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Protein Quality Control and Integrated Stress Response Related to Pain...
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Protein Quality Control and Integrated Stress Response Related to Pain Disorders

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 September 2020) | Viewed by 9482

Special Issue Editor

Prof. Dr. Tomohiko Aoe

E-Mail Website
Guest Editor
Pain Center, Teikyo University Chiba Medical Center, Teikyo University, 3426-3 Anesaki, Ichihara City 299-0111, Chiba, Japan
Interests: cell biology; ER (endoplasmic reticulum) stress; chaperone; neuroscience; opioid; neurodegeneration; anesthetic action; chronic Pain
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein quality control ensures the intracellular transport of properly folded proteins to proper locations in the cell. Disturbance of this process leads to integrated stress response including the unfolded protein response in the endoplasmic reticulum and the heat shock response in the cytosol. Integrated stress response compensates against the accumulation of misfolded proteins due to extracellular insults such as oxidative stress and toxic substances as well as intrinsic conditions such as aging, malnutrition, and gene modifications. Integrated stress response involves intracellular signaling and various cellular interactions, often associated with pathogenic conditions.

Acute and chronic pain cause changes in the intracellular signal transduction system and affect cell–cell interactions. These changes may be correlated with protein quality control and stress response. This Special Issue focuses on protein quality control and integrated stress response related to acute and chronic pain disorders. Topics may include the pathophysiology of neuropathic pain, the neurotoxicity of general anesthesia, opioid tolerance, opioid misuse, pain disorders with neurodegenerative diseases, etc. We welcome the submission of review articles and original studies regarding basic cellular experiments, animal models, and human diseases.

Prof. Dr. Tomohiko Aoe
Guest Editor

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Keywords

  • proteostasis
  • ER stress
  • UPR
  • heat shock response
  • HSP
  • chaperone
  • protein aggregation
  • analgesia
  • anesthesia
  • opioid

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Published Papers (3 papers)

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Research

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15 pages, 2210 KiB  
Article
Pharmacological Chaperones Attenuate the Development of Opioid Tolerance
by Youta Okuyama, Hisayo Jin, Hiroshi Kokubun and Tomohiko Aoe
Int. J. Mol. Sci. 2020, 21(20), 7536; https://doi.org/10.3390/ijms21207536 - 13 Oct 2020
Cited by 6 | Viewed by 2696
Abstract
Opioids are potent analgesics widely used to control acute and chronic pain, but long-term use induces tolerance that reduces their effectiveness. Opioids such as morphine bind to mu opioid receptors (MORs), and several downstream signaling pathways are capable of inducing tolerance. We previously [...] Read more.
Opioids are potent analgesics widely used to control acute and chronic pain, but long-term use induces tolerance that reduces their effectiveness. Opioids such as morphine bind to mu opioid receptors (MORs), and several downstream signaling pathways are capable of inducing tolerance. We previously reported that signaling from the endoplasmic reticulum (ER) contributed to the development of morphine tolerance. Accumulation of misfolded proteins in the ER induced the unfolded protein response (UPR) that causes diverse pathological conditions. We examined the effects of pharmacological chaperones that alleviate ER stress on opioid tolerance development by assessing thermal nociception in mice. Pharmacological chaperones such as tauroursodeoxycholic acid and 4-phenylbutyrate suppressed the development of morphine tolerance and restored analgesia. Chaperones alone did not cause analgesia. Although morphine administration induced analgesia when glycogen synthase kinase 3β (GSK3β) was in an inactive state due to serine 9 phosphorylation, repeated morphine administration suppressed this phosphorylation event. Co-administration of chaperones maintained the inactive state of GSK3β. These results suggest that ER stress may facilitate morphine tolerance due to intracellular crosstalk between the UPR and MOR signaling. Pharmacological chaperones may be useful in the management of opioid misuse. Full article
(This article belongs to the Special Issue Protein Quality Control and Integrated Stress Response Related to Pain Disorders)
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Review

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19 pages, 1583 KiB  
Review
Unraveling the Connection: Pain and Endoplasmic Reticulum Stress
by Ryoko Kawanaka, Hisayo Jin and Tomohiko Aoe
Int. J. Mol. Sci. 2024, 25(9), 4995; https://doi.org/10.3390/ijms25094995 - 3 May 2024
Cited by 3 | Viewed by 1584
Abstract
Pain is a complex and multifaceted experience. Recent research has increasingly focused on the role of endoplasmic reticulum (ER) stress in the induction and modulation of pain. The ER is an essential organelle for cells and plays a key role in protein folding [...] Read more.
Pain is a complex and multifaceted experience. Recent research has increasingly focused on the role of endoplasmic reticulum (ER) stress in the induction and modulation of pain. The ER is an essential organelle for cells and plays a key role in protein folding and calcium dynamics. Various pathological conditions, such as ischemia, hypoxia, toxic substances, and increased protein production, may disturb protein folding, causing an increase in misfolding proteins in the ER. Such an overload of the folding process leads to ER stress and causes the unfolded protein response (UPR), which increases folding capacity in the ER. Uncompensated ER stress impairs intracellular signaling and cell function, resulting in various diseases, such as diabetes and degenerative neurological diseases. ER stress may be a critical universal mechanism underlying human diseases. Pain sensations involve the central as well as peripheral nervous systems. Several preclinical studies indicate that ER stress in the nervous system is enhanced in various painful states, especially in neuropathic pain conditions. The purpose of this narrative review is to uncover the intricate relationship between ER stress and pain, exploring molecular pathways, implications for various pain conditions, and potential therapeutic strategies. Full article
(This article belongs to the Special Issue Protein Quality Control and Integrated Stress Response Related to Pain Disorders)
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17 pages, 2310 KiB  
Review
TRPV1 Channel: A Noxious Signal Transducer That Affects Mitochondrial Function
by Rebeca Juárez-Contreras, Karina Angélica Méndez-Reséndiz, Tamara Rosenbaum, Ricardo González-Ramírez and Sara Luz Morales-Lázaro
Int. J. Mol. Sci. 2020, 21(23), 8882; https://doi.org/10.3390/ijms21238882 - 24 Nov 2020
Cited by 25 | Viewed by 4597
Abstract
The Transient Receptor Vanilloid 1 (TRPV1) or capsaicin receptor is a nonselective cation channel, which is abundantly expressed in nociceptors. This channel is an important transducer of several noxious stimuli, having a pivotal role in pain development. Several TRPV1 studies have focused on [...] Read more.
The Transient Receptor Vanilloid 1 (TRPV1) or capsaicin receptor is a nonselective cation channel, which is abundantly expressed in nociceptors. This channel is an important transducer of several noxious stimuli, having a pivotal role in pain development. Several TRPV1 studies have focused on understanding its structure and function, as well as on the identification of compounds that regulate its activity. The intracellular roles of these channels have also been explored, highlighting TRPV1′s actions in the homeostasis of Ca2+ in organelles such as the mitochondria. These studies have evidenced how the activation of TRPV1 affects mitochondrial functions and how this organelle can regulate TRPV1-mediated nociception. The close relationship between this channel and mitochondria has been determined in neuronal and non-neuronal cells, demonstrating that TRPV1 activation strongly impacts on cell physiology. This review focuses on describing experimental evidence showing that TRPV1 influences mitochondrial function. Full article
(This article belongs to the Special Issue Protein Quality Control and Integrated Stress Response Related to Pain Disorders)
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