Identification of protein kinase C domains involved in its translocation induced by propofol
Propofol is widely used for general anesthesia and sedation; however, the mechanisms of its anesthetic and adverse effects are not fully understood. We have previously shown that propofol activates protein kinase C (PKC) and induces its translocation in a subtype-specific manner. The purpose of this...
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| Published in | European journal of pharmacology Vol. 955; p. 175806 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier B.V
15.09.2023
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| Abstract | Propofol is widely used for general anesthesia and sedation; however, the mechanisms of its anesthetic and adverse effects are not fully understood. We have previously shown that propofol activates protein kinase C (PKC) and induces its translocation in a subtype-specific manner. The purpose of this study was to identify the PKC domains involved in propofol-induced PKC translocation. The regulatory domains of PKC consist of C1 and C2 domains, and the C1 domain is subdivided into the C1A and C1B subdomains. Mutant PKCα and PKCδ with each domain deleted were fused with green fluorescent protein (GFP) and expressed in HeLa cells. Propofol-induced PKC translocation was observed by time-lapse imaging using a fluorescence microscope. The results showed that persistent propofol-induced PKC translocation to the plasma membrane was abolished by the deletion of both C1 and C2 domains in PKCα and by the deletion of the C1B domain in PKCδ. Therefore, propofol-induced PKC translocation involves the C1 and C2 domains of PKCα and the C1B domain of PKCδ. We also found that treatment with calphostin C, a C1 domain inhibitor, abolished propofol-induced PKCδ translocation. In addition, calphostin C inhibited the propofol-induced phosphorylation of endothelial nitric oxide synthase (eNOS). These results suggest that it may be possible to modulate the exertion of propofol effects by regulating the PKC domains involved in propofol-induced PKC translocation.
•Propofol. a general anesthetic, induced the translocation of PKCαand PKCδ.•Both C1 and C2 domains were required for propofol-induced PKCα translocation.•The C1B domain was critical for propofol-induced PKCδ translocation.•Calphostin C, a C1 domain inhibitor, abolished propofol-induced PKCδ translocation. |
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| AbstractList | Propofol is widely used for general anesthesia and sedation; however, the mechanisms of its anesthetic and adverse effects are not fully understood. We have previously shown that propofol activates protein kinase C (PKC) and induces its translocation in a subtype-specific manner. The purpose of this study was to identify the PKC domains involved in propofol-induced PKC translocation. The regulatory domains of PKC consist of C1 and C2 domains, and the C1 domain is subdivided into the C1A and C1B subdomains. Mutant PKCα and PKCδ with each domain deleted were fused with green fluorescent protein (GFP) and expressed in HeLa cells. Propofol-induced PKC translocation was observed by time-lapse imaging using a fluorescence microscope. The results showed that persistent propofol-induced PKC translocation to the plasma membrane was abolished by the deletion of both C1 and C2 domains in PKCα and by the deletion of the C1B domain in PKCδ. Therefore, propofol-induced PKC translocation involves the C1 and C2 domains of PKCα and the C1B domain of PKCδ. We also found that treatment with calphostin C, a C1 domain inhibitor, abolished propofol-induced PKCδ translocation. In addition, calphostin C inhibited the propofol-induced phosphorylation of endothelial nitric oxide synthase (eNOS). These results suggest that it may be possible to modulate the exertion of propofol effects by regulating the PKC domains involved in propofol-induced PKC translocation.Propofol is widely used for general anesthesia and sedation; however, the mechanisms of its anesthetic and adverse effects are not fully understood. We have previously shown that propofol activates protein kinase C (PKC) and induces its translocation in a subtype-specific manner. The purpose of this study was to identify the PKC domains involved in propofol-induced PKC translocation. The regulatory domains of PKC consist of C1 and C2 domains, and the C1 domain is subdivided into the C1A and C1B subdomains. Mutant PKCα and PKCδ with each domain deleted were fused with green fluorescent protein (GFP) and expressed in HeLa cells. Propofol-induced PKC translocation was observed by time-lapse imaging using a fluorescence microscope. The results showed that persistent propofol-induced PKC translocation to the plasma membrane was abolished by the deletion of both C1 and C2 domains in PKCα and by the deletion of the C1B domain in PKCδ. Therefore, propofol-induced PKC translocation involves the C1 and C2 domains of PKCα and the C1B domain of PKCδ. We also found that treatment with calphostin C, a C1 domain inhibitor, abolished propofol-induced PKCδ translocation. In addition, calphostin C inhibited the propofol-induced phosphorylation of endothelial nitric oxide synthase (eNOS). These results suggest that it may be possible to modulate the exertion of propofol effects by regulating the PKC domains involved in propofol-induced PKC translocation. Propofol is widely used for general anesthesia and sedation; however, the mechanisms of its anesthetic and adverse effects are not