کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9415810 | 1614323 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Chronic treatment with amyloid β1-42 inhibits non-cholinergic high-affinity choline transport in NG108-15 cells through protein kinase C signaling
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کلمات کلیدی
NMStPAAPPPKCHC-3N-methylscopolamineCHT1tetradecanoyl phorbol acetateAβ1–42 - Aβ1-42β-Amyloid - β-آمیلوئیدHemicholinium-3 binding - اتصال هیمیکولینیم-3Disorders of the nervous system - اختلالات سیستم عصبیCholine transporter-like protein - پروتئین حمل کننده مانند کولینamyloid precursor protein - پروتئین پیش ماده آمیلوئیProtein kinase C - پروتئین کیناز سی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Chronic treatment with amyloid β1-42 inhibits non-cholinergic high-affinity choline transport in NG108-15 cells through protein kinase C signaling Chronic treatment with amyloid β1-42 inhibits non-cholinergic high-affinity choline transport in NG108-15 cells through protein kinase C signaling](/preview/png/9415810.png)
چکیده انگلیسی
We investigated the influence of the amyloid-β-peptide1-42 on hemicholinum-3-sensitive high-affinity choline uptake in NG108-15 cells. RT-PCR analysis revealed the presence of mRNA for a choline transporter-like protein but not for cholinergic high-affinity choline transporter. Differentiation of cells increased both hemicholinum-3-sensitive choline uptake and high-affinity hemicholinium-3 binding. This transport was not influenced by tenfold excess of carnitine. Continuous presence of submicromolar concentrations of amyloid-β-peptide1-42 during differentiation resulted in a decrease of both choline uptake and hemicholinium-3 binding. These effects were not present when amyloid-β-peptide1-42 was added 5 min prior to measurements. Neither differentiation nor amyloid-β-peptide1-42 treatment changed levels of choline transporter-like protein mRNA. Protein kinase C inhibition by staurosporine or its inactivation by continuous presence of tetradecanoyl phorbol acetate prevented the inhibitory effect of amyloid-β-peptide1-42 treatment on choline uptake. Activation of protein kinase C by tetradecanoyl phorbol acetate during measurement had inhibitory effect on choline uptake in control but not amyloid-β-peptide1-42-treated cells. The concentration of amyloid-β-peptide1-42 maximally effective on hemicholinium-3-sensitive choline uptake had no effect on cell growth, oxidative activity, membrane integrity, number of surface muscarinic receptors, caspase-3 and -8 activities, or uptake of deoxyglucose. Results demonstrate that long-term treatment with non-toxic concentrations of amyloid-β-peptide1-42 downregulates choline uptake presumably mediated by a choline transporter-like protein through activation of protein kinase C signaling. The decrease of choline uptake may have relevance to the pathogenesis of Alzheimer's disease.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Brain Research - Volume 1062, Issues 1â2, 16 November 2005, Pages 101-110
Journal: Brain Research - Volume 1062, Issues 1â2, 16 November 2005, Pages 101-110
نویسندگان
Jana Nováková, Lenka Mikasová, Eva Machová, VÄra Lisá, VladimÃr Doležal,