کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6276860 | 1295745 | 2010 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Glycogen synthase kinase-3β and the p25 activator of cyclin dependent kinase 5 increase pausing of mitochondria in neurons
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کلمات کلیدی
KLCp25eGFPenhanced chemiluminescentRPMIDAPIECLGSK-3βcdk5NGFaxoplasmic transport - حمل و نقل آکسوپلاسمیstandard error of the mean - خطای استاندارد میانگینKinesin light chain - زنجیره سبک Kinesinnerve growth factor - فاکتور رشد عصبSEM - مدل معادلات ساختاری / میکروسکوپ الکترونی روبشیpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازenhanced green fluorescent protein - پروتئین فلورسنت سبز افزایش یافته استcyclin dependent kinase 5 - کییناز وابسته به کیناز 5Glycogen synthase kinase-3β - گلیکوزین سنتاز کیناز 3β
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Glycogen synthase kinase-3β and the p25 activator of cyclin dependent kinase 5 increase pausing of mitochondria in neurons Glycogen synthase kinase-3β and the p25 activator of cyclin dependent kinase 5 increase pausing of mitochondria in neurons](/preview/png/6276860.png)
چکیده انگلیسی
The complex bi-directional axoplasmic transport of mitochondria is essential for proper metabolic functioning of neurons and is controlled by phosphorylation. We have investigated by time-lapse imaging the effects of increased expression of glycogen synthase kinase-3β (GSK-3β) and of the p25 activator of cyclin dependent kinase 5 on mitochondria movements in mammalian cortical neurons and in PC12 cells. Both GSK-3β and p25 increased the stationary behaviour of mitochondria in PC12 and in neurons, decreased their anterograde transport but did not affect the intrinsic velocities of mitochondria. The microtubule-associated tau proteins were more phosphorylated in GSK-3β and p25 transfected neurons, but ultrastructural observation showed that these cells still contained microtubules and nocodazole treatment further reduced residual mitochondria movements in GSK-3β or p25 transfected neurons, indicating that microtubule disruption was not the primary cause of increased mitochondrial stationary behaviour in GSK-3β or p25 transfected neurons. Our results suggest that increased expression of GSK-3β and p25 acted rather by decreasing the frequency of mitochondrial movements driven by molecular motors and that GSK-3β and p25 might regulate these transports by controlling the time that mitochondria spend pausing, rather than their velocities.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuroscience - Volume 167, Issue 4, 2 June 2010, Pages 1044-1056
Journal: Neuroscience - Volume 167, Issue 4, 2 June 2010, Pages 1044-1056
نویسندگان
M. Morel, M. Authelet, R. Dedecker, J.P. Brion,