The effects of carbon tetrachloride (CCl(4)) treatment on acute liver damage in knock out (heat shock proteins -- HSP70-/-) mice and wild-type (C57BL/6) mice were examined. Acute liver injury was induced by a single intraperitoneal injection of 0.3 ML/kg CCl(4) in olive oil. Mice were sacrificed at 12, 24, 48 and 72 h after treatment. To assess hepatotoxicity, alanine transaminase, neutrophil infiltration and degree of necrosis were measured. Western blot analysis was employed for heat shock proteins. The result revealed that HSP70-/- mice showed higher alanine transaminase levels and a more severe degree of neutrophilic infiltration and necrosis than those of wild-type mice. Furthermore, HSP70-/- mice recovered more slowly from CCl(4) treatment. In HSP70-/- mice, HSP47 was overexpressed. Therefore, HSP70-/- mice could be an adequate model of acute liver toxicity study.
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http://dx.doi.org/10.1016/j.etp.2007.02.005 | DOI Listing |
Nutrients
December 2024
Institute for Health and Sport, Victoria University, Melbourne, VIC 3030, Australia.
Background: Obesity is a risk factor for developing cardiovascular diseases (CVDs) by impairing normal vascular function. Natural products are gaining momentum in the clinical setting due to their high efficacy and low toxicity. extract (CFE) has been shown to control appetite and promote weight loss; however, its effect on vascular function remains poorly understood.
View Article and Find Full Text PDFBiomedicines
December 2024
St. Petersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre «Kurchatov Institute», Orlova roshcha 1, Gatchina 188300, Russia.
Stress protein HSP70 administered exogenously has demonstrated high potential as an efficient adjuvant in antitumor immune response. To enhance the antigen-presenting activity, bioavailability, and stability of exogenous recombinant human HSP70, we propose incorporating it into plant extracellular vesicles. Earlier, we found that grapefruit-derived extracellular vesicles (GEV) were able to store the protein with no loss of its major function, chaperone activity.
View Article and Find Full Text PDFInt J Biol Sci
January 2025
Department of Otolaryngology Head and Neck Surgery/Deep Underground Space Medical Center, West China Hospital, Sichuan University, Chengdu, China.
Heat acclimation (HA) is an evolutionarily conserved trait that enhances tolerance to novel stressors by inducing heat shock proteins (HSPs). However, the molecular mechanisms underlying this phenomenon remain elusive. In this study, we established a HA mouse model through intermittent heat stimulation.
View Article and Find Full Text PDFInt J Prev Med
November 2024
Department of Anatomical Sciences, School of Medicine, Isfahan University of Medical Sciences, Isfahan, Iran.
Nat Commun
December 2024
Department of Biochemistry, McGill University, Montreal, QC, Canada.
Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted protein folding. However, this is challenging in neuronal projections because of their polarized morphology and constant synaptic proteome remodeling. Using high-resolution fluorescence microscopy, we discover that hippocampal and spinal cord motor neurons of mouse and human origin localize a subset of chaperone mRNAs to their dendrites and use microtubule-based transport to increase this asymmetric localization following proteotoxic stress.
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