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Entrapment and Incaprettamento
Published in Burkhard Madea, Asphyxiation, Suffocation,and Neck Pressure Deaths, 2020
Vittorio Fineschi, Matteo Scopetti, Emanuela Turillazzi
Finally, death due to entrapment in small, enclosed spaces is most likely due to oxygen deprivation, but hyperthermia and heat stroke also need to be considered [1,13,14]. Immunohistochemical investigation of markers of heat shock (heat shock proteins HSP90, HSP70 and HSP27) should be performed when circumstantial data suggest a potential causal inference of such mechanisms [20].
Tyrosine Kinase Inhibitors: Targets Other Than FLT3, BCR-ABL, and c-KIT
Published in Gertjan J. L. Kaspers, Bertrand Coiffier, Michael C. Heinrich, Elihu Estey, Innovative Leukemia and Lymphoma Therapy, 2019
Suzanne R. Hayman, Judith E. Karp
Additional Hsps likely to be of future clinical importance as therapeutic targets are the two major antiapoptotic proteins, Hsp70 and Hsp27. Both Hsps are known to exert their antiapoptotic effects at the level of the mitochondria but via different mechanisms, as the stimuli that induce their expressions are not completely redundant (3). Hsp27 appears to inhibit apoptosis through Fas and other receptor-mediated pathways, while Hsp70 primarily appears to inhibit apoptosis by agents that directly or indirectly induce oxidative stress, through either the generation of ROS or the depletion of intracellular antioxidants such as glutathione. Both Hsp70 and Hsp27 have been implicated in multidrug resistance (MDR) and have been associated with chemotherapeutic resistance in leukemia (46–48). Moreover, Hsp70 can inhibit apoptosis induced by both topoisomerase I- and II-directed drugs (49,50).
Mitochondrial Pathologies and Their Neuromuscular Manifestations
Published in Shamim I. Ahmad, Handbook of Mitochondrial Dysfunction, 2019
Carlos Ortez, Andrés Nascimento
HSPB1 and HSPB8 are small Heat Shock Proteins that act as ATP-independent chaperones in protein folding, but are also implicated in architecture of the cytoskeleton. Previous studies have shown that disruption of assembly and aggregation of neurofilaments are the results of HSPB1 mutations in CMT2F146,147 and HSPB8 in CMT2L148. A report showed that the CMT2-causing mutant HSPB1S135F decreased the abundance of acetylated a-tubulin (a guidance cue used by motor proteins to move their cargoes) and impaired mitochondrial anterograde and retrograde movement in cultured dorsal root ganglion sensory neurons isolated from transgenic mice149, suggesting the pathogenic role of alpha-tubulin deacetylation in mutant HSPB1-induced neuropathies. Interestingly, increasing alpha-tubulin acetylation by pharmacological inhibition of histone deacetylase 6 (HDAC6) corrected the axonal transport defects caused by HSPB1 mutations and rescued the CMT phenotype of symptomatic mutant HSPB1 mice, offering perspectives for using HDAC6 inhibitors as a therapeutic strategy for hereditary axonopathies149. Compared to HSPB1, the role of HSPB8 is not as well characterized, but the CMT2-causing K141E mutation in HSPB8 induces similar functional and structural deficiency. Kinesin family member 1B mutation (KIF1B)
Salt-induced phosphoproteomic changes in the subfornical organ in rats with chronic kidney disease
Published in Renal Failure, 2023
Xin Wang, Huizhen Wang, Jiawen Li, Lanying Li, Yifan Wang, Aiqing Li
This study identified 6808 phosphopeptides, corresponding to 2661 phosphoproteins (Supplementary Tables S1-1 and S1-2). Two phosphorylated proteins, GAP43 and Hsp27, among these phosphoproteins, merited additional investigation. Phosphorylated GAP43, with Ser41 as its primary phosphorylation site, is required for neural development and regeneration [24–26]. In this study, phosphorylated GAP43 increased in HC group rather than NC group. The result indicated that salt load was a potent risk factor that deteriorated SFO injury in CKD rats, and SFO made a protective response in return. As a molecular chaperone, Hsp27 repairs misfolded proteins in large oligomers. When phosphorylated at Ser15, Ser78, or Ser82 (corresponding to 86 in rats), it can be converted to the dissociated form [27]. Numerous studies have revealed that phosphorylated Hsp27 protects against cardiovascular and neurological diseases [28–30]. Stetler et al. found that ischemic neuronal injury could be mitigated in mice with sustained activation at Ser15 or Ser82 rather than Ser78 [31], basically consistent with our results. Compared to a normal-salt diet in CKD rats, a high-salt diet significantly enhanced Hsp27 phosphorylation at two sites, Ser15 (1.71-fold) and Ser86 (1.47-fold). Additionally, no phosphorylation of Ser78 was detected. Therefore, these results indicated that SFO strongly reacted to high salt-induced injury.
Multipotent mesenchymal stromal cells are sensitive to thermic stress – potential implications for therapeutic hyperthermia
Published in International Journal of Hyperthermia, 2020
Alexander Rühle, Andreas Thomsen, Rainer Saffrich, Maren Voglstätter, Birgit Bieber, Tanja Sprave, Patrick Wuchter, Peter Vaupel, Peter E. Huber, Anca-Ligia Grosu, Nils H. Nicolay
Expression of the heat shock proteins HSP27, HSP60, HSP70 and the heat shock transcription factor HSF1 have been linked to the ability of cells to deal with thermal stress and were therefore investigated in our study [28,29]. NHDFs exhibited slightly higher expression levels of several heat shock proteins compared to MSCs (Figure 6(C), Supplementary Figure S1). The differences in the expression levels were most prominent between MSC2 and NHDF cells. Especially for HSP60, hyperthermia treatment with 42 °C led to increased protein levels in comparison with untreated controls. MSC1 cells were found to exhibit the highest heat shock protein levels among the different MSC samples. Although MSCs had slightly lower heat shock protein levels than NHDFs, there was still a strong expression of these proteins compared to β-actin levels.
The Effects of Curcumin on Serum Heat Shock Protein 27 Antibody Titers in Patients with Metabolic Syndrome
Published in Journal of Dietary Supplements, 2019
Farzaneh Mohammadi, Maryam Ghazi-Moradi, Majid Ghayour-Mobarhan, Habibollah Esmaeili, Mohsen Moohebati, Maryam Saberi-Karimian, Hamideh Safarian, Shima Tavallaie, Gordon A. Ferns, Amirhosein Sahebkar
Hsps are intracellular proteins, and their upregulation protects cells during stressful conditions (Pourghadamyari et al., 2011). Hsp27 is a member of the small Hsp family. Its functions include protein chaperone activity, regulation of cellular glutathione, apoptosis signaling, and modifying inflammatory response. It is expressed in many cell types, including cardiomyocytes and endothelial cells (Ghayour-Mobarhan, Rahsepar, Tavallaie, Rahsepar, & Ferns, 2009; Tucker, Ustyugov, Bryantsev, Konkel, & Shelden, 2009). According to several past studies, circulating levels of Hsp27 and its corresponding antibody (anti-Hsp27) increase in conditions such as coronary artery disease (Pourghadamyari et al., 2011), acute coronary syndrome (Ghayour‐Mobarhan et al., 2008; Heidari-Bakavoli et al., 2012), and MetS (Sahebkar et al., 2011).