Stimulation of excitatory amino acid release from adult mouse brain glia subcellular particles by high mobility group box 1 protein

Pedrazzi, Marco; Raiteri, Luca; Bonanno, Giambattista; Patrone, Mauro; Ledda, S.; Passalacqua, Mario; Milanese, Marco; Melloni, Edon; Raiteri, Maurizio; Pontremoli, S.; Sparatore, Bianca

doi:10.1111/j.1471-4159.2006.04120.x

Cited by 70 publications

(74 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After decapitation, the cerebellum was rapidly removed and placed in ice-cold medium, and nerve terminals (purified synaptosomes) were prepared as reported previously (Nakamura et al, 1993;Pedrazzi et al, 2006;Marcoli et al, 2008). In brief, the tissue was homogenized in 10 volumes of 0.32 M sucrose, buffered at pH 7.4 with Tris-HCl, using a glass-Teflon tissue grinder (clearance, 0.25 mm).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of Presynaptic Release-Facilitatory Kainate Autoreceptors by Extracellular Cyclic GMP

Cervetto¹,

Maura²,

Marcoli³

2009

J Pharmacol Exp Ther

View full text Add to dashboard Cite

We found that both ␣-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) and kainate autoreceptors were present on the glutamate-releasing terminals of cerebellar parallel/climbing fibers and that they functioned as facilitatory autoreceptors. Extracellular cGMP inhibited the neurotransmitter release evoked by presynaptic kainate receptor activation; the inhibitory effect of extracellular cGMP was selective for the kainate autoreceptor-mediated response and did not affect the AMPA autoreceptor-mediated response. Endogenously synthesized cGMP might be the physiological source for the extracellular cGMP modulating the response to kainate autoreceptor activation.It has long been known that intracellular cGMP, whose production is linked through nitric oxide formation to the activation of cerebellar glutamatergic transmission, functions as a crucial cerebellar intracellular messenger, e.g., in the long-term depression of excitatory transmission at parallel fiber-Purkinje cell synapses (Ito and Karachot, 1992;Boxall and Garthwaite, 1996;Daniel et al., 1998;Hartell, 2001, and references therein). It is also known that cGMP can be actively transported from the intracellular compartment to extracellular fluid through membrane transport proteins (including a probenecid-sensitive transporter and members of the multidrug-resistance protein family; Sager, 2004). Activation of glutamate receptors has been shown to increase intracellular cGMP levels and to cause cGMP release from the intracellular to the extracellular compartment in cultured cerebellar neurons (Montoliu et al., 1999) or in cerebellar slices (in a probenecid-sensitive way) (Tjörnhammar et al., 1986), with the extracellular cGMP levels matching the intracellular levels. Indeed, extracellular cGMP has been exploited in in vivo models as a reliable measure of activation of cerebellar glutamatergic transmission (Wood and Rao, 1991;Luo et al., 1994;Fedele and Raiteri, 1999). Nevertheless, the roles of extracellular cGMP in the cerebellum have hardly been studied. Interference of cGMP with the response to activation of ionotropic glutamate receptors has been occasionally reported in cultured cerebellar cells; extracellular cGMP has been reported to inhibit glutamate responses at ␣-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)/ kainate receptors in Purkinje cells and in granules (Linden et al., 1995;Poulopoulou and Nowak, 1998) and to prevent glutamate neurotoxicity in cerebellar neurons (Montoliu et al., 1999). It has also been reported to inhibit binding to a kainate low-affinity site in rat cerebellum membranes (Migani et al., 1997).We investigated the ability of extracellular cGMP to interfere with AMPA/kainate receptor responses in the adult cerebellum, by using superfused purified synaptosomes, which allow direct functional evidence of presynaptic release-regulating receptors. Two aspects were investigated: 1) the presence and functioning of AMPA and kainate autoreceptors on the glutamatergic terminals of rat cerebellar parallel/climbin...

show abstract

Section: Methodsmentioning

confidence: 99%

Inhibition of Presynaptic Release-Facilitatory Kainate Autoreceptors by Extracellular Cyclic GMP

Cervetto¹,

Maura²,

Marcoli³

2009

J Pharmacol Exp Ther

View full text Add to dashboard Cite

show abstract

“…Several studies suggest that extracellular HMGB1 can aggravate tissue damage in neuronal tissues. 10,43 In these studies, extracellular HMGB1 plays a key role in the development of neuronal injury through the induction of inflammation, microglial activation, and neuronal excitotoxicity. According to these recent reports, the presence of extracellular HMGB1 concomitantly with MCP-1 is a possible deteriorating factor for RD, in spite of its essential role in the nucleus.…”

Section: Hmgb1 In Retinal Detachment N Arimura Et Almentioning

confidence: 99%

Intraocular expression and release of high-mobility group box 1 protein in retinal detachment

