کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2552814 | 1124864 | 2007 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Dynorphin peptides differentially regulate the human κ opioid receptor
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کلمات کلیدی
موضوعات مرتبط
علوم پزشکی و سلامت
پزشکی و دندانپزشکی
کاردیولوژی و پزشکی قلب و عروق
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![عکس صفحه اول مقاله: Dynorphin peptides differentially regulate the human κ opioid receptor Dynorphin peptides differentially regulate the human κ opioid receptor](/preview/png/2552814.png)
چکیده انگلیسی
Dynorphins, endogenous peptides for the κ opioid receptor, play important roles in many physiological and pathological functions. Here, we examined how prolonged treatment with three major prodynorphin peptides, dynorphin A (1-17) (Dyn A), dynorphin B (1-13) (Dyn B) and α-neoendorphin (α-Neo), regulated the human kappa opioid receptor (hKOR) stably expressed in Chinese hamster ovary (CHO) cells. Results from receptor binding and [35S]GTPγS binding assays showed that these peptides were potent full agonists of the hKOR with comparable receptor reserve and intrinsic efficacy to stimulate G proteins. A 4-h incubation with α-Neo at a concentration of â¼Â 600 Ã EC50 value (from [35S]GTPγS binding) resulted in receptor down-regulation to a much lower extent than the incubation with Dyn A and Dyn B at comparable concentrations (â¼Â 10% vs. â¼Â 65%). Extending incubation period and increasing concentrations did not significantly affect the difference. The plateau level of α-Neo-mediated receptor internalization (30 min) was significantly less than those of Dyn A and Dyn B. Omission of the serum from the incubation medium or addition of peptidase inhibitors into the serum-containing medium enhanced α-Neo-, but not Dyn A- or Dyn B-, mediated receptor down-regulation and internalization; however, the degrees of α-Neo-induced adaptations were still significantly less than those of Dyn A and Dyn B. Thus, these endogenous peptides differentially regulate KOR after activating the receptor with similar receptor occupancy and intrinsic efficacy. Both stability in the presence of serum and intrinsic capacity to promote receptor adaptation play roles in the observed discrepancy among the dynorphin peptides.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Life Sciences - Volume 80, Issue 15, 20 March 2007, Pages 1439-1448
Journal: Life Sciences - Volume 80, Issue 15, 20 March 2007, Pages 1439-1448
نویسندگان
Yong Chen, Chongguang Chen, Lee-Yuan Liu-Chen,