التفاصيل البيبلوغرافية
| العنوان: |
Opioid-Modulated Receptor Localization and Erk1/2 Phosphorylation in Cells Coexpressing μ-Opioid and Nociceptin Receptors. |
| المؤلفون: |
Zhuo, Guan-Yu, Chen, Ming-Chi, Lin, Tzu-Yu, Lin, Shih-Ting, Chen, Daniel Tzu-Li, Lee, Cynthia Wei-Sheng |
| المصدر: |
International Journal of Molecular Sciences; Jan2023, Vol. 24 Issue 2, p1048, 16p |
| مصطلحات موضوعية: |
OPIOID receptors, NOCICEPTIN, FLUORESCENCE resonance energy transfer, LIPID rafts |
| مستخلص: |
We attempted to examine the alterations elicited by opioids via coexpressed μ-opioid (MOP) and nociceptin/orphanin FQ (NOP) receptors for receptor localization and Erk1/2 (p44/42 MAPK) in human embryonic kidney (HEK) 293 cells. Through two-photon microscopy, the proximity of MOP and NOP receptors was verified by fluorescence resonance energy transfer (FRET), and morphine but not buprenorphine facilitated the process of MOP-NOP heterodimerization. Single-particle tracking (SPT) further revealed that morphine or buprenorphine hindered the movement of the MOP-NOP heterodimers. After exposure to morphine or buprenorphine, receptor localization on lipid rafts was detected by immunocytochemistry, and phosphorylation of Erk1/2 was determined by immunoblotting in HEK 293 cells expressing MOP, NOP, or MOP+NOP receptors. Colocalization of MOP and NOP on lipid rafts was enhanced by morphine but not buprenorphine. Morphine stimulated the phosphorylation of Erk1/2 with a similar potency in HEK 293 cells expressing MOP and MOP+NOP receptors, but buprenorphine appeared to activate Erk1/2 solely through NOP receptors. Our results suggest that opioids can fine-tune the cellular localization of opioid receptors and phosphorylation of Erk1/2 in MOP+NOP-expressing cells. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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