کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1964297 | 1058540 | 2007 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Heterooligomerization of human dopamine receptor 2 and somatostatin receptor 2
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کلمات کلیدی
ICLsomatostatin-28somatostatin-14C-tailTMDPBSforskolinPTXGPCRFskNGSG-protein-coupled receptor - G-پروتئین گیرندهDimerization - اندازه گیریIntracellular loop - حلقه داخل سلولیDopamine - دوپامینnormal goat serum - سرم طبیعی بزPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریHeterodimerization - ناپایداریDopamine receptor - گیرنده دوپامینSomatostatin receptor - گیرنده سوماتوستاتین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Somatostatin and dopamine receptors are well expressed and co-localized in several brain regions, suggesting the possibility of functional interactions. In the present study we used a combination of pharmacological, biochemical and photobleaching fluorescence resonance energy transfer (pbFRET) to determine the functional interactions between human somatostatin receptor 2 (hSSTR2) and human dopamine receptor 2 (hD2R) in both co-transfected CHO-K1 or HEK-293 cells as well as in cultured neuronal cells which express both the receptors endogenously. In monotransfected CHO-K1 or HEK-293 cells, D2R exists as a preformed dimer which is insensitive to agonist or antagonist treatment. In control CHO-K1 cells stably co-transfected with hD2R and hSSTR2, relatively low FRET efficiency and weak expression in co-immunoprecipitate from HEK-293 cells suggest the absence of preformed heterooligomers. However, upon treatment with selective ligands, hD2R and hSSTR2 exhibit heterodimerization. Agonist-induced heterodimerization was accompanied by increased affinity for dopamine and augmented hD2R signalling as well as prolonged hSSTR2 internalization. In contrast, cultured striatal neurons display constitutive heterodimerization between D2R and SSTR2, which were agonist-independent. However, heterodimerization in neurons was completely abolished in the presence of the D2R antagonist eticlopride. These findings suggest that hD2R and hSSTR2 operate as functional heterodimers modulated by ligands in situ, which may prove to be a useful model in designing new therapeutic drugs.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 19, Issue 11, November 2007, Pages 2304-2316
Journal: Cellular Signalling - Volume 19, Issue 11, November 2007, Pages 2304-2316
نویسندگان
Alessandra Baragli, Haydar Alturaihi, Heather L. Watt, Ali Abdallah, Ujendra Kumar,