Heat shock proteins play important housekeeping roles in a variety of cells within the body during normal control conditions. The many different functions for heat shock proteins in the cell depend upon the specific heat shock protein involved. Each protein is nominally differentiated based upon its molecular size. However, in addition to their role in normal cell function, heat shock proteins may play an even more important role as pro-survival proteins conserved through evolution to protect the cell from a variety of stresses. The ability of a cell to withstand these environmental stresses is critical to its capacity to adapt and remain viable. Loss of this ability may lead to pathological states. Abnormal localization, structure or function of the heat shock proteins has been associated with many pathologies, including those involving heart disease. Heat shock proteins like HSP60 and HSP70 in particular have been identified as playing important roles in inflammation and immune reactions. Inflammation has been identified recently as an important pathological risk factor for heart disease. It is perhaps not surprising therefore, that heat shock protein family has been increasingly identified as an important intracellular pathway associated with inflammatory-mediated heart conditions including atherosclerosis. This paper reviews the evidence in support of a role for heat shock proteins in cardiovascular disease and the potential to target these proteins to alter the progression of atherosclerotic disease.
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http://dx.doi.org/10.2174/1389450116666150416115423 | DOI Listing |
Microb Cell Fact
January 2025
College of Architecture and Environment, Sichuan University, Chengdu, 610065, Sichuan, China.
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View Article and Find Full Text PDFBiomed Pharmacother
January 2025
Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo n. 2, Prague 16610, Czech Republic; Department of Genetics and Microbiology, Charles University and Research Center BIOCEV, Prumyslova 595, Vestec 25250, Czech Republic. Electronic address:
Intracellular protein aggregation causes proteotoxic stress, underlying highly debilitating neurodegenerative disorders in parallel with decreased proteasome activity. Nevertheless, under such stress conditions, the expression of proteasome subunits is upregulated by Nuclear Factor Erythroid 2-related factor 1 (NRF1), a transcription factor that is encoded by NFE2L1. Activating the NRF1 pathway could accordingly delay the onset of neurodegenerative and other disorders with impaired cell proteostasis.
View Article and Find Full Text PDFCell Death Dis
January 2025
Faculty of Science and Medicine, Department of Oncology, Microbiology and Immunology, Anatomy unit, University of Fribourg, CH-1700, Fribourg, Switzerland.
Cell death mediated by executioner caspases is essential during organ development and for organismal homeostasis. The mechanistic role of activated executioner caspases in antibacterial defense during infections with intracellular bacteria, such as Listeria monocytogenes, remains elusive. Cell death upon intracellular bacterial infections is considered altruistic to deprive the pathogens of their protective niche.
View Article and Find Full Text PDFFront Med (Lausanne)
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Department of Medicine, Firestone Institute for Respiratory Health, McMaster University, Hamilton, ON, Canada.
Background: Sarcoidosis is a systemic granulomatous disease of unknown cause. Natural improvement with favorable outcome is common, but a significant number of patients present with difficult to manage and progressive disease. The identification of biomarkers associated with disease activity and progression is warranted.
View Article and Find Full Text PDFPlant Commun
January 2025
College of Life Sciences, Basic Forestry and Proteomics Research Center, Fujian Agriculture and Forestry University, Fuzhou 350002, China. Electronic address:
High-temperature stress, also referred to as heat stress, often has detrimental effects on plant growth and development. Phytochromes have been implicated in regulating plant heat stress responses, but the role of blue-light receptors, such as cryptochromes, in plant blue light-dependent heat stress response has remained unclear. We found that the blue light receptor cryptochrome 1 (CRY1) negatively regulates heat stress tolerance (thermotolerance) in Arabidopsis.
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