Genistein inhibits glutamate-induced apoptotic processes in primary neuronal cell cultures: An involvement of aryl hydrocarbon receptor and estrogen receptor/glycogen synthase kinase-3β intracellular signaling pathway

Kajta, Małgorzata; Domin, Helena; Grynkiewicz, Grzegorz; Lasoń, W.

doi:10.1016/j.neuroscience.2006.11.059

Cited by 60 publications

(57 citation statements)

References 47 publications

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“…It is important to note that in the present study, despite the long incubation time, the drugs were used at low concentrations. Because protein trafficking takes time, it is appropriate to use the long term treatment in our study, which is actually consistent with many previous studies successfully using long term drug treatment to alter actin cytoskeleton, lipid rafts, and tyrosine phosphorylation (51)(52)(53)(54)(55).…”

Section: Journal Of Biological Chemistrysupporting

confidence: 85%

Clustering and Activity Tuning of Kv1 Channels in Myelinated Hippocampal Axons

2011

Journal of Biological Chemistry

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Precise localization of axonal ion channels is crucial for proper electrical and chemical functions of axons. In myelinated axons, Kv1 (Shaker) voltage-gated potassium (Kv) channels are clustered in the juxtaparanodal regions flanking the node of Ranvier. The clustering can be disrupted by deletion of various proteins in mice, including contactin-associated protein-like 2 (Caspr2) and transient axonal glycoprotein-1 (TAG-1), a glycosylphosphatidylinositol-anchored cell adhesion molecule. However, the mechanism and function of Kv1 juxtaparanodal clustering remain unclear. Here, using a new myelin coculture of hippocampal neurons and oligodendrocytes, we report that tyrosine phosphorylation plays a critical role in TAG-1-mediated clustering of axonal Kv1.2 channels. In the coculture, myelin specifically ensheathed axons but not dendrites of hippocampal neurons and clustered endogenous axonal Kv1.2 into internodes. The trans-homophilic interaction of TAG-1 was sufficient to position Kv1.2 clusters on axonal membranes in a neuron/HEK293 coculture. Mutating a tyrosine residue (Tyr 458 ) in the Kv1.2 C terminus or blocking tyrosine phosphorylation disrupted myelin-and TAG-1-mediated clustering of axonal Kv1.2. Furthermore, Kv1.2 voltage dependence and activation threshold were reduced by TAG-1 coexpression. This effect was eliminated by the Tyr 458 mutation or by cholesterol depletion. Taken together, our studies suggest that myelin regulates both trafficking and activity of Kv1 channels along hippocampal axons through TAG-1. Proper subcellular targeting of various Kv channels2 is critical for neuronal excitability and synaptic transmission. Molecular mechanisms underlying polarized axon-dendrite targeting of Kv channels have been extensively studied (1-10). In contrast, channel targeting in distinct membrane domains within axons is much less understood. Most axons in mammals are wrapped by layers of compact lipid membranes from myelinating glial cells, oligodendrocytes in the central nervous system (CNS) and Schwann cells in the peripheral nervous system. Myelinated axons form distinct membrane domains, such as nodes of Ranvier, paranodes, and juxtaparanodal (JXP), and internodal regions (11)(12)(13)(14). In myelinated axons of both CNS and peripheral nervous system, Kv1 channels are clustered into JXP regions, controlling the fidelity of action potential conduction (11,(15)(16)(17).Based on the findings that the JXP targeting of Kv1 channels was largely eliminated in both Caspr2 (contactin-associated protein-like 2) and TAG-1 (transient axonal glycoprotein-1) knock-out mice, it was hypothesized that Caspr2 interacts with TAG-1 and clusters Kv1 channels via a PDZ domain-containing protein (18,19). Whereas Caspr2 is expressed only in neurons, TAG-1 is expressed in both neurons and myelinating glial cells (19 -21). Caspr2 has a PDZ domain ligand at its C terminus, but deleting PDZ domain-containing proteins, such as PSD-95 (postsynaptic density-95) and/or PSD-93 (postsynaptic density-93), in mice had no effect on the K...

