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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Pasek, Johanna G. Wang, Xiaohan Colbran, Roger J. |
| Description | Country affiliation: United States Author Affiliation: Pasek JG ( Department of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, TN, United States.); Wang X ( Vanderbilt Brain Institute, Vanderbilt University Medical Center, Nashville, TN, United States); Colbran RJ ( Department of Molecular Physiology and Biophysics, Vanderbilt University Medical Center, Nashville, TN, United States) |
| Abstract | Calcium signaling regulates synaptic plasticity and many other functions in striatal medium spiny neurons to modulate basal ganglia function. Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is a major calcium-dependent signaling protein that couples calcium entry to diverse cellular changes. CaMKII activation results in autophosphorylation at Thr286 and sustained calcium-independent CaMKII activity after calcium signals dissipate. However, little is known about the mechanisms regulating striatal CaMKII. To address this, mouse brain slices were treated with pharmacological modulators of calcium channels and punches of dorsal striatum were immunoblotted for CaMKII Thr286 autophosphorylation as an index of CaMKII activation. KCl depolarization increased levels of CaMKII autophosphorylation ~2-fold; this increase was blocked by an LTCC antagonist and was mimicked by treatment with pharmacological LTCC activators. The chelation of extracellular calcium robustly decreased basal CaMKII autophosphorylation within 5min and increased levels of total CaMKII in cytosolic fractions, in addition to decreasing the phosphorylation of CaMKII sites in the GluN2B subunit of NMDA receptors and the GluA1 subunit of AMPA receptors. We also found that the maintenance of basal levels of CaMKII autophosphorylation requires low-voltage gated T-type calcium channels, but not LTCCs or R-type calcium channels. Our findings indicate that CaMKII activity is dynamically regulated by multiple calcium channels in the striatum thus coupling calcium entry to key downstream substrates. |
| File Format | HTM / HTML |
| ISSN | 10447431 |
| e-ISSN | 10959327 |
| DOI | 10.1016/j.mcn.2015.08.003 |
| Journal | Molecular and Cellular Neuroscience |
| Volume Number | 68 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Cell Biology Discipline Molecular Biology Discipline Neurology Calcium Channels, L-type Physiology Calcium-calmodulin-dependent Protein Kinase Type 2 Metabolism Corpus Striatum Pharmacology Animals Calcium Calcium Channel Agonists Calcium Channel Blockers Chelating Agents Drug Effects Egtazic Acid Analogs & Derivatives Enzyme Inhibitors Gene Expression Regulation In Vitro Techniques Mice Mice, Inbred C57bl Pyrroles Receptors, Glutamate Signal Transduction Spider Venoms Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Cellular and Molecular Neuroscience |
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