Differential effects of ischemia and reperfusion on c-Jun N-terminal kinase isoform protein and activity

Shackelford, Deborah A.; Yeh, Richard

doi:10.1016/s0169-328x(01)00245-5

Cited by 19 publications

(17 citation statements)

References 62 publications

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“…9B). Previously we reported increased activity of a 29-30-kDa c-Jun kinase in the particulate fractions of rabbit spinal cord after ischemia and reperfusion (Shackelford and Yeh, 2001). This activity segregated with the Triton X-100-insoluble material in the rabbit, whereas the 32-35-kDa activity was detected in the cytosols and detergent-soluble and -insoluble fractions of the rat brain.…”

Section: Activation Of a 32-35-kda Cjun Kinase During Reperfusionmentioning

confidence: 86%

“…Previously we demonstrated that JNK activity could be directly analyzed by an in-gel kinase assay of total cytosolic or particulate fractions from rabbit spinal cord, employing a GST-c-Jun or GST-ATF-2 construct as substrate (Shackelford and Yeh, 2001). In rabbit or rat brain homogenates, however, other proteins obscure direct identification of JNK isoforms.…”

Section: Jnk Phosphorylation and Activity During Ischemia And Reperfumentioning

confidence: 99%

“…7). The JNK1 p46 isoform accounts for the majority of activity in CNS tissue (Shackelford and Yeh, 2001;Kuan et al, 2003;Brecht et al, 2005). JNK1 activity was specifically monitored by an in-gel kinase assay of the Fig.…”

Section: Jnk Phosphorylation and Activity During Ischemia And Reperfumentioning

confidence: 99%

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Modulation of ERK and JNK activity by transient forebrain ischemia in rats

Shackelford

Yeh

2006

J of Neuroscience Research

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The mitogen-activated protein (MAP) kinase families of ERK and JNK participate in numerous intracellular signaling pathways and are abundantly expressed in the CNS. Activation of ERK and JNK during reperfusion of ischemic tissue is implicated in promoting cell death, insofar as inhibition of either pathway reduces neuronal cell death. However, ERK or JNK activation provides protection in other neuronal injury models. In this study, we monitored the concurrent modulation of ERK and JNK activity in the hippocampus, neocortex, and striatum during ischemia and immediately upon reperfusion in a rat model of transient global ischemia. All three regions incur a similar reduction in blood flow during occlusion but show different extents and temporal patterns of injury following reperfusion. ERK and JNK were active in the normal rat forebrain, and phosphorylation was reduced by ischemia. Upon reperfusion, ERK was rapidly activated in the hippocampus, neocortex, and striatum, whereas JNK phosphorylation increased in the hippocampus and striatum but not in the neocortex. The response of JNK vs. ERK more closely reflects the susceptibility of these regions. JNK1 was the predominant phosphorylated isoform. A minor pool of phosphorylated JNK3 increased above the control level after reperfusion in hippocampal but not in neocortical particulate fractions. In addition, a novel 32-35-kDa c-Jun kinase activity was detected in the hippocampus, neocortex, and striatum. The results show that ERK and JNK activities are rapidly, but not identically, modulated by ischemia and reperfusion and indicate that the MAP kinase pathways contribute to regulating the response to acute CNS injury.

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Section: Activation Of a 32-35-kda Cjun Kinase During Reperfusionmentioning

confidence: 86%

Section: Jnk Phosphorylation and Activity During Ischemia And Reperfumentioning

confidence: 99%

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Modulation of ERK and JNK activity by transient forebrain ischemia in rats

Shackelford

Yeh

2006

J of Neuroscience Research

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“…Hayashi et al [97] demonstrated that JNK1 protein expression was increased, phosphorylated, and translocated to nuclei in the brain after focal ischaemia. However, in a reversible rabbit spinal cord ischaemia model, ischaemia caused a decrease in JNK1 activity implying that cell death in-duced by acute neuronal injury was not associated with increased total JNK activity [98] . In an animal model of stroke, p-JNK was found in neurons undergoing apoptosis [99] , while p-JNK was colocalized with TUNEL-positive apoptotic neurons after cerebral ischaemia in mice [96] .…”

Section: Jnk and Phosphorylated Jnkmentioning

confidence: 89%

Pathophysiology of Acute Ischaemic Stroke: An Analysis of Common Signalling Mechanisms and Identification of New Molecular Targets

et al. 2006

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Stroke continues to be a major cause of death and disability. The currently available therapies have proven to be highly unsatisfactory (except thrombolysis) and attempts are being made to identify and characterize signalling proteins which could be exploited to design novel therapeutic modalities. The pathophysiology of stroke is a complex process. Delaying interventions from the first hours to days or even weeks following blood vessel occlusion may lead to worsening or impairment of recovery in later stages. The objective of this review is to critically evaluate the major mechanisms underlying stroke pathophysiology, especially the role of cell signalling in excitotoxicity, inflammation, apoptosis, neuroprotection and angiogenesis, and highlight potential novel targets for drug discovery.

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“…The neuroprotective effects of anthocyanin on phospho-JNK and p53 level in vivoThe activation of c-Jun N-terminal kinase (JNK) and p53 upregulation are associated with neuronal cell death in cerebral ischemia(Hayashi et al, 2000;Krupinski et al, 2003;Li et al, 1997;Renolleau et al, 1997;Shackelford and Yeh, 2001). Thus, Morphological evaluation and TUNEL assay (magnification 400×).…”

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confidence: 99%