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Section: Journal Of Biological Chemistrysupporting

confidence: 85%

Clustering and Activity Tuning of Kv1 Channels in Myelinated Hippocampal Axons

2011

Journal of Biological Chemistry

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“…Apigenin consistently did not increase AMPK and ACC phosphorylations in HepG2 cells (Zang et al, 2006). Genistein protects cells at 0.1 to 40 M (Kajta et al, 2007;Kim et al, 2007), but the compound activates AMPK in adipocytes at 50 to 200 M (Hwang et al, 2005). Hence, its beneficial effect may not result from AMPK activation.…”

Section: Parp-lkb1-dependent Mitochondrial Protection 893mentioning

confidence: 90%

Resveratrol Protects Mitochondria against Oxidative Stress through AMP-Activated Protein Kinase-Mediated Glycogen Synthase Kinase-3β Inhibition Downstream of Poly(ADP-ribose)polymerase-LKB1 Pathway

Shin¹,

Cho²,

Kim³

2009

Mol Pharmacol

188

136

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Arachidonic acid (AA, a proinflammatory fatty acid) in combination with iron promotes excess reactive oxygen species (ROS) production and exerts a deleterious effect on mitochondria. We have shown previously that activation of AMP-activated protein kinase (AMPK) protects hepatocytes from AA ϩ iron-induced apoptosis. Resveratrol, a polyphenol in grapes, has beneficial effects mediated through SIRT1, LKB1, and AMPK. This study investigated the potential of resveratrol to protect against the mitochondrial impairment induced by AA ϩ iron and the underlying mechanism for this cytoprotection. Resveratrol treatment inhibited apoptosis, ROS production, and glutathione depletion elicited by AA ϩ iron in HepG2 cells. In addition, resveratrol attenuated superoxide generation in mitochondria and inhibited mitochondrial dysfunction induced by AA ϩ iron. Overall, AMPK activation by resveratrol contributed to cell survival, as supported by the reversal of its restoration of mitochondrial membrane potential by either overexpression of a dominant-negative mutant of AMPK␣ or compound C treatment. Resveratrol increased inhibitory phosphorylation of glycogen synthase kinase-3␤ (GSK3␤) downstream of AMPK, which contributed to mitochondrial protection and cell survival. Likewise, small interfering RNA knockdown of LKB1, an upstream kinase of AMPK, reduced the ability of resveratrol to protect cells from mitochondrial dysfunction. Furthermore, this LKB1-dependent mitochondrial protection resulted from resveratrol's poly(ADP-ribose)polymerase activation, but not SIRT1 activation, as supported by the experiment using 3-aminobenzamide, a poly(ADP-ribose)polymerase inhibitor. Other polyphenols, such as apigenin, genistein, and daidzein, did not activate AMPK or protect mitochondria against AA ϩ iron. Thus, resveratrol protects cells from AA ϩ iron-induced ROS production and mitochondrial dysfunction through AMPKmediated inhibitory phosphorylation of GSK3␤ downstream of poly(ADP-ribose)polymerase-LKB1 pathway.

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“…Genistein, a phytoestrogen, protects SH-SY5Y cells (Bang et al, 2004) as well as cultured hippocampal neurons (Zeng et al, 2004) from A␤ toxicity. However, in addition to its action on estrogen receptors, genistein is also a general tyrosine kinase inhibitor that protects cultured neurons from L-glutamate toxicity (Kajta et al, 2007). Genistein enhances the amplitude of ACh responses when human ␣7 nAChRs are expressed in Xe- FIG.…”

Section: B Nicotinic Receptor-mediated Neuroprotection: a Particularmentioning

confidence: 99%

“…The potentiating effect of genistein on AChevoked responses did not involve a large shift in the EC 50 for ACh (Grønlien et al, 2007). Thus, although an involvement of estrogen receptors has been demonstrated for the protective action of genistein (Kajta et al, 2007), it is tempting to speculate that the neuroprotective effect of genistein may also involve, at least in part, the enhancement of nAChR function through the inhibition of tyrosine kinase action upon nAChRs. In support of this notion, ␤-estradiol protects PC12 cells from amyloid toxicity, and this is prevented when ␣7 nAChRs are blocked with methyllycaconitine (Svensson and Nordberg, 1999).…”

Section: Nicotinic Acetylcholine Receptors and Alzheimer's Diseasementioning

confidence: 99%

Nicotinic Acetylcholine Receptor Signalling: Roles in Alzheimer's Disease and Amyloid Neuroprotection

et al. 2009

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Genistein inhibits glutamate-induced apoptotic processes in primary neuronal cell cultures: An involvement of aryl hydrocarbon receptor and estrogen receptor/glycogen synthase kinase-3β intracellular signaling pathway

Cited by 60 publications

References 47 publications

Clustering and Activity Tuning of Kv1 Channels in Myelinated Hippocampal Axons

Clustering and Activity Tuning of Kv1 Channels in Myelinated Hippocampal Axons

Resveratrol Protects Mitochondria against Oxidative Stress through AMP-Activated Protein Kinase-Mediated Glycogen Synthase Kinase-3β Inhibition Downstream of Poly(ADP-ribose)polymerase-LKB1 Pathway

Nicotinic Acetylcholine Receptor Signalling: Roles in Alzheimer's Disease and Amyloid Neuroprotection

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