Protein Kinase C-γ and Calcium/Calmodulin-Dependent Protein Kinase II-α Are Persistently Translocated to Cell Membranes of the Rat Brain during and after Middle Cerebral Artery Occlusion
(2004) In Journal of Cerebral Blood Flow and Metabolism 24(1). p.54-61- Abstract
The levels of protein kinase C-γ (PKC-γ) and the calcium/calmodulin-dependent kinase II-α (CaMKII-α) were measured in crude synaptosomal (P2), particulate (P3), and cytosolic (S3) fractions of the neocortex of rats exposed to 1-hour and 2-hour middle cerebral artery occlusion (MCAO) and 2-hour MCAO followed by 2-hour reperfusion. During MCAO, PKC levels increased in P2 and P3 in the most severe ischemic areas concomitantly with a decrease in S3. In the penumbra, PKCγ decreased in S3 without any significant increases in P2 and P3. Total PKC-γ also decreased in the penumbra but not in the ischemic core, suggesting that the protein is degraded by an energy-dependent mechanism, possibly by the 26S proteasome. The CaMKII-α levels increased... (More)
The levels of protein kinase C-γ (PKC-γ) and the calcium/calmodulin-dependent kinase II-α (CaMKII-α) were measured in crude synaptosomal (P2), particulate (P3), and cytosolic (S3) fractions of the neocortex of rats exposed to 1-hour and 2-hour middle cerebral artery occlusion (MCAO) and 2-hour MCAO followed by 2-hour reperfusion. During MCAO, PKC levels increased in P2 and P3 in the most severe ischemic areas concomitantly with a decrease in S3. In the penumbra, PKCγ decreased in S3 without any significant increases in P2 and P3. Total PKC-γ also decreased in the penumbra but not in the ischemic core, suggesting that the protein is degraded by an energy-dependent mechanism, possibly by the 26S proteasome. The CaMKII-α levels increased in P2 but not P3 during ischemia and reperfusion in all ischemic regions, particularly in the ischemic core. Concomitantly, the levels in S3 decreased by 20% to 40% in the penumbra and by approximately 80% in the ischemic core. There were no changes in the total levels of CaMKII-α during MCAO. The authors conclude that during and after ischemia, PKC and CaMKII-α are translocated to the cell membranes, particularly synaptic membranes, where they may modulate cellular function, such as neurotransmission, and also affect cell survival. Drugs preventing PKC and/or CaMKII-α translocation may prove beneficial against ischemic cell death.
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- author
- Matsumoto, Shohei ; Shamloo, Mehrdad ; Matsumoto, Eriko ; Isshiki, Atsushi and Wieloch, Tadeusz LU
- organization
- publishing date
- 2004-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- CaMKII, Cell death, Protein kinase C, Signal transduction, Stroke
- in
- Journal of Cerebral Blood Flow and Metabolism
- volume
- 24
- issue
- 1
- pages
- 8 pages
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:0347363880
- pmid:14688616
- ISSN
- 0271-678X
- language
- English
- LU publication?
- yes
- id
- 2d9703f6-a4f1-489a-8cd1-6dc3a7b9b3ac
- date added to LUP
- 2016-10-05 15:04:16
- date last changed
- 2024-05-17 13:30:12
@article{2d9703f6-a4f1-489a-8cd1-6dc3a7b9b3ac, abstract = {{<p>The levels of protein kinase C-γ (PKC-γ) and the calcium/calmodulin-dependent kinase II-α (CaMKII-α) were measured in crude synaptosomal (P2), particulate (P3), and cytosolic (S3) fractions of the neocortex of rats exposed to 1-hour and 2-hour middle cerebral artery occlusion (MCAO) and 2-hour MCAO followed by 2-hour reperfusion. During MCAO, PKC levels increased in P2 and P3 in the most severe ischemic areas concomitantly with a decrease in S3. In the penumbra, PKCγ decreased in S3 without any significant increases in P2 and P3. Total PKC-γ also decreased in the penumbra but not in the ischemic core, suggesting that the protein is degraded by an energy-dependent mechanism, possibly by the 26S proteasome. The CaMKII-α levels increased in P2 but not P3 during ischemia and reperfusion in all ischemic regions, particularly in the ischemic core. Concomitantly, the levels in S3 decreased by 20% to 40% in the penumbra and by approximately 80% in the ischemic core. There were no changes in the total levels of CaMKII-α during MCAO. The authors conclude that during and after ischemia, PKC and CaMKII-α are translocated to the cell membranes, particularly synaptic membranes, where they may modulate cellular function, such as neurotransmission, and also affect cell survival. Drugs preventing PKC and/or CaMKII-α translocation may prove beneficial against ischemic cell death.</p>}}, author = {{Matsumoto, Shohei and Shamloo, Mehrdad and Matsumoto, Eriko and Isshiki, Atsushi and Wieloch, Tadeusz}}, issn = {{0271-678X}}, keywords = {{CaMKII; Cell death; Protein kinase C; Signal transduction; Stroke}}, language = {{eng}}, number = {{1}}, pages = {{54--61}}, publisher = {{Nature Publishing Group}}, series = {{Journal of Cerebral Blood Flow and Metabolism}}, title = {{Protein Kinase C-γ and Calcium/Calmodulin-Dependent Protein Kinase II-α Are Persistently Translocated to Cell Membranes of the Rat Brain during and after Middle Cerebral Artery Occlusion}}, volume = {{24}}, year = {{2004}}, }