Glutamate signalling in non-neuronal tissues

Skerry, Timothy M.; Genever, Paul G.

doi:10.1016/s0165-6147(00)01642-4

Cited by 275 publications

(196 citation statements)

References 54 publications

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“…On the contrary, not selective inhibitors such as l-aspartic acid (IC 50 = 5 ± 1,8 M), l-glutamic acid (IC 50 = 6.6 ± 2,7 M) and THA (IC 50 = 3 ± 1,2 M) and SOS (IC 50 = 110 ± 22 M), an EAAT1 and EAAT3 inhibitor, effectively inhibited platelet glutamate uptake, although SOS K i value was higher compared to those of other inhibitors but similar to that previously observed in human motor cortex [2]. The IC 50 values of each inhibitor were calculated from at least four independent experiments and expressed as mean ± S.E.M.…”

Section: Resultssupporting

confidence: 74%

“…A high affinity glutamate uptake, with kinetic characteristics similar to brain synaptosomes, was also shown in platelets, which appear the major site of clearance of glutamate from blood [34]. NMDA receptors were described in platelets [22,50] and in megakaryocytes [24,50], suggesting their importance in regulating platelet activation and aggregation. We recently described a glutamate release from platelets during aggregation, underling that peripheral glutamate signaling seems to play a role in the regulation of platelet functions [33].…”

Section: Introductionmentioning

confidence: 98%

“…Platelets were extensively studied as models of synaptic apparatus, since they release and reuptake neurotransmitters such as serotonin and dopamine [3,57], express serotonin [51] and glutamate receptors [23,50] and they served as clinical markers for neuropsychiatric disorders such as depression. Moreover, in AD they were recently proposed as CNS model to study molecular amyloid-precursor protein (APP) alterations [9].…”

Section: Introductionmentioning

confidence: 99%

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Glutamate transporters in platelets: EAAT1 decrease in aging and in Alzheimer’s disease

Zoia

Cogliati

Tagliabue

et al. 2004

Neurobiology of Aging

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Platelets release glutamate upon activation and are an important clearance system of the amino acid from blood, through high-affinity glutamate uptake, similar to that described in brain synaptosomes. Since platelet glutamate uptake is decreased in neurodegenerative disorders, we performed a morphological and molecular characterization of platelet glutamate transporters. The three major brain glutamate transporters EAAT1, EAAT2 and EAAT3 are expressed in platelets, with similar molecular weight, although at lower density than brain. A Na + -dependent-high-affinity glutamate uptake was competitively inhibited by known inhibitors but not by dihydrokainic acid, suggesting platelet EAAT2 does not play a major role in glutamate uptake at physiological conditions. We observed decreased glutamate uptake V max , without modification of transporter affinity, in aging, which could be linked to the selective decrease of EAAT1 expression and mRNA. Moreover, in AD patients we found a further EAAT1 reduction compared to age-matched controls, which could explain the decrease of platelet uptake previously described. Platelet glutamate transporters may be used as peripheral markers to investigate the role of glutamate in patients with neuropsychiatric disorders.

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Section: Resultssupporting

confidence: 74%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Glutamate transporters in platelets: EAAT1 decrease in aging and in Alzheimer’s disease

Zoia

Cogliati

Tagliabue

et al. 2004

Neurobiology of Aging

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“…The glutamatergic system consists of glutamate receptor, vesicular glutamate transporter (VGLUT) and plasma glutamate transporter 12 . Multiple glutamate receptors have been found in the pancreas [13][14][15][16] .…”

Section: Introductionmentioning

confidence: 99%

Sp1 Is Required for Glucose-Induced Transcriptional Regulation of Mouse Vesicular Glutamate Transporter 2 Gene

Bai

et al. 2008

Gastroenterology

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Background & Aims-Vesicular glutamate transporter (VGLUT) has been reported to be involved in glucose-induced insulin secretion. It has been shown that glucose stimulates the expression of VGLUT isoform 2 (VGLUT2) in β cells via transcriptional mechanism. In this study, we identified the mouse VGLUT2 (mVGLUT2) promoter and characterized the transcriptional mechanism of glucose-stimulated mVGLUT2 expression in β-cells.

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“…8 mGlu receptors are found in peripheral cells that do not receive synaptic innervation (such as thymocytes, hepatocytes, keratinocytes, melanocytes, osteoblasts, and cells of the male germ line), and that, with the exception of melanocytes, do not originate from the neural crest. 9 Individual mGlu receptors have been detected in cancer cells both inside and outside the CNS. [10][11][12][13] In addition, mGlu receptor subtypes with a long C-terminal domain are endowed with 'constitutive activity', and are therefore active in the absence of extracellular glutamate.…”

mentioning

confidence: 99%

Metabotropic glutamate receptors regulate differentiation of embryonic stem cells into GABAergic neurons

et al. 2008

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Mouse embryonic stem (ES) cells were stimulated to differentiate either as adherent monolayer cultures in DMEM/F12 supplemented with N2/B27, or as floating embryoid bodies (EBs) exposed to 1 lM retinoic acid (RA) for 4 days, starting from 4 DIV, and subsequently re-plated in DMEM/F12 medium. Adherent monolayer cultures of ES cells expressed mGlu5 receptors throughout the entire differentiation period. Selective pharmacological blockade of mGlu5 receptors with methyl-6-(phenylethynyl)-pyridine (MPEP) (1 lM, added once a day) accelerated the appearance of the neuronal marker, b-tubulin. In addition, treatment with MPEP increased the number of cells expressing glutamate decarboxylase-65/67 (GAD 65/67 ), a marker of GABAergic neurons. In floating EBs, mGlu5 receptors are progressively replaced by mGlu4 receptors. The orthosteric mGlu4/6/ 7/8 receptor agonist, L-2-amino-4-phosphonobutanoate (L-AP4), or the selective mGlu4 receptor enhancer, PHCCC, -both combined with RA at concentrations of 30 lM -increased the expression of both b-tubulin and GAD 65/67 , inducing the appearance of fully differentiated neurons that released GABA in response to membrane depolarization. We conclude that mGlu receptor subtypes regulate neuronal differentiation of ES cells in a context-dependent manner, and that subtype-selective ligands of these receptors might be used for the optimization of in vitro protocols aimed at producing GABAergic neurons from ES cells.

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Glutamate signalling in non-neuronal tissues

Cited by 275 publications

References 54 publications

Glutamate transporters in platelets: EAAT1 decrease in aging and in Alzheimer’s disease

Glutamate transporters in platelets: EAAT1 decrease in aging and in Alzheimer’s disease

Sp1 Is Required for Glucose-Induced Transcriptional Regulation of Mouse Vesicular Glutamate Transporter 2 Gene

Metabotropic glutamate receptors regulate differentiation of embryonic stem cells into GABAergic neurons

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