Search results for "Heat Shock Proteins"
showing 10 items of 47 documents
Functional Implications of Multiple IM30 Oligomeric States
2019
The inner membrane-associated protein of 30 kDa (IM30), also known as the vesicle-inducing protein in plastids 1 (Vipp1), is essential for photo-autotrophic growth of cyanobacteria, algae and higher plants. While its exact function still remains largely elusive, it is commonly accepted that IM30 is crucially involved in thylakoid membrane biogenesis, stabilization and/or maintenance. A characteristic feature of IM30 is its intrinsic propensity to form large homo-oligomeric protein complexes. 15 years ago, it has been reported that these supercomplexes have a ring-shaped structure. However, the in vivo significance of these ring structures is not finally resolved yet and the formation of mor…
The Binding Mechanism of Epolactaene to Hsp60 Unveiled by in Silico Modelling
2016
Molecular Dynamics (MD) simulations and DFT/MM calculations were performed in order to rationalize available experimental results and to provide structural details on the binding mechanism of Epolactaene (EPO) to the 60 KDa Heat Shock Protein (Hsp60). The available crystal structure of Hsp60 represents the last step of the chaperone folding cycle, while the Hsp60-EPO complex was obtained by using a homology model of Hsp60, in order to simulate a state related to the beginning of the folding cycle (Rs1). The results of MD simulations point out that EPO shows the highest binding affinity for the empty ATP binding site. The presence of ATP opens a channel that allows the entrance of both EPO d…
Exosomes in cancer theranostic: Diamonds in the rough
2017
IF 3.306; International audience; During the last 10 years, exosomes, which are small vesicles of 50-200 nm diameter of endosomal origin, have aroused a great interest in the scientific and clinical community for their roles in intercellular communication in almost all physiological and pathological processes. Most cells can potentially release these nanovesicles that share with the parent cell a similar lipid bilayer with transmembrane proteins and a panel of enclosed soluble proteins such as heat shock proteins and genetic material, thus acting as potential nanoshuttles of biomarkers. Exosomes surface proteins allow their targeting and capture by recipient cells, while the exosomes' conte…
Exosomal Chaperones and miRNAs in Gliomagenesis: State-of-Art and Theranostics Perspectives
2018
Gliomas have poor prognosis no matter the treatment applied, remaining an unmet clinical need. As background for a substantial change in this situation, this review will focus on the following points: (i) the steady progress in establishing the role of molecular chaperones in carcinogenesis; (ii) the recent advances in the knowledge of miRNAs in regulating gene expression, including genes involved in carcinogenesis and genes encoding chaperones; and (iii) the findings about exosomes and their cargo released by tumor cells. We would like to trigger a discussion about the involvement of exosomal chaperones and miRNAs in gliomagenesis. Chaperones may be either targets for therapy, due to their…
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,…
60KDa chaperonin (HSP60) is over-expressed during colorectal carcinogenesis
2003
The aim of the present study was to evaluate the expression of the heat shock protein 60 (HSP60), a mitochondrial matrix-associated protein belonging to the chaperonin family, in colorectal adenomas and cancers, comparing them to normal colonic tissues and hyperplastic polyps. We performed both immunohistochemistry and Western blot analysis for HSP60. Immunohistochemistry resulted positive in all tubular adenomas and infiltrating adenocarcinomas. By contrast, normal tissues and hyperplastic polyps were negative. Quantitative analysis showed that tubular adenomas with different levels of dysplasia did not present statistical differences concerning HSP60 positivity. In addition, carcinomas al…
Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix
2003
In the present study, we evaluated the presence and the level of expression of HSP10 in two carcinogenetic models: the 'adenoma-carcinoma sequence' of large bowel and the 'dysplasia-carcinoma sequence' of uterine exocervix. We found HSP10 was overexpressed during the carcinogenesis of both organs. In particular, HSP10 was overexpressed early in large bowel carcinogenesis, while the expression of this protein in exocervical carcinogenesis gradually increased from normal through dysplastic to neoplastic tissues. The quantitative analysis of immunohistochemistry and the Western blotting confirmed these results. Our previous observations showed overexpression of HSP60 in the same carcinogenetic…
Immunological aspects of heat shock protein functions and their significance in the development of cancer vaccines
2022
The primary function of intracellular heat shock proteins (HSPs) is to protect the cell by suppressing the effects of various stress factors by either refolding misfolded proteins or blocking apoptosis. After neoplastic transformation, cells overexpress HSPs, which act as factors promoting the neoplastic process by stabilizing proteins responsible for carcinogenesis, however, HSPs can be released into the extracellular environment where they act as important modulators of the immune response. In a tumor microenvironment, extracellular HSPs are able to induce a pro- or anti-neoplastic response, using various mechanisms of affecting immune cells, The study of the role of extracellular HSPs in…
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…
Exosomal Heat Shock Proteins as New Players in Tumour Cell-to-cell Communication
2014
Exosomes have recently been proposed as novel elements in the study of intercellular communication in normal and pathological conditions. The biomolecular composition of exosomes reflects the specialized functions of the original cells. Heat shock proteins (Hsps) are a group of chaperone proteins with diverse biological roles. In recent years, many studies have focused on the extracellular roles played by Hsps that appear to be involved in cancer development and immune system stimulation. Hsps localized on the surface of exosomes, secreted by normal and tumour cells, could be key players in intercellular cross-talk, particularly during the course of different diseases, such as cancer. Exoso…