroenterologiaSettore MED/18 - Chirurgia Generaleheat shock proteinse ulcerative colitis IBD
researchProduct

HSP-MOLECULAR CHAPERONES IN CANCER BIOGENESIS AND TUMOR THERAPY: AN OVERVIEW

2012

Molecular chaperones, many of which are heat-shock proteins (HSPs), are an important class of molecules with various functions. Pathological conditions in which chaperones become etiological and/or pathogenic factors are called chaperonopathies, and are classified into by defect, by excess, and by "mistake". In the latter case, the chaperone is structurally and functionally normal but paqrtecipates in pathwais that favor diseases, aòlthough in some cases the chaperone may have post-translational modifications that may lead it to change its location and function and, thus, to become pathogenic. For example, HSP-chaperones are involved in acrcinogenesis in various ways, so that some forms of …

Settore MED/18 - Chirurgia GeneraleCell Transformation NeoplasticSettore MED/09 - Medicina InternaSettore BIO/16 - Anatomia UmanaNeoplasmsmolecular chaperones chapoeronig system chaperonology chaperonopathy by mistake cancer HSP60 chaperonin chaperonopathy.AnimalsHumansMolecular Targeted TherapyCancer VaccinesHeat-Shock Proteins
researchProduct

Chaperons moleculae in brain tumors-CHAMOBRAT TRIAL: HSP60 and microRNAs related levels in tissue and circulating exosomes in human brain tumors befo…

Current regimen for high-grade gliomas is maximal safe surgical resection followed by external beam radiotherapy with concurrent temozolamide. Maximal tumor resection, however, must be balanced with preservation of the patient’s neurological function. A crucial prognostic factor in oncological neurosurgery is the extent of resection. Several studies have addressed the importance of extent of resection in gliomas surgery. Despite development in the fields of pre operative and intraoperative neuroimaging and neuromonitoring have ameliorated the survival rate and the quality of life for patients affected by high grade gliomas, the clinical outcome of patients with such gliomas remains extremel…

Settore MED/27 - NeurochirurgiaHigh grade glioma (HGG) heat shock proteins (Hsps) miRNA CHAPERONOLOGY ATYPICAL MENINGIOMAS BRAIN TUMOR SURGERY MOLECULAR ANALYSIS
researchProduct

Sequence of the new Drosophila melanogaster small heat-shock-related gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5.

1995

Abstract In this study, we report the molecular cloning of a novel Drosophila melanogaster small heat-shock (HS)-homologous gene, l(2)efl, identified on the right arm of the second chromosome at locus 59F4,5. We describe the temporal expression of l(2)efl in the wild-type and present its structure. The deduced amino-acid sequence of the Efl protein shows significant homology to all known small HS proteins identified in Drosophila and vertebrates, and to mammalian α-crystallin.

Signal peptideTranscription GeneticMolecular Sequence DataRestriction MappingLocus (genetics)Genes InsectMolecular cloningHomology (biology)biology.animalSequence Homology Nucleic AcidGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerRelated geneCloning MolecularGeneHeat-Shock ProteinsIn Situ HybridizationGeneticsbiologyBase SequenceSequence Homology Amino AcidVertebrateGeneral MedicineSequence Analysis DNAbiology.organism_classificationDrosophila melanogasterInsect HormonesGenes LethalDrosophila melanogasterGene
researchProduct

4,5,6,7-Tetrahydro-isoxazolo-[4,5-c]-pyridines as a new class of cytotoxic Hsp90 inhibitors.

2014

Hsp90 is considered an interesting therapeutic target for anticancer drug development. Here we describe a new class of 4,5,6,7-tetrahydro-isoxazolo-[4,5-c]-pyridine compounds. A small library of derivatives has been synthesized and investigated. Some reported compounds show interesting properties combining both notable binding to Hsp90 and potent cell growth inhibitory activity. N-5 substitution with a 2,4 resorcinol carboxamide appears crucial for activity. Moreover, a derivative bearing a hydroxamic acid residue bound to C-3 amide portion was found to inhibit both Hsp90 and HDAC6.

Spectrometry Mass Electrospray IonizationMagnetic Resonance Spectroscopymedicine.drug_classStereochemistryPyridinesCarboxamideApoptosisResorcinolAnti-cancer drugschemistry.chemical_compoundResidue (chemistry)AmideDrug DiscoveryHeat shock protein 90 Anti-cancer drugs 4567-Tetrahydro-isoxazolo-[45-c]- pyridinesmedicineCytotoxic T cellHumansHeat shock protein 90HSP90 Heat-Shock ProteinsPharmacologyHydroxamic acidChemistryCell growthOrganic ChemistryGeneral MedicineNuclear magnetic resonance spectroscopy4 5 6 7-Tetrahydro-isoxazolo-[4 5-c]-pyridinesFlow CytometrySettore CHIM/08 - Chimica Farmaceuticahsp90Settore BIO/14 - Farmacologia4 5 6 7-Tetrahydro-isoxazolo-[4 5-c]-pyridines; Anti-cancer drugs; Heat shock protein 90;K562 CellsCell DivisionEuropean journal of medicinal chemistry
researchProduct