Response to oxidative stress of peripheral blood mononuclear cells from multiple sclerosis patients and healthy controls

Pistono, Cristiana; Monti, Maria Cristina; Boiocchi, Chiara; Berzolari, Francesca Gigli; Osera, Cecilia; Mallucci, Giulia; Cuccia, Mariaclara; Pascale, Alessia; Montomoli, Cristina; Bergamaschi, Roberto

doi:10.1007/s12192-019-01049-0

Cited by 10 publications

(8 citation statements)

References 57 publications

(63 reference statements)

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“…The main molecular functions of Major Histocompatibility Complex (MHC) include the processing and presentation of protein antigens, the extensive involvement in the induction and regulation of immune responses, which plays a key role in vertebrate adaptation and innate immunity ( Horton et al, 2004 ). Hsp70, encoded by the HSPA1B gene, is located in MHC class III ( Pistono et al, 2020 ). MHC related gene expression was up-regulated in rainbow trout head kidney at high temperature, indicating that Hsp70/110 genes was involved in immune response.…”

Section: Discussionmentioning

confidence: 99%

Genome-wide identification of Hsp70/110 genes in rainbow trout and their regulated expression in response to heat stress

Luo

2020

PeerJ

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Heat shock proteins (Hsps) play an important role in many biological processes. However, as a typical cold water fish, the systematic identification of Hsp70/110 gene family of rainbow trout (Oncorhynchus mykiss) has not been reported, and the role of Hsp70/110 gene in the evolution of rainbow trout has not been described systematically. In this study, bioinformatics methods were used to analyze the Hsp70/110 gene family of rainbow trout. A total of 16 hsp70/110 genes were identified and classified into ten subgroups. The 16 Hsp70/110 genes were all distributed on chromosomes 2, 4, 8 and 13. The molecular weight is ranged from 78.93 to 91.39 kD. Gene structure and motif composition are relatively conserved in each subgroup. According to RNA-seq analysis of rainbow trout liver and head kidney, a total of four out of 16 genes were significantly upregulated in liver under heat stress, and a total of seven out of 16 genes were significantly upregulated in head kidney. RT-qPCR was carried out on these gene, and the result were consistent with those of RNA-seq. The significantly regulated expressions of Hsp70/110 genes under heat stress indicats that Hsp70/110 genes are involved in heat stress response in rainbow trout. This systematic analysis provided valuable information about the diverse roles of Hsp70/110 in the evolution of teleost, which will contribute to the functional characterization of Hsp70/110 genes in further research.

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Section: Discussionmentioning

confidence: 99%

Genome-wide identification of Hsp70/110 genes in rainbow trout and their regulated expression in response to heat stress

Luo

2020

PeerJ

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“…Overexpression of HSP70 suppresses ROS production from mitochondria in human lung microvascular endothelial cells (HLMVEC) exposed to bacterial toxins [ 96 ]. The H SP A1B rs1061581 polymorphism (1267 A/G), which is linked to the risk of developing multiple sclerosis, is related to ROS levels and has a role in the variation in HSP A1B expression levels under oxidative stimulus [ 97 ].…”

Section: Protection Effect and Upregulated Expression Of Hsp70 Under ...mentioning

confidence: 99%

Hsp70 in Redox Homeostasis

Zhang

Gong

et al. 2022

Cells

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Cellular redox homeostasis is precisely balanced by generation and elimination of reactive oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and DNA to damage cells but can also act as signaling molecules to modulate transcription factors and epigenetic pathways that determine cell survival and death. Hsp70 proteins are central hubs for proteostasis and are important factors to ameliorate damage from different kinds of stress including oxidative stress. Hsp70 members often participate in different cellular signaling pathways via their clients and cochaperones. ROS can directly cause oxidative cysteine modifications of Hsp70 members to alter their structure and chaperone activity, resulting in changes in the interactions between Hsp70 and their clients or cochaperones, which can then transfer redox signals to Hsp70-related signaling pathways. On the other hand, ROS also activate some redox-related signaling pathways to indirectly modulate Hsp70 activity and expression. Post-translational modifications including phosphorylation together with elevated Hsp70 expression can expand the capacity of Hsp70 to deal with ROS-damaged proteins and support antioxidant enzymes. Knowledge about the response and role of Hsp70 in redox homeostasis will facilitate our understanding of the cellular knock-on effects of inhibitors targeting Hsp70 and the mechanisms of redox-related diseases and aging.

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“…Data also showed a redox imbalance in the plasma that occurs concomitantly with increased levels of extracellular HSP70 (eHSP70). Another important link between HSP and OS is that the HSP70-2 polymorphism is related to ROS levels and appears to have a role in the different expressions of HSP70-2 (a sensor for the redox status of the cells) under oxidative stimulus [ 46 ]. HSP and OS interaction can even be related to a pineal hormone—melatonin—which is considered a potent candidate in the regulation of oxidative damage [ 47 ].…”

Section: Heat Shock Proteins and Oxidative Stressmentioning

confidence: 99%

Heat Shock Proteins in Oxidative Stress and Ischemia/Reperfusion Injury and Benefits from Physical Exercises: A Review to the Current Knowledge

Szyller

Bil‐Lula

2021

Oxidative Medicine and Cellular Longevity

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Heat shock proteins (HSPs) are molecular chaperones produced in response to oxidative stress (OS). These proteins are involved in the folding of newly synthesized proteins and refolding of damaged or misfolded proteins. Recent studies have been focused on the regulatory role of HSPs in OS and ischemia/reperfusion injury (I/R) where reactive oxygen species (ROS) play a major role. ROS perform many functions, including cell signaling. Unfortunately, they are also the cause of pathological processes leading to various diseases. Biological pathways such as p38 MAPK, HSP70 and Akt/GSK-3β/eNOS, HSP70, JAK2/STAT3 or PI3K/Akt/HSP70, and HSF1/Nrf2-Keap1 are considered in the relationship between HSP and OS. New pathophysiological mechanisms involving ROS are being discovered and described the protein network of HSP interactions. Understanding of the mechanisms involved, e.g., in I/R, is important to the development of treatment methods. HSPs are multifunctional proteins because they closely interact with the antioxidant and the nitric oxide generation systems, such as HSP70/HSP90/NOS. A deficiency or excess of antioxidants modulates the activation of HSF and subsequent HSP biosynthesis. It is well known that HSPs are involved in the regulation of several redox processes and play an important role in protein-protein interactions. The latest research focuses on determining the role of HSPs in OS, their antioxidant activity, and the possibility of using HSPs in the treatment of I/R consequences. Physical exercises are important in patients with cardiovascular diseases, as they affect the expression of HSPs and the development of OS.

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Response to oxidative stress of peripheral blood mononuclear cells from multiple sclerosis patients and healthy controls

Cited by 10 publications

References 57 publications

Genome-wide identification of Hsp70/110 genes in rainbow trout and their regulated expression in response to heat stress

Genome-wide identification of Hsp70/110 genes in rainbow trout and their regulated expression in response to heat stress

Hsp70 in Redox Homeostasis

Heat Shock Proteins in Oxidative Stress and Ischemia/Reperfusion Injury and Benefits from Physical Exercises: A Review to the Current Knowledge

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