Free radicals are involved in continuous activation of nonreceptor tyrosine protein kinase c-Src after ischemia/reperfusion in rat hippocampus

Guo, Jun; Meng, Fanjie; Zhang, Guangyi; Zhang, Quanguang

doi:10.1016/s0304-3940(03)00483-x

Cited by 17 publications

(12 citation statements)

References 14 publications

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“…The level of phosphorylated Y416 was also found to be increased in both synaptosomes [160] and post-synaptic densities [16,35,160] prepared from the rodent forebrain region after the return of blood supply to the insulted area. In agreement with the immunoblotting data, in vitro enzyme activity assays confirmed that Src function in either whole hippocampal homogenates [78], or hippocampal synaptosomes [180] was clearly greater several hours after a brief period of global ischaemia.…”

Section: Ischaemia and The General Cellular Pattern Of Tyrosine Phospsupporting

confidence: 73%

Tyrosine Phosphorylation of the NMDA Receptor Following Cerebral Ischaemia

Pavlov¹,

Mielke²

2012

Protein Phosphorylation in Human Health

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Section: Ischaemia and The General Cellular Pattern Of Tyrosine Phospsupporting

confidence: 73%

Tyrosine Phosphorylation of the NMDA Receptor Following Cerebral Ischaemia

Pavlov¹,

Mielke²

2012

Protein Phosphorylation in Human Health

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“…Our previous studies have shown that Src activation is required for MAP kinase activation (15) and that sustained MAP kinase activation is required for optimal cell migration and proliferation in response to IGF-I (13). In addition, free radical-stimulated continuous activation of Src during ischemia/reperfusion has been reported in rat hippocampus (25), and oxidation of Src is a prerequisite for Src activation in response to IGF-I (9). However, free radicals diffuse quickly.…”

Section: Function Of Shps-1-localized Nox4mentioning

confidence: 99%

Recruitment of Nox4 to a Plasma Membrane Scaffold Is Required for Localized Reactive Oxygen Species Generation and Sustained Src Activation in Response to Insulin-like Growth Factor-I

Shen

Wai

et al. 2013

Journal of Biological Chemistry

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Background: Nox4-derived ROS is required for Src oxidation and activation. Results: Grb2 recruits Nox4 to the scaffold protein SHPS-1, and Nox4 colocalization with Src on SHPS-1 allows Nox4 to activate Src. Conclusion: Nox4 recruitment to SHPS-1 is essential for sustained Src activation and cell proliferation. Significance: This is the first report that localized ROS generation mediates growth factor signaling in vitro and in vivo.

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“…In this context, c-Src has been shown to be involved in both ligand-dependent mechanisms of Nox activation (as seen after AngII and aldosterone stimulation) (15,81) and ligand-independent mechanisms of Nox activation (as seen after hypoxia=reoxygenation injury) (69). Furthermore, the redox-activation of Src kinases following hypoxia=reoxygenation injury has been well established (22,31,32,40,105), although the link to Nox activation in this context remains understudied. This section will focus on mechanisms by which c-Src may play a role in the initiation, maintenance, and=or modulation of redoxosome-dependent signaling cascades that utilize NADPH oxidase, with a focus on the mechanisms involved in reoxygenation injury.…”

Section: Redoxosomal Signaling Via C-src In the Absence Of A Ligand Fmentioning

confidence: 99%

Signaling Components of Redox Active Endosomes: The Redoxosomes

Oakley

Abbott

et al. 2009

Antioxidants & Redox Signaling

184

160

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Subcellular compartmentalization of reactive oxygen species (ROS) plays a critical role in transmitting cell signals in response to environmental stimuli. In this regard, signals at the plasma membrane have been shown to trigger NADPH oxidase-dependent ROS production within the endosomal compartment and this step can be required for redox-dependent signal transduction. Unique features of redox-active signaling endosomes can include NADPH oxidase complex components (Nox1, Noxo1, Noxa1, Nox2, p47phox, p67phox, and=or Rac1), ROS processing enzymes (SOD1 and=or peroxiredoxins), chloride channels capable of mediating superoxide transport and=or membrane gradients required for Nox activity, and novel redox-dependent sensors that control Nox activity. This review will discuss the cytokine and growth factor receptors that likely mediate signaling through redox-active endosomes, and the common mechanisms whereby they act. Additionally, the review will cover ligand-independent environmental injuries, such as hypoxia=reoxygenation injury, that also appear to facilitate cell signaling through NADPH oxidase at the level of the endosome. We suggest that redox-active endosomes encompass a subset of signaling endosomes that we have termed redoxosomes. Redoxosomes are uniquely equipped with redox-processing proteins capable of transmitting ROS signals from the endosome interior to redox-sensitive effectors on the endosomal surface. In this manner, redoxosomes can control redoxdependent effector functions through the spatial and temporal regulation of ROS as second messengers. Antioxid. Redox Signal. 11, 1313-1333

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Free radicals are involved in continuous activation of nonreceptor tyrosine protein kinase c-Src after ischemia/reperfusion in rat hippocampus

Cited by 17 publications

References 14 publications

Tyrosine Phosphorylation of the NMDA Receptor Following Cerebral Ischaemia

Tyrosine Phosphorylation of the NMDA Receptor Following Cerebral Ischaemia

Recruitment of Nox4 to a Plasma Membrane Scaffold Is Required for Localized Reactive Oxygen Species Generation and Sustained Src Activation in Response to Insulin-like Growth Factor-I

Signaling Components of Redox Active Endosomes: The Redoxosomes

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