کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4341115 | 1295824 | 2007 | 16 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Neurotrophin B receptor kinase increases Kv subfamily member 1.3 (Kv1.3) ion channel half-life and surface expression
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
MCLC terminusIPLEPLinternal plexiform layer of the olfactory bulbcopy DNAGCLKv1.3HEK 293GFPKv1.5MYCN terminusBDNF - BDNF یا فاکتور نورونزایی مشتقشده از مغز BSA - BSAcDNA - cDNAbovine serum albumin - آلبومین سرم گاوhomogenization buffer - بافر همگن سازیTyrosine kinase - تیروزین کینازminimum essential medium - حداقل حداقل مورد نیازhuman embryonic kidney 293 cells - سلول های انسانی جنینی انسان 293Shaker - شاکرendoplasmic reticulum - شبکه آندوپلاسمی Brain-derived neurotrophic factor - فاکتور نوروتروفی مشتق شده از مغزPhenylalanine - فنیلآلانینTrafficking - قاچاقexternal plexiform layer of the olfactory bulb - لایه بیرونی خارجی لامپ بویاییmitral cell layer of the olfactory bulb - لایه سلولی میترال لامپ بویاییglomerular layer of the olfactory bulb - لنف گلومرول لامپ بویاییMEM - مامانNeurotrophins - نوروتروفین olfactory bulb - پیاز بویاییPotassium channel - کانال پتاسیمInsulin receptor kinase - کیناز گیرنده انسولین
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب (عمومی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Kv subfamily member 1.3 (Kv1.3), a member of the Shaker family of potassium channels, has been found to play diverse roles in immunity, metabolism, insulin resistance, sensory discrimination, and axonal targeting in addition to its traditional role in the stabilization of the resting potential. We demonstrate that the neurotrophin B receptor (TrkB) causes an upregulation of Kv1.3 ion channel protein expression in the absence of the preferred ligand for the receptor (brain-derived neurotrophic factor; BDNF) and oppositely downregulates levels of Kv subfamily member 1.5. Although the effect occurs in the absence of the ligand, Kv1.3 upregulation by TrkB is dependent upon the catalytic domain of the TrkB kinase as well as tyrosine (Y) residues in the N and C terminus of the Kv1.3 channel. Using pulse-chase experiments we find that TrkB alters the half-life residence of the channel by approximately 2Ã and allows it to sustain activity as reflected in an increased current magnitude without alteration of kinetic properties. TrkB and Kv1.3 co-immunoprecipitate from tissue preparations of the mouse olfactory bulb and olfactory cortex, and by immunocytochemical approaches, are found to be co-localized in the glomerular, mitral cell, and internal plexiform layers of the olfactory bulb. These data suggest that Kv1.3 is not only modulated by direct phosphorylation in the presence of BDNF-activated TrkB kinase, but also may be fine tuned via regulation of surface expression while in the proximity of neurotrophic factor receptors. Given the variability of TrkB expression during development, regeneration, or neuronal activation, modulation of surface expression and turnover of Kv channels could significantly impact neuronal excitability, distinct from that of tyrosine kinase phosphorylation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuroscience - Volume 144, Issue 2, 19 January 2007, Pages 531-546
Journal: Neuroscience - Volume 144, Issue 2, 19 January 2007, Pages 531-546
نویسندگان
B.S. Colley, K.C. Biju, A. Visegrady, S. Campbell, D.A. Fadool,