کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9002490 | 1118588 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Glycine taken up through GLYT1 and GLYT2 heterotransporters into glutamatergic axon terminals of mouse spinal cord elicits release of glutamate by homotransporter reversal and through anion channels
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کلمات کلیدی
GDA[3H]d-aspartatedl-threo-β-benzyloxyaspartic acidNppbVGLUT1PSD-95GFAP5-nitro-2-(3-phenylpropylamino)benzoic acid - 5-نیترو-2- (3-phenylpropylamino) بنزوئیک اسید5,7-dichlorokynurenic acid - 5،7-dichlorokynurenic اسیدdl-TBOA - DL-TBOASDS–PAGE - SDS-PAGECarrier-mediated release - آزادی رسانه ای نهادSDS–polyacrylamide gel electrophoresis - الکتروفورز ژل SDS-polyacrylamide gelglutamate release - انتشار گلوتاماتBAPTA - بیایپیتیایGlial fibrillary acidic protein - پروتئین اسیدی فیبریلاسیون گلایالanion channels - کانال های آنیونی
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
داروشناسی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Glycine concentration-dependently elicited [3H]d-aspartate ([3H]d-ASP) release from superfused mouse spinal cord synaptosomes. Glycine effect was insensitive to strychnine or 5,7-dichlorokynurenic acid, but was prevented by the glycine transporter blocker glycyldodecylamide. Glycine also evoked release of endogenous glutamate, which was sensitive to glycyldodecylamide and abolished in low-Na+ medium. Experiments with purified synaptosomes and gliasomes show that the glycine-evoked [3H]d-ASP release largely originates from glutamatergic nerve terminals. The glycine-evoked [3H]d-ASP release was halved by NFPS, a selective blocker of GLYT1 transporters, or by Org 25543, a selective GLYT2 blocker, and almost abolished by a mixture of the two, suggesting that activation of GLYT1 and GLYT2 present on glutamatergic terminals triggers the release of [3H]d-ASP. Accordingly, confocal microscopy experiments show localization of GLYT1 and GLYT2 in purified synaptosomes immuno-stained for the vesicular glutamate transporter vGLUT1. The glycine effect was independent of extra- and intraterminal Ca2+ ions. It was partly inhibited by the glutamate transporter blocker dl-TBOA and largely prevented by the anion channel blockers niflumic acid and NPPB. To conclude, transporters for glycine (GLYT1 or/and GLYT2) and for glutamate coexist on the same spinal cord glutamatergic terminals. Activation of glycine heterotransporters elicits glutamate release partly by homotransporter reversal and largely through anion channels.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical Pharmacology - Volume 69, Issue 1, 1 January 2005, Pages 159-168
Journal: Biochemical Pharmacology - Volume 69, Issue 1, 1 January 2005, Pages 159-168
نویسندگان
Luca Raiteri, Sara Stigliani, Antonella Siri, Mario Passalacqua, Edon Melloni, Maurizio Raiteri, Giambattista Bonanno,