Search results for "chaperon"

The molecular anatomy of human Hsp60 and its effects on Amyloid-β peptide

Heat Shock Protein 60 (HSP60) is ubiquitous and highly conserved, being present in eukaryotes and prokaryotes, including pathogens. This chaperonin is typically considered a mitochondrial protein but it is also found in other intracellular sites, extracellularly and in circulation. HSP60 is an indispensable component of the Chaperoning System and plays a key role in protein quality control, preventing off-pathway folding events and refolding misfolded proteins. This makes HSP60 a putative therapeutic agent for neurodegenerative diseases associated with aggregation of misfolded proteins, for example, Alzheimer’s Disease. We produced and purified recombinant human HSP60 and investigated the e…

Physiactisome: A New Nanovesicle Drug Containing Heat Shock Protein 60 for Treating Muscle Wasting and Cachexia.

2022

Currently, no commercially available drugs have the ability to reverse cachexia or counteract muscle wasting and the loss of lean mass. Here, we report the methodology used to develop Physiactisome—a conditioned medium released by heat shock protein 60 (Hsp60)—overexpressing C2C12 cell lines enriched with small and large extracellular vesicles. We also present evidence supporting its use in the treatment of cachexia. Briefly, we obtain a nanovesicle-based secretion by genetically modifying C2C12 cell lines with an Hsp60-overexpressing plasmid. The secretion is used to treat naïve C2C12 cell lines. Physiactisome activates the expression of PGC-1α isoform 1, which is di…

Expression of 60-kD Heat Shock Protein Increases during Carcinogenesis in the Uterine Exocervix

2002

<i>Objectives:</i> The aim of the present study was to determine the presence and expression of the 60-kD heat shock protein (HSP60) in the dysplasia-carcinoma sequence in the uterine exocervix and to evaluate its diagnostic and prognostic significance. <i>Methods and Results:</i> We performed Western blot and immunohistochemical analyses on biopsies from 40 cases, consisting of 10 normal exocervical biopsies, 10 low-grade squamous intraepithelial lesions (L-SIL), 10 high-grade squamous intraepithelial lesions (H-SIL) and 10 cancerous exocervices (G2 grade). The immunohistochemical results were quantified by computer-assisted image analysis. Western blot analysis sho…

Duchenne Muscular Dystrophy (DMD): Should it be Considered a Systemic Disease?

2016

Duchenne muscular dystrophy (DMD) is an X-linked muscle disease characterized by progressive skeletal muscle loss and development of respiratory failure due to involvement of respiratory muscles. Similar to human DMD, the mdx mouse model lacks dystrophin but is characterized by relatively mild muscle injury, allowing testing the effects of mild endurance exercise training on dystrophic skeletal muscle. We were interested to study the effects of exercise training on airway cells in trained mdx mice by applying the same protocol previously tested in Swiss mice. We found that mdx mice showed little airway inflammation associated with training, but developed increasing apoptosis of airway cells…

Skeletal muscle HSP60 expression is fiber-type specific and increases after endurance training

2013

Heat shock protein (Hsp) 60 is primarily localized inside mitochondrial, plays a key role in the translocation of proteins and cytoprotection, and its levels increase in skeletal muscle upon exercise. The purpose of this study was to examine muscle fiber specificity of HSP60 at rest and after an endurance training program of 6 weeks. Forth-eight young (7-weeks old) healthy mice (BALB/c) were subdivided into sedentary and trained groups. Training was performed over a period of 6 weeks on a rota-rod, at a gradually increasing duration and speed. Eight mice of each group were sacrificed after 15, 30 and 45 days. Two days after the last exercise session all mice were sacrificed by cervical disl…

Heat Shock Protein 60 in Hepatocellular Carcinoma: Insights and Perspectives

2020

Heat shock protein 60 (HSP60) is a mitochondrial chaperone that is implicated in physiological and pathological processes. For instance, it contributes to protein folding and stability, translocation of mitochondrial proteins, and apoptosis. Variations in the expression levels of HSP60 have been correlated to various diseases and cancers, including hepatocellular carcinoma (HCC). Unlike other HSPs which clearly increase in some cancers, data about HSP60 levels in HCC are controversial and difficult to interpret. In the current review, we summarize and simplify the current knowledge about the role of HSP60 in HCC. In addition, we highlight the possibility of its targeting, using chemical com…

THE CHAPERONE SYSTEM IN SALIVARY GLAND DEVELOPMENT

2023

The chaperone system (CS) canonical function is to maintain protein homeostasis. Proper folding of nascent peptides is crucial in developing tissue. The chief components of the CS are 95th National Congress of the Italian Society for Experimental Biology | Trieste, Italy, 12-15 April 2023Non-commercial use only the molecular chaperones, which play key roles in development as indicated by their presence in embryonic tissue as early as at two-cell stage. However, scarce information on the CS in developing tissues is available, especially at advanced stages of embryogenesis and its role is not fully understood. In our previous study, we reported the presence of molecular chaperones in the duct…

Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles.

2004

ABSTRACT Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML −/− ) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted…