Background: Heat shock proteins (HSPs) are a family of proteins that are known to play a significant role in the repair of denatured proteins in the cell. It seems that cytoprotective properties of HSPs may help in malignant progression by facilitating tumor cell growth and survival. The purpose of this study is to evaluate HSP27 and HSP70 expression in various histopathological grades of squamous cell carcinoma (SCC).
Materials And Methods: In this retrospective-analytical study, the sections of 51 formalin-fixed paraffin-embedded biopsy specimens of SCC from various sites of oral and paraoral regions and 10 normal oral mucosa were immunostained by Novolink Polymer technique to determine the expression of HSP27 and HSP70. Then the data were analyzed according to the Kruskal-Walis, Mann-Whitney and the Spearman correlation tests (P<0.05).
Results: The expression of HSP27 in well-differentiated SCC was significantly higher than normal epithelium (P=0.007) and in moderately differentiated SCC higher than poorly-differentiated SCC (P=0.023). Inverse correlation was observed between HSP27 expression and SCC's histopathological grade (P=0.001, r=-0.448). There was no significant difference between HSP70 staining of specimens (P=0.38).
Conclusions: The present study revealed that the expression level of HSP27 was inversely related to histopathological grade of SCC and it may provide prognostic value for patients with SCC, but there was no significant relationship between the expression of HSP70 and histopathological grades of SCC.
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http://dx.doi.org/10.4103/1735-3327.95230 | DOI Listing |
Front Mol Neurosci
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Laboratory of Genomic Research, Research Institute for Genetic and Molecular Epidemiology, Kursk State Medical University, Kursk, Russia.
As many proteins prioritize functionality over constancy of structure, a proteome is the shortest stave in the Liebig's barrel of cell sustainability. In this regard, both prokaryotes and eukaryotes possess abundant machinery supporting the quality of the proteome in healthy and stressful conditions. This machinery, namely chaperones, assists in folding, refolding, and the utilization of client proteins.
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December 2024
College of Veterinary Medicine, 70578 Nanjing Agricultural University, Nanjing, 210095, China.
Heat stress impacts male reproduction in animal husbandry. Carnosic acid (CA), a potent antioxidant, mitigates oxidative stress and apoptosis. αB-crystallin, a small heat shock protein, regulates apoptosis and oxidative stress.
View Article and Find Full Text PDFBiochem Pharmacol
December 2024
Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Southwest Medical University, Luzhou 646000, China; Key Laboratory of Medical Electrophysiology, Ministry of Education & Medical Electrophysiological Key Laboratory of Sichuan Province, (Collaborative Innovation Center for Prevention of Cardiovascular Diseases), Institute of Cardiovascular Research, Southwest Medical University, Luzhou 646000, China. Electronic address:
Parkinson's disease (PD) is characterized by the accumulation of misfolded α-synuclein (α-syn). Promoting the degradation of misfolded proteins has been shown to be an effective approach to alleviate PD. This review highlights the roles of specific heat shock proteins (HSPs) in modulating α-syn aggregation and neuronal survival.
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October 2024
Ruminant Nutrition and Anaerobe Laboratory, Department of Animal Science and Technology, Sunchon National University, Suncheon 57922, Korea.
Mol Cell Neurosci
December 2024
Department of Physiology, School of Medicine, Istanbul Medeniyet University, Istanbul, Türkiye; Regenerative and Restorative Medical Research Center (REMER), Research Institute for Health Sciences and Technologies (SABITA), Istanbul Medipol University, Istanbul, Türkiye.
Brain injury develops from a complex series of pathophysiological phases, resulting in acute necrotic or delayed apoptotic cell death after traumatic brain injury (TBI). Inhibition of apoptotic cell death is critical for the treatment of acute neurodegenerative disorders, such as TBI. Here, we investigated the role of phosphodiesterase 10A (PDE10A) in the development of neuronal injury, particularly in apoptotic cell death.
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