2018
DOI: 10.1007/978-3-319-74715-6_14
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Heat Shock Protein 70 (Hsp70) in the Regulation of Platelet Function

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Cited by 5 publications
(3 citation statements)
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“…This pathway activates a conformational change in the extracellular domains of proteins such as fibrinogen or von Willebrand factor, and fibrinogens act as bridges between platelets to generate platelet aggregation 23 . Additionally, as noted above we also found the up-regulation of Hsp70, a specific chaperone that forms complexes with other co-chaperones in maintaining hemostasis and is associated with intracellular organization of signaling systems and platelet function 24 , and expression of Hsp70 is an endogenous mechanism by which living cells adapt to stress 25 . Moreover, Hsp70 is associated with the inside-out activation of integrin-αIIbβ3 and the activation of platelet aggregation as well as granule secretion and platelet formation under conditions of physiological shear 26 .…”
Section: Discussionsupporting
confidence: 74%
“…This pathway activates a conformational change in the extracellular domains of proteins such as fibrinogen or von Willebrand factor, and fibrinogens act as bridges between platelets to generate platelet aggregation 23 . Additionally, as noted above we also found the up-regulation of Hsp70, a specific chaperone that forms complexes with other co-chaperones in maintaining hemostasis and is associated with intracellular organization of signaling systems and platelet function 24 , and expression of Hsp70 is an endogenous mechanism by which living cells adapt to stress 25 . Moreover, Hsp70 is associated with the inside-out activation of integrin-αIIbβ3 and the activation of platelet aggregation as well as granule secretion and platelet formation under conditions of physiological shear 26 .…”
Section: Discussionsupporting
confidence: 74%
“…More recent findings have indicated that the platelet HSP90/Hsp70 system has been hypothesized to modulate intracellular trafficking and multidrug resistance MDR4/ ABCC4 localization [17]. The HSP members additionally play essential roles in the assembly of actinomyosin filament, an important step in the change of platelet shape and spreading [18]. For instance, HSP27 has been implicated as a downstream p38 MAPK target in the assembly of the cytoskeleton, and phosphorylation of HSP27 is important for the secretion of platelet granules [19].…”
Section: Discussionmentioning
confidence: 99%
“…HSP60 and HSP90, which differ in molecular weight, position, and functions, are up-regulated as an aftermath of heat shock liability in fish, denoting that these may be harnessed as a stress marker (Rigg et al 2018). Still, emodin administration redounded in a drop in HSP60 and HSP90 gene expression compared to control, pointing that supplemented emodin levels of 25 and 50 mg kg -1 could not initiate HSP expression under free stress trials, resulting in M. rosenbergii failing to maintain cellular hemostasis.…”
Section: Figurementioning
confidence: 99%