As our group has shown, the NO-synthase inhibitor L-NNA decreased 2-3 times heat shock-induced synthesis of the heat shock protein HSP70 (FEBS Lett. 370 (1995) 159-162). It was suggested that NO is involved in such induction. In the present study, it was found that (1) injection of the NO donor dinitrosyl iron complex (DNIC) into rats results in accumulation of HSP70 in the heart; (2) heat shock is accompanied by increased generation of NO (EPR assay) and HSP70 accumulation in cultured cells; (3) DNIC induces HSP70 accumulation in cultured cells not exposed to heat shock.
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http://dx.doi.org/10.1016/0014-5793(96)00691-6 | DOI Listing |
Aquat Toxicol
January 2025
Nantes Université, Institut des Substances et Organismes de la Mer, ISOMer, UR 2160, Nantes F-44000, France.
Improving the understanding of how chemicals affect on organisms and assessing the associated environmental risks is of major interest in environmental studies. This can be achieved by using complementary approaches based on the study of the molecular responses of organisms. Because of the known chemical pressures on the environment, regulations on the content of some chemicals, such as cadmium, have been mostly completed.
View Article and Find Full Text PDFExp Cell Res
January 2025
School of Clinical and Basic Medical Sciences, Shandong First Medical University, Shandong Academy of Medical Sciences, Jinan, 250117, China; Department of Cardiology, The First Affiliated Hospital of Shandong First Medical University & Shandong Provincial Qianfoshan Hospital, Shandong Medicine and Health Key Laboratory of Cardiac Electrophysiology and Arrhythmia, Jinan, 250014, China; Medical Science and Technology Innovation Center, Shandong First Medical University & Shandong Academy of Medical Sciences, Jinan, 250117, China. Electronic address:
Atherosclerosis (AS) is a chronic disease initiated by vascular endothelial dysfunction, with low shear stress (SS) being a critical inducing factor in this dysfunction. Apoptosis, a form of programmed cell death, is closely associated with AS progression. However, the impact of low SS on endothelial apoptosis and its specific molecular mechanisms remains unclear.
View Article and Find Full Text PDFAdv Rheumatol
January 2025
Department of Ophthalmology, Otolaryngology, Head and Neck Surgery, Ribeirão Preto Medical School, University of São Paulo, São Paulo, Brazil.
Background: Endoplasmic reticulum stress (ERS) and the unfolded protein response (UPR) are adaptive mechanisms for conditions of high protein demand, marked by an accumulation of misfolded proteins in the endoplasmic reticulum (ER). Rheumatic autoimmune diseases (RAD) are known to be associated with chronic inflammation and an ERS state. However, the activation of UPR signaling pathways is not completely understood in Sjögren's disease (SD).
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 PDFGenes (Basel)
November 2024
School of Neurobiology, Biochemistry and Biophysics, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.
The human mitochondrial proteome comprises approximately 1500 proteins, with only 13 being encoded by mitochondrial DNA. The remainder are encoded by the nuclear genome, translated by cytosolic ribosomes, and subsequently imported into and sorted within mitochondria. The process of mitochondria-destined protein import is mediated by several intricate protein complexes distributed among the four mitochondrial compartments.
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