کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6277696 | 1295771 | 2009 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The distribution and characterization of endogenous protein arginine N-methyltransferase 8 in mouse CNS
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کلمات کلیدی
ADMAEWS12nPRMTISHSNRPAGEVPLORFMo5RMCCPUmAbPBSBSA - BSAIn situ hybridization - Hybridization در محلmonoclonal Ab - Monoclonal Abbovine serum albumin - آلبومین سرم گاوpolyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدIHC - ایمونوهیستوشیمیImmunohistochemistry - ایمونوهیستوشیمیabducens nucleus - تحریک هستهsubstantia nigra - توده سیاهSubcellular distribution - توزیع زیر سلولیRoom temperature - دمای اتاقasymmetric dimethylarginine - دی متیل آرژینین نامتقارنhorse serum - سرب اسبpostnuclear supernatant - فلوئور اتانولopen reading frame - قاب خواندن بازPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریhypoglossal nucleus - هسته hypoglossalReticular nucleus - هسته Reticularmotor trigeminal nucleus - هسته سه هسته ای موتورCaudate putamen - پاتامن CaudateProtein methylation - پروتئین متیلاسیونPNS - کارمندان دولت
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب (عمومی)
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چکیده انگلیسی
Protein arginine N-methyltransferase (PRMT) 8 was first discovered from a database search for genes harboring four conserved methyltransferase motifs, which shares more than 80% homology to PRMT1 in amino acid [Lee J, Sayegh J, Daniel J, Clarke S, Bedford MT (2005) PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J Biol Chem 280:32890-32896]. Interestingly, its tissue distribution is strikingly restricted to mouse CNS. To characterize the function in the CNS neurons, we raised an antiserum against PRMT8 to perform immunohistochemistry (IHC) and Western blot analysis. By IHC, the immunoreactivity of endogenous PRMT8 was broadly distributed in the CNS neurons with markedly intense signals in the cerebellum, hippocampal formation, and cortex, but was not detected in the cerebellar granular layer. In some subset of the neurons, the immunoreactivity was observed in the dendrites and axon bundles. The subcellular localization of the immunoreactivity was dominantly nuclear, arguing against the original report that exogenously expressed PRMT8 localizes to the plasma membrane via the N-terminal myristoylation. A series of the exogenously expressed proteins with different in-frame translation initiation codons was tested for comparison with the endogenous protein in molecular size. The third initiator codon produced the protein that was equivalent in size to the endogenous and showed a similar localizing pattern in PC12 cells. In conclusion, PRMT8 is a neuron-specific nuclear enzyme and the N-terminus does not contain the glycine end for myristoylation target.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuroscience - Volume 163, Issue 4, 10 November 2009, Pages 1146-1157
Journal: Neuroscience - Volume 163, Issue 4, 10 November 2009, Pages 1146-1157
نویسندگان
A. Kousaka, Y. Mori, Y. Koyama, T. Taneda, S. Miyata, M. Tohyama,