https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:34507 2+ -calmodulin stimulated protein kinase II (CaMKII) is a major mediator of ischaemia-induced cell death and suggest that CaMKII would be a good target for neuroprotective therapies in acute treatment of stroke. However, as CaMKII regulates many cellular processes in many tissues any clinical treatment involving the inhibition of CaMKII would need to be able to specifically target the functions of ischaemia-activated CaMKII. In this review we summarise new developments in our understanding of the molecular mechanisms involved in ischaemia-induced CaMKII-mediated cell death that have identified ways in which such specificity of CaMKII inhibition after stroke could be achieved. We also review the mechanisms and phases of tissue damage in ischaemic stroke to identify where and when CaMKII-mediated mechanisms may be involved.]]> Wed 20 Mar 2019 10:25:57 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:13385 Wed 11 Apr 2018 17:04:51 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:17044 2+ and calmodulin (CaM) as regulators of the cell cycle. Ca²⁺/CaM-stimulated proteins, including the family of multifunctional Ca²⁺/CaM-stimulated protein kinases (CaMK), have also been identified as mediators of cell cycle progression. CaMKII is the best-characterized member of this family, and is regulated by multi-site phosphorylation and targeting. Using pharmacological inhibitors that were believed to be specific for CaMKII , CaMKII has been implicated in every phase of the cell cycle. However, these ‘specific’ inhibitors also produce effects on other CaMKs. These additional effects are usually ignored, and the effects of the inhibitors are normally attributed to CaMKII without further investigation. Using new specific molecular techniques, it has become clear that CaMKI is an important regulator of G₁, whereas CaMKII is essential for regulating G₂/M and the metaphase-anaphase transition. If the mechanisms controlling these events can be fully elucidated, new targets for controlling proliferative diseases may be identified.]]> Wed 11 Apr 2018 11:04:43 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:7995 Wed 11 Apr 2018 09:42:48 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:44961 2+ signalling in key events of cancer cell function and tumour progression, such as proliferation, migration, invasion and survival, has recently begun to be appreciated. Many cellular Ca²⁺-stimulated signalling cascades utilise the intermediate, calmodulin (CaM). The Ca²⁺/CaM complex binds and activates a variety of enzymes, including members of the multifunctional Ca²⁺/calmodulin-stimulated protein kinase (CaMK) family. These enzymes control a broad range of cancer-related functions in a multitude of tumour types. Herein, we explore the cancer-related functions of these kinases and discuss their potential as targets for therapeutic intervention.]]> Tue 25 Oct 2022 13:45:27 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:53626 Tue 12 Dec 2023 15:26:24 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:12418 Thu 30 Mar 2023 15:53:20 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:16963 Thu 30 Mar 2023 15:52:22 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:34319 2+-calmodulin stimulated protein kinase II) that initiates cell death. This study investigated the involvement of CaMKII phosphorylation at T286 and T253 in producing this persistent activation. In T286A-αCaMKII transgenic mice that lack the ability to phosphorylate αCaMKII at T286, transient occlusion of the middle cerebral artery for 90 min resulted in no significant difference in infarct size compared to normal littermate controls. Overexpression of the phospho-mimic mutant T286D-αCaMKII in differentiated neuroblastoma cell lines did not enhance excitotoxicity-induced cell death compared to overexpression of wild type αCaMKII. By contrast, overexpression of the phospho-mimic mutant T253D-αCaMKII significantly enhanced excitotoxicity-induced cell death whereas overexpression of the phospho-null mutant T253V-αCaMKII produced no enhancement. These results indicate that T286 phosphorylation does not play a significant role in ischaemia/excitotoxicity induced CaMKII-mediated cell death and suggest that T253 phosphorylation is required to produce the persistent activation of CaMKII involved in ischaemia/excitotoxicity induced cell death.]]> Thu 27 Jan 2022 15:59:30 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:13748 Sat 24 Mar 2018 10:39:18 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:1174 Sat 24 Mar 2018 08:28:28 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:1805 Sat 24 Mar 2018 08:27:31 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:19054 Sat 24 Mar 2018 08:05:15 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:17046 Sat 24 Mar 2018 08:05:06 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:52685 Fri 20 Oct 2023 10:05:02 AEDT ]]>