fully understood. We have previously shown that propofol activates protein kinase C (PKC) and induces its translocation in a subtype-specific manner. The purpose of this study was to identify the PKC domains involved in propofol-induced PKC translocation. The regulatory domains of PKC consist of C1 and C2 domains, and the C1 domain is subdivided into the C1A and C1B subdomains. Mutant PKCα and PKCδ with each domain deleted were fused with green fluorescent protein (GFP) and expressed in HeLa cells. Propofol-induced PKC translocation was observed by time-lapse imaging using a fluorescence microscope. The results showed that persistent propofol-induced PKC translocation to the plasma membrane was abolished by the deletion of both C1 and C2 domains in PKCα and by the deletion of the C1B domain in PKCδ. Therefore, propofol-induced PKC translocation involves the C1 and C2 domains of PKCα and the C1B domain of PKCδ. We also found that treatment with calphostin C, a C1 domain inhibitor, abolished propofol-induced PKCδ translocation. In addition, calphostin C inhibited the propofol-induced phosphorylation of endothelial nitric oxide synthase (eNOS). These results suggest that it may be possible to modulate the exertion of propofol effects by regulating the PKC domains involved in propofol-induced PKC translocation. Propofol is widely used for general anesthesia and sedation; however, the mechanisms of its anesthetic and adverse effects are not fully understood. We have previously shown that propofol activates protein kinase C (PKC) and induces its translocation in a subtype-specific manner. The purpose of this study was to identify the PKC domains involved in propofol-induced PKC translocation. The regulatory domains of PKC consist of C1 and C2 domains, and the C1 domain is subdivided into the C1A and C1B subdomains. Mutant PKCα and PKCδ with each domain deleted were fused with green fluorescent protein (GFP) and expressed in HeLa cells. Propofol-induced PKC translocation was observed by time-lapse imaging using a fluorescence microscope. The results showed that persistent propofol-induced PKC translocation to the plasma membrane was abolished by the deletion of both C1 and C2 domains in PKCα and by the deletion of the C1B domain in PKCδ. Therefore, propofol-induced PKC translocation involves the C1 and C2 domains of PKCα and the C1B domain of PKCδ. We also found that treatment with calphostin C, a C1 domain inhibitor, abolished propofol-induced PKCδ translocation. In addition, calphostin C inhibited the propofol-induced phosphorylation of endothelial nitric oxide synthase (eNOS). These results suggest that it may be possible to modulate the exertion of propofol effects by regulating the PKC domains involved in propofol-induced PKC translocation. •Propofol. a general anesthetic, induced the translocation of PKCαand PKCδ.•Both C1 and C2 domains were required for propofol-induced PKCα translocation.•The C1B domain was critical for propofol-induced PKCδ translocation.•Calphostin C, a C1 domain inhibitor, abolished propofol-induced PKCδ translocation. |
| ArticleNumber | 175806 |
| Author | Uchida, Kazue Narasaki, Soshi Urabe, Tomoaki Hide, Izumi Tanaka, Shigeru Sakai, Norio Tsutsumi, Yasuo M. Kajimoto, Taketoshi Harada, Kana Yanase, Yuhki Noguchi, Soma |
| Author_xml | – sequence: 1 givenname: Soshi surname: Narasaki fullname: Narasaki, Soshi organization: Dept of Mol & Pharmacol Neurosci, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 2 givenname: Soma surname: Noguchi fullname: Noguchi, Soma organization: Dept of Mol & Pharmacol Neurosci, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 3 givenname: Tomoaki surname: Urabe fullname: Urabe, Tomoaki organization: Dept of Mol & Pharmacol Neurosci, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 4 givenname: Kana surname: Harada fullname: Harada, Kana organization: Dept of Mol & Pharmacol Neurosci, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 5 givenname: Izumi surname: Hide fullname: Hide, Izumi organization: Dept of Mol & Pharmacol Neurosci, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 6 givenname: Shigeru surname: Tanaka fullname: Tanaka, Shigeru organization: Dept of Mol & Pharmacol Neurosci, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 7 givenname: Yuhki surname: Yanase fullname: Yanase, Yuhki organization: Dept of Pharmacotherapy, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 8 givenname: Taketoshi surname: Kajimoto fullname: Kajimoto, Taketoshi organization: Div of Biochem, Dept of Biochem and Mol Biol, Kobe Univ Grad Sch of Med, Japan – sequence: 9 givenname: Kazue surname: Uchida fullname: Uchida, Kazue organization: Dept of Dermatology, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 10 givenname: Yasuo M. surname: Tsutsumi fullname: Tsutsumi, Yasuo M. organization: Dept of Anesthesiology ＆ Critical Care, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan – sequence: 11 givenname: Norio orcidid: 0000-0002-6648-8761 surname: Sakai fullname: Sakai, Norio email: nsakai@hiroshima-u.ac.jp organization: Dept of Mol & Pharmacol Neurosci, Grad Sch of Biomed & Health Sci, Hiroshima Univ, Japan |
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| Keywords | Translocation Protein kinase C Propofol Endothelial nitric oxide synthase (eNOS) |
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| Title | Identification of protein kinase C domains involved in its translocation induced by propofol |
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