Search results for " HSP70."
showing 10 items of 38 documents
Membrane-anchored heat-shock protein 70 (Hsp70) in cancer.
2020
International audience; Hsp70 is a highly conserved and inducible heat shock protein that belongs to the HSP70 family of molecular chaperones and plays a central role in protein homeostasis. The main function of Hsp70 is to protect cells from physiological, pathological and environmental insults, as it assists an ATP-dependent manner the process of protein folding. Since Hsp70 provides critical cell survival functions, cancer cells are assumed to rely on this chaperone. Strong evidence suggests that Hsp70 is upregulated in different type of cancers and is involved in tumor growth, invasion, migration and resistance to anti-cancer therapy. Interestingly, this Hsp70 upregulation induces Hsp70…
Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting
2018
Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including the nature of protein misfolding, which results in the production of toxic species. Considering the involvement of (mis)folding processes in AD aetiology, targeting molecular chaperones represents a promising therapeutic perspective. This review analyses the connection between AD and molecular chaperones, with particular attention toward the most important heat shock proteins (HSPs) as representative components of the human chaperome: Hsp60,…
Different immunohistochemical levels of Hsp60 and Hsp70 in a subset of brain tumors and putative role of Hsp60 in neuroepithelial tumorigenesis
2013
In this work we analysed, by immunohistochemistry, a series of brain tumors to detect the levels and cellular distribution of Hsp60 and Hsp70. We found that Hsp60 levels were significantly higher than those of Hsp70 in neuroepithelial tumors, while levels of both molecules were not significantly different from each other in meningeal neoplasms. In particular, Hsp60 immunopositivity was present mainly at the cytoplasmic level, while Hsp70 immunopositivity was found both in the cytoplasm and in the nucleus of tumor cells. The levels of these molecules in healthy control cells were always very low. Finally, Hsp60 and Hsp70 levels did not correlate with the different types (WHO grade) of neopla…
Role of Hsp70 in Multiple Sclerosis: An Overview
2019
For many years heat shock protein 70 (Hsp70) was considered exclusively an intracellular chaperone contributing to protein proteostasis and in apoptotic pathway block. Lately it has been demonstrated that Hsp70 is actively released in the extracellular environment, thereby promoting the activation of the immune system by stimulating innate and adaptive responses through the activation of APCs. Its expression in the nervous system is induced in a variety of pathological conditions. Emerging evidences displayed that Hsp70 is a critical regulator in normal neural cells. Multiple sclerosis (MS) is an autoimmune disease of the central nervous system (CNS) directed against myelin antigens. In thi…
Oligodendroglioma cells shed microvesicles which contain TRAIL as well as molecular chaperones and induce cell death in astrocytes.
2011
Microvesicles (MVs) shed from G26/24 oligodendroglioma cells were previously reported to cause a reproducible, dose-dependent, inhibitory effect on neurite outgrowth, and eventually neuronal apoptosis, when added to primary cultures of rat cortical neurons. These effects were reduced but not abolished by functional monoclonal antibodies against Fas-L. In order to investigate whether MVs contain other factors able to induce cell death, we tested them for TRAIL and found clear evidence of its presence in the vesicles. This finding suggests the possibility that Fas-L and TRAIL cooperate in inducing brain cell death. Aimed at understanding the route through which the vesicles deliver their mess…
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…
A constitutive 70 kDa heat-shock protein is localized on the fibres of spindles and asters at metaphase in an ATP-dependent manner: A new chaperone r…
2001
In the present study, double immunofluorescence and immunoblot analysis have been used to show that centrosomes, isolated from Paracentrotus lividus sea urchin embryos at the first mitotic metaphase, contain the constitutive chaperone, heat-shock protein (HSP) 70. More specifically, we demonstrate that centrosomes contain only the HSP70-d isoform, which is one of the four isoforms identified in P. lividus . We also provide evidence that p34(cell division control kinase-2) and t complex polypeptide-1 (TCP-1) α, a subunit of the TCP-1 complex, are localized on the centrosomes. Furthermore, inhibition of TCP-1 in vivo, via microinjecting an anti-(TCP-1α) antibody into P. lividus eggs before fe…
Curcumin entrapped into lipid nanosystems inhibits neuroblastoma cancer cell growth and activates Hsp70 protein
2010
Curcumin is a natural anti-cancer compound utilized on a wide variety of human cancer cell lines and animal carcinogenesis models. However, its clinical application has been limited for its minimal systemic bioavailability. Nanoparticle-based drug delivery approaches have the potential for rendering hydrophobic molecules such as curcumin dispersible in aqueous media, thus overtaking the limits of its poor solubility. In this paper, we reported the preparation and chemical-physical characterization of Nanostructured Lipid Carriers (NLC) containing curcumin, based on Imwitor, Compritol or Precirol as lipid matrix. By in vitro experiments, we have demonstrated that these nano-systems are able …
In-Gel Assay to Evaluate Antioxidant Enzyme Response to Silver Nitrate and Silver Nanoparticles in Marine Bivalve Tissues
2022
Silver is back in vogue today as this metal is used in the form of nanomaterials in numerous commercial products. We have developed in-gel electrophoretic techniques to measure the activity of the antioxidant enzymes catalase (CAT), superoxide dismutase (SOD), and glutathione peroxidase (GPX), and used the same techniques in combination with HSP70 Western blot analysis to evaluate the effects of nanomolar amounts of silver nitrate and 5 nm alkane-coated silver nanoparticles in tissues of the marine bivalve Mytilus galloprovincialis (Lam.) exposed for 28 days in mesocosms. Our results showed a negligible effect for nanosilver exposure and dose-dependent effects for the nitrate form.
Diagnosis of sublethal stress in the marine sponge Geodia cydonium: application of the 70 kDa heat-shock protein and a novel biomarker, the Rab GDP d…
1997
Abstract Sponges (Porifera) are among the major phyla inhabiting the marine hard-substrate benthos, both in respect to the number of species and their biomass. Hence reliable biomarkers need to be developed to monitor the environmental load in those animals. Recently, the cDNA for the heat shock protein HSP70 has been isolated from the sponge Geodia cydonium and found to be a reliable indicator for temperature stress. In the present study, we have isolated the Rab GDP-dissociation inhibitor (GDI), which has previously been shown to be a key element in the intracellular traffic system. The 1521 bp long cDNA, encoding sponge GDI, has been isolated and analyzed. The deduced aa sequence ( M r =…