کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8998371 | 1115625 | 2005 | 16 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Plasticity-specific phosphorylation of CaMKII, MAP-kinases and CREB during late-LTP in rat hippocampal slices in vitro
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کلمات کلیدی
CaMKIIAP5PKCα-amino-3-hydroxy-5-methyl-4-isoxazolepropionate receptorNMDARaCSFpKaAMPARTBSTPVDFmAbCREBPBSLFSEPSP - epspiMAPK/ERK - MAPK / ERKMonoclonal antibody - آنتی بادی مونوکلونالPopulation spike - افزایش جمعیتlow-frequency stimulation - تحریک با فرکانس پایینlong-term potentiation - تقویت درازمدتLTP - تقویت طولانی مدت یا LTP polyvinyl difluoride - دیوفوردین پلیوینیلSerine/threonine kinase - سریین / ترئونین کینازPhosphate buffered saline - فسفات بافر شورartificial cerebrospinal fluid - مایع مغزی نخاعی مصنوعیexcitatory postsynaptic potential - پتانسیل پست سیناپتی هیجان انگیزcAMP-dependent protein kinase A - پروتئین کیناز A وابسته به cAMPProtein kinase C - پروتئین کیناز سیN-methyl d-aspartate receptor - گیرنده N-methyl d-aspartate
موضوعات مرتبط
علوم زیستی و بیوفناوری
علم عصب شناسی
علوم اعصاب رفتاری
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چکیده انگلیسی
Processes of learning, memory formation and functional plasticity, such as long-term potentiation (LTP) are associated with activity changes of αCaMKII, MAPKs and CREB proteins. Little is known on the temporal regulation of the phosphorylation states of these proteins during late-LTP, a period which requires the synthesis of new macromolecules and has been postulated to correlate with the consolidation of a memory trace at the cellular level. We now present data from hippocampal slices in vitro obtained from adult rats that describe such specific phosphorylation changes of the above mentioned three molecules during early- and late-LTP. We detail that LTP induction and its maintenance reveals a delayed onset of continuous CREB phosphorylation with two separate peaks at 45 min and 6 h before it decays back to baseline phosphorylation levels; whereas αCaMKII and MAPK2 remain in a specific, but enhanced phosphorylation state throughout the induction, early- and late-LTP. These LTP-regulated phopshorylation events were NMDAR-dependent and upon the activity of a translated serine-threonine kinase. Interestingly, only the late enhancement of pCREB was clearly dependent on protein synthesis. Our data extend results describing the regulation of αCaMKII, MAPKs and CREB phosphorylation during early stages of LTP, suggesting a specific role of these enzymes also during phases of LTP consolidation in adult animals.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Neuropharmacology - Volume 49, Issue 4, September 2005, Pages 477-492
Journal: Neuropharmacology - Volume 49, Issue 4, September 2005, Pages 477-492
نویسندگان
Tariq Ahmed, Julietta U. Frey,