کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5816204 | 1115562 | 2009 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Combined roles of loops C and D in the interactions of a neonicotinoid insecticide imidacloprid with the α4β2 nicotinic acetylcholine receptor
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
LBDEC50NeonicotinoidsnAChRImaxACh - آهAcetylcholine - استیل کولینImidacloprid - ایمیداکلوپریدligand binding domain - دامنه اتصال لیگاندHomology modeling - مدل سازی همگراacetylcholine binding protein - پروتئین اتصال دهنده استیل کولینIon channels - کانال های یونیnicotinic acetylcholine receptor - گیرنده استیلکولین نیکوتین
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب رفتاری
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Combined roles of loops C and D in the interactions of a neonicotinoid insecticide imidacloprid with the α4β2 nicotinic acetylcholine receptor Combined roles of loops C and D in the interactions of a neonicotinoid insecticide imidacloprid with the α4β2 nicotinic acetylcholine receptor](/preview/png/5816204.png)
چکیده انگلیسی
Neonicotinoid insecticides are widely used for crop protection based on their selective actions on insect nicotinic acetylcholine receptors (insect nAChRs). Loops C and D in insect nAChRs have been shown to possess structural features favorable for neonicotinoid-nAChR interactions. However, it remains to be resolved whether such features serve either co-operatively, or independently, to enhance neonicotinoid sensitivity of nAChRs. We therefore examined using voltage-clamp electrophysiology the effects on the response to imidacloprid of combinatorial substitutions of residues in loops C and D of the chicken α4β2 nAChR by those present in insect nAChRs. The E219P mutation in loop C of the α4 subunit resulted in enhanced responses to imidacloprid of α4β2, whereas E219S and E219T mutations barely influenced its actions. On the other hand, mutations in loop D (T77R; E79V and T77N; E79R) alone shifted the imidacloprid concentration-response curve to the left (lower concentrations). Interestingly, all three mutations did, however, further enhance the agonist efficacy of imidacloprid when combined with the mutations in loop D. Such synergistic effects of the two loops on the interactions with imidaclprid were observed irrespective of subunit stoichiometry. Computational modeling of the ligand binding domain of the wild-type and mutant α4β2 nAChRs using the crystal structure of the acetylcholine binding protein from Lymnaea stagnalis also indicated that interactions with loop F of loops C and D may contribute to determining the response to imidacloprid.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuropharmacology - Volume 56, Issue 1, January 2009, Pages 264-272
Journal: Neuropharmacology - Volume 56, Issue 1, January 2009, Pages 264-272
نویسندگان
Kayoko Toshima, Satoshi Kanaoka, Atsushi Yamada, Kiyoshi Tarumoto, Miki Akamatsu, David B. Sattelle, Kazuhiko Matsuda,