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Autonomous activity of CaMKII is only transiently increased following the induction of long-term potentiation in the rat hippocampus

Lengyel, I.; Voss, K.; Cammaroto, M.; Bradshaw, K.; Brent, V.; Murphy, K. P. S. J.; Giese, K.P.; Rostas, J.A.P. and Bliss, T.V.P. (2004). Autonomous activity of CaMKII is only transiently increased following the induction of long-term potentiation in the rat hippocampus. European Journal of Neuroscience, 20(11) pp. 3063–3072.

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A major role has been postulated for a maintained increase in the autonomous activity of CaMKII in the expression of long-term potentiation (LTP). However, attempts to inhibit the expression of LTP with CaMKII inhibitors have yielded inconsistent results. Here we compare the changes in CaMKII autonomous activity and phosphorylation at Thr286 of αCaMKII in rat hippocampal slices using chemical or tetanic stimulation to produce either LTP or short-term potentiation (STP). Tetanus-induced LTP in area CA1 requires CaMKII activation and Thr286 phosphorylation of αCaMKII, but we did not observe an increase in autonomous activity. Next we induced LTP by 10 min exposure to 25 mm tetraethyl-ammonium (TEA) or 5 min exposure to 41 mm potassium (K) after pretreatment with calyculin A. Exposure to K alone produced STP. These protocols allowed us to monitor temporal changes in autonomous activity during and after exposure to the potentiating chemical stimulus. In chemically induced LTP, autonomous activity was maximally increased within 30 s whereas this increase was significantly delayed in STP. However, in both LTP and STP the two-fold increase in autonomous activity measured immediately after stimulation was short-lived, returning to baseline within 2–5 min after re-exposure to normal ACSF. In LTP, but not in STP, the phosphorylation of αCaMKII at Thr286 persisted for at least 60 min after stimulation. These results confirm that LTP is associated with a maintained increase in autophosphorylation at Thr286 but indicate that a persistent increase in the autonomous activity of CaMKII is not required for the expression of LTP.

Item Type: Journal Article
Copyright Holders: Federation of European Neuroscience Societies
ISSN: 0953-816X
Keywords: CaMKII; long-term potentiation; protein kinases; protein phosphatases; protein phosphorylation
Academic Unit/Department: Science > Life, Health and Chemical Sciences
Interdisciplinary Research Centre: Biomedical Research Network (BRN)
Item ID: 3590
Depositing User: Kerry Murphy
Date Deposited: 30 Jun 2006
Last Modified: 14 Jan 2016 15:56
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