Search results for " hsp27"

showing 7 items of 7 documents

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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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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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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The Chaperone System in Breast Cancer: Roles and Therapeutic Prospects of the Molecular Chaperones Hsp27, Hsp60, Hsp70, and Hsp90

2022

Breast cancer (BC) is a major public health problem, with key pieces of information needed for developing preventive and curative measures still missing. For example, the participation of the chaperone system (CS) in carcinogenesis and anti-cancer responses is poorly understood, although it can be predicted to be a crucial factor in these mechanisms. The chief components of the CS are the molecular chaperones, and here we discuss four of them, Hsp27, Hsp60, Hsp70, and Hsp90, focusing on their pro-carcinogenic roles in BC and potential for developing anti-BC therapies. These chaperones can be targets of negative chaperonotherapy, namely the elimination/blocking/inhibition of the chaperone(s)…

Settore BIO/16 - Anatomia UmanaCarcinogenesisOrganic ChemistryHSP27 Heat-Shock ProteinsBreast NeoplasmsChaperonin 60General MedicineCatalysisComputer Science ApplicationsInorganic ChemistryHumansbreast cancer chaperone system Hsp inhibitors Hsp27Hsp60Hsp70Hsp90 molecular chaperones immunotherapy negative chaperonotherapyCarcinogenesisFemaleHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologySpectroscopyInternational Journal of Molecular Sciences
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Focusing on a quantification and characterization of extracellular vesicles from blood in brain tumors

Molecular chaperones are required to maintain the proteome in a folded and functional state. Chaperones are structurally and functionally normal but participate in pathways that favor disease, as a tumorigenesis (1). The incidence of brain tumors is increasing rapidly and surgery is the first therapeutic intervention to safeguard the patient's life. The prognosis is poor even after surgical resection, followed by post-operatory chemo- and radio-therapy (2). Tumor-secreted extracellular vesicles (EVs) are critical mediators of intercellular communication between tumor cells and stromal cells in local and distant microenvironments. EVs play an essential role in both primary tumor growth and m…

Settore BIO/16 - Anatomia UmanaHSP60 HSP27 HSP10 exosomes brain tumor biomarkers
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Chaperones in disease: quantitative changes in chronic obstructive pulmonary disease (COPD)

2010

Settore BIO/16 - Anatomia Umanachaperones COPD lung cells epithelium hsp10 hsp60 hsp27 hsp40 hsp70 hsp90 cigarette smoke
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Immunomorphological Patterns of Chaperone System Components in Rare Thyroid Tumors with Promise as Biomarkers for Differential Diagnosis and Providin…

2023

Hurthle cell (HC), anaplastic (AC), and medullary (MC) carcinomas are low frequency thyroid tumors that pose several challenges for physicians and pathologists due to the scarcity of cases, information, and histopathological images, especially in the many areas around the world in which sophisticated molecular and genetic diagnostic facilities are unavailable. It is, therefore, cogent to provide tools for microscopists to achieve accurate diagnosis, such as histopathological images with reliable biomarkers, which can help them to reach a differential diagnosis. We are investigating whether components of the chaperone system (CS), such as the molecular chaperones, can be considered dependabl…

chaperone system.Cancer ResearchOncologySettore BIO/16 - Anatomia Umanathyroid cancermedullary carcinomathyroid cancer; Hurthle cell carcinoma; medullary carcinoma; anaplastic carcinoma; Hsp27; Hsp60; Hsp90; chaperone systemHsp90Hurthle cell carcinomaanaplastic carcinomaHsp27Hsp60Cancers
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