The induction of heat shock (stress) proteins (HSP) is a response by cells due to a variety of physical, chemical, and infectious agents. They have a significant role as cytoprotectants, in the regulation of cellular functions, and in the recovery after sublethal injury. Using antibody to mammalian HSP 72/73, we have performed as immunohistological study of human renal tissue in normal and diseased states, including idiopathic nephrotic syndrome, proliferative and crescentic glomerulonephritis, and interstitial nephritis. A significant increase of HSP expression was noted in certain segments of the tubule in acute interstitial nephritis and in glomerulonephritis accompanied by active interstitial inflammation. A possible role by the inflammatory mediators in the induction of HSP in those cases is suggested.
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http://dx.doi.org/10.1159/000189108 | DOI Listing |
Adv Sci (Weinh)
January 2025
School of Laboratory Medicine and Biotechnology, Southern Medical University, Guangzhou, 510515, China.
Despite substantial advances in the antitumor effects of annonaceous acetogenins (ACGs), the absence of a defined biological action mechanism remains a major barrier to their clinical application. Here, it is found that squamocin effectively depletes both EZH2 and MYC in multiple cancer cell lines, including head and neck squamous cell carcinoma, and gastric and colorectal cancer, demonstrating potent efficacy in suppressing these in vivo tumor models. Through the combination of surface plasmon resonance (SPR), differential scanning fluorimetry (DSF), and cellular thermal shift assay (CETSA), heat shock protein 90α (HSP90α) is identified as the direct binding target of squamocin.
View Article and Find Full Text PDFWound Repair Regen
January 2025
Department of Burn, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Bacterial colonisation in hypertrophic scars (HSs) has been reported, yet the precise mechanism of their contribution to scar formation remains elusive. To address this, we examined HS and normal skin (NS) tissues through Gram staining and immunofluorescence. We co-cultured fibroblasts with heat-inactivated Staphylococcus aureus (S.
View Article and Find Full Text PDFIUCrJ
March 2025
Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, People's Republic of China.
Heat-shock protein 90 (HSP90) is a highly active molecular chaperone that plays a crucial role in cellular function. It facilitates the folding, assembly and stability of various oncogenic proteins, particularly kinases and transcription factors involved in regulating tumor growth and maintenance signaling pathways. Consequently, HSP90 inhibitors are being explored as drugs for cancer therapy.
View Article and Find Full Text PDFCrit Rev Oncog
January 2025
Department of Biotechnology, Dr. B.R. Ambedkar University, Srikakulam 532410, Andhra Pradesh, India.
The heat shock protein 90 kDa (HSP90) is highly conserved across diverse species, including humans, and upregulated in various cancers. As a result, it has been identified as a promising target for advancing anticancer medicine. The introduction of combinatorial chemistry in drug discovery has emphasized the need to develop new technologies in screening, designing, decoding, synthesizing, and screening combinatorial drug libraries.
View Article and Find Full Text PDFJ Exp Zool A Ecol Integr Physiol
January 2025
Department of Biology, Widener University, Chester, Pennsylvania, USA.
Cold-water fishes, such as Brook trout (Salvelinus fontinalis), are being challenged by the consequences of climate change. The ability of these fish to acclimate to warmer environmental conditions is vital to their survival. Acclimation to warmer water may allow brook trout to reduce the metabolic costs of higher temperatures.
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