Search results for "chaperon"

showing 10 items of 358 documents

Other Types of Chaperonopathies

2013

A mechanism causing a chaperonopathy that is introduced in this chapter consists of the absence of a chaperone from the place where it is needed (i.e., chaperonopathies by misplacement). Also in this chapter are discussed the unfolded-protein response (UPR), chaperone-mediated autophagy (CMA), and illustrative examples of chaperonopathies by mistake, or collaborationism. In these conditions, one or more chaperones, apparently normal in structure, perform functions that favor disease rather than the contrary, hence the name of chaperonopathy by mistake or collaborationism (a molecule that ought to protect the cell and the organism promotes pathogenesis instead). Many examples of chaperonopat…

biologybusiness.industryAutophagyMistakeDiseasemedicine.diseasemedicine.disease_causeBioinformaticsMyasthenia gravisThyroiditisAutoimmunityPathogenesisChaperone (protein)biology.proteinMedicinebusiness
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Metal specificity of the Ni(II) and Zn(II) binding sites of the N-terminal and G-domain of E. coli HypB

2021

HypB is one of the chaperones required for proper nickel insertion into [NiFe]-hydrogenase. Escherichia coli HypB has two potential Ni(II) and Zn(II) binding sites—the N-terminal one and the so-called GTPase one. The metal-loaded HypB–SlyD metallochaperone complex activates nickel release from the N-terminal HypB site. In this work, we focus on the metal selectivity of the two HypB metal binding sites and show that (i) the N-terminal region binds Zn(II) and Ni(II) ions with higher affinity than the G-domain and (ii) the lower affinity G domain binds Zn(II) more effectively than Ni(II). In addition, the high affinity N-terminal domain, both in water and membrane mimicking SDS solution, has a…

biologychemistry.chemical_elementZincmedicine.disease_causeInorganic ChemistryMetalCrystallographyNickelchemistryG-domainChaperone (protein)visual_artbiology.proteinvisual_art.visual_art_mediummedicineMetallochaperone complexBinding siteEscherichia coliDalton Transactions
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A multipronged approach to unveil the emerging role of Hsp60 in chronic obstructive pulmonary disease

2011

Inflammation is a major component of chronic obstructive pulmonary disease (COPD) and its cause and mechanisms are still incompletely understood. For example, the role of heat shock proteins (Hsps), many of which are molecular chaperones, has not been explored in detail in COPD, despite the fact that these molecules are known to participate in inflammation in other diseases. It has been shown that extracellular Hsps can signal certain types of T cells, macrophages, dendritic cells, and neutrophils and, thereby, elicit inflammation and immunity. However, these phenomena have not been investigated in COPD despite: a) the increasing awareness of Hsp participation in inflammation and immunity; …

bronchial mucosaneutrophilsairwayinflammationheat shock proteinchaperonechemical and pharmacologic phenomenaairways; bronchial mucosa; heat shock proteins; chaperones; inflammation; neutrophils
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Immunopositivity of heat shock protein 60 as a biomarker of bronchial carcinogenesis

2005

business.industryBronchial NeoplasmsBronchiChaperonin 60hsp60medicine.disease_causePulmonary Disease Chronic ObstructiveOncologyCarcinoma Basal CellHeat shock proteinCancer researchmedicineBiomarkers TumorBiomarker (medicine)HumansCarcinogenesisbusiness
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Heat Shock Proteins in Multiple Sclerosis Pathogenesis: Friend or Foe?

2015

Multiple Sclerosis is a complex chronic inflammatory, neurodegenerative disease conditioned by genetic, epigenetic and environmental factors. Main pathological features of MS include areas of focal demyelination of white matter characterized by gliosis, neuron and oligodendrocyte loss. Neurodegenerative as well as immune-mediated processes play a role in the pathogenesis of this disease. One of these immunogenic factors could be represented by the heat shock proteins. HSP exhibit cytoprotective and cytostimulatory effects due to their molecular chaperones role, in many brain model misfolding diseases such as Alzheimer’s and Parkinson’s diseases, whereas still no unambiguous results have bee…

business.industryMultiple sclerosisCentral nervous systemDiseasemedicine.diseasemedicine.disease_causeOligodendrocyteAutoimmunityPathogenesismedicine.anatomical_structureGliosisAutoimmunity Central nervous system Chaperone activity Demyelination Heat shock proteins Multiple sclerosisHeat shock proteinmedicinemedicine.symptomSettore BIO/06 - Anatomia Comparata E CitologiabusinessNeuroscience
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Editorial: Physiology and Pathophysiology of Heat Shock Protein 60

2020

business.industrypost translational modificationshepatocellular carcinomaacquired chaperonopathieBioinformaticsHsp60Biochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryPathophysiologypost translational modificationlcsh:Biology (General)cardiovascular diseasegenetic chaperonopathieHeat shock proteinPosttranslational modificationMedicineHSP60acquired chaperonopathiesbusinessgenetic chaperonopathieslcsh:QH301-705.5Molecular Biologychaperonotherapy
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Hsp56 protein and mRNA distribution in normal and stressed P. lividus embryos

2008

It was previously demonstrated that Paracentrotus lividus Hsp56 mitochondrial chaperonin is con- stitutively expressed during development, that it increases after heat-shock and cadmium treatment, and that it has a specific territorial distribution, both in normal and heat-shocked embryos, as shown by immunolocalization experiments. In this work, we analyzed by Western blot the territorial distribution of the protein in plutei exposed to heat-shock or sublethal cadmium concentrations, and we found that Hsp56 increases in both ectodermal and en- dodermal cells. Moreover, by “in situ” hybridization, we looked at Hsp56 mRNA during normal development and under stress conditions. We found that th…

cadmium chaperonin mitochondria
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Study of the effects of Pleurotuseryngii var. eryngii on heat shock proteins and cytokines levels in a mouse model of colon carcinoma

Medicinal mushrooms are wonderful source of nutraceuticals with a wide range of benefit for human health. The current anti-cancer therapy is not always target specific and often is associated with complications for patients. Therefore new effective and less toxic therapeutic approaches are needed. Heat shock proteins (Hsps) are highly expressed in a variety of cancer types contributing to tumor cell propagation. Here, we treated C26 colon cancer cells with a cold-water extracts of an edible mushrooms Pleurotuseryngii var. eryngii (Pleuery). Hsp90, 70, 60 and 27 levels were measured by western blotting and immunofluorescence analysis. Moreover, we evaluated Pleueryanti cancer effect in an an…

cancer molecular chaperones Heat Shock Proteins
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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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ROLE OF CHAPERONES IN HEALTHY BOWEL AND IBD.

2015

The chaperoning system is the wole complement of chaperones, co-chaperones and chaperone cofactors of the body that preserves cell and tissue homeostasis. Its structural and/or functional defects can cause pathologic conditions, nemed chaperonopathies. Large bowel homeostasis includes a healthy status of the mucosal tissues and the microbiota. An alteration of one of them may determine, in turn, modifications of the other. Molecular chaperones of bacteria and human origin have been implicated in inflammatory bowel disease (IBD). In IBD chaperone levels usually increase and their cellular and subcellular loclization change. This is considered a physiological stress-response of mucosal cells …

chaperones chaperonopathy Intestinal Bowel Diseases IBDSettore MED/12 - GastroenterologiaImmunologyGeneticsSettore BIO/06 - Anatomia Comparata E CitologiaMolecular BiologyBiochemistryBiotechnology
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