Arimura

Kii

Hashiguchi

et al. 2009

Laboratory Investigation

View full text Add to dashboard Cite

High-mobility group box 1 (HMGB1) protein is a multifunctional protein, which is mainly present in the nucleus and is released extracellularly by dying cells and/or activated immune cells. Although extracellular HMGB1 is thought to be a typical danger signal of tissue damage and is implicated in diverse diseases, its relevance to ocular diseases is mostly unknown. To determine whether HMGB1 contributes to the pathogenesis of retinal detachment (RD), which involves photoreceptor degeneration, we investigated the expression and release of HMGB1 both in a retinal cell death induced by excessive oxidative stress in vitro and in a rat model of RD-induced photoreceptor degeneration in vivo. In addition, we assessed the vitreous concentrations of HMGB1 and monocyte chemoattractant protein 1 (MCP-1) in human eyes with RD. We also explored the chemotactic activity of recombinant HMGB1 in a human retinal pigment epithelial (RPE) cell line. The results show that the nuclear HMGB1 in the retinal cell is augmented by death stress and upregulation appears to be required for cell survival, whereas extracellular release of HMGB1 is evident not only in retinal cell death in vitro but also in the rat model of RD in vivo. Furthermore, the vitreous level of HMGB1 is significantly increased and is correlated with that of MCP-1 in human eyes with RD. Recombinant HMGB1 induced RPE cell migration through an extracellular signalregulated kinase-dependent mechanism in vitro. Our findings suggest that HMGB1 is a crucial nuclear protein and is released as a danger signal of retinal tissue damage. Extracellular HMGB1 might be an important mediator in RD, potentially acting as a chemotactic factor for RPE cell migration that would lead to an ocular pathological wound-healing response.

show abstract

“…And HMGB1 also regulated the release of excitatory neurotransmitters. Pedraai suggested (Pedrazzi et al., 2006) that HMGB1 also promotes the release of endogenous glutamic acid and D‐aspartic acid in vitro from glial cells. In the study of AD, the expression of HMGB1 was coexisting with the senile plaques induced by β‐amyloid peptide (Aβ).…”

Section: Introductionmentioning

confidence: 99%

High expression of the HMGB1–TLR4 axis and its downstream signaling factors in patients with Parkinson's disease and the relationship of pathological staging

Yang

Han

et al. 2018

Brain and Behavior

View full text Add to dashboard Cite

ObjectiveTo detect the expression of high‐mobility group box protein 1 (HMGB1) and toll‐like receptor 4 (TLR4) and their downstream signaling factors—myeloid differentiation factor 88 (MyD88), nuclear factor kappa B (NF‐κB), and tumor necrosis factor alpha (TNF‐α)—in the sera of patients with Parkinson's disease (PD) in order to evaluate the relationship of the HMGB1–TLR4 axis with PD development and progression.MethodsThe serum HMGB1 and TLR4 protein levels of 120 patients with PD and 100 healthy volunteers were measured using double‐antibody sandwich ELISA, and their correlations with PD staging, disease duration, drug treatment effectiveness, and clinical classification were analyzed. In addition, their correlations with the key downstream factors of the HMGB1–TLR4 axis (MyD88, NF‐κB, and TNF‐α) were analyzed.ResultsHMGB1 and TLR4 expressions were higher in the peripheral blood of patients with PD than in healthy volunteers. PD patients with poor drug treatment outcomes had significantly higher HMGB1 and TLR4 expressions than PD patients with stable drug treatment outcomes. Higher HMGB1 and TLR4 expressions were found in patients at higher PD stages, and patients with >4‐year disease duration had significantly higher HMGB1 and TLR4 expressions than patients with <4‐year disease duration. No significant difference in HMGB1 and TLR4 expressions was found among patients with tremor‐dominant, akinetic‐rigid, and mixed subtypes of PD. NF‐κB and TNF‐α expressions were positively correlated with high expression of the HMGB1–TLR4 axis.ConclusionHigh expression of the HMGB1–TLR4 axis is closely associated with PD development, progression, drug treatment effectiveness, staging, and disease duration and has great significance for PD diagnosis and treatment.

show abstract

Stimulation of excitatory amino acid release from adult mouse brain glia subcellular particles by high mobility group box 1 protein

Cited by 70 publications

References 51 publications

Inhibition of Presynaptic Release-Facilitatory Kainate Autoreceptors by Extracellular Cyclic GMP

Inhibition of Presynaptic Release-Facilitatory Kainate Autoreceptors by Extracellular Cyclic GMP

Intraocular expression and release of high-mobility group box 1 protein in retinal detachment

High expression of the HMGB1–TLR4 axis and its downstream signaling factors in patients with Parkinson's disease and the relationship of pathological staging

Contact Info

Product

Resources

About