Glutamate receptor channels in rat DRG neurons: Activation by kainate and quisqualate and blockade of desensitization by con A

Huettner, James E.

doi:10.1016/0896-6273(90)90163-a

Cited by 399 publications

(339 citation statements)

References 58 publications

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“…This result agrees with an earlier study (Bowie et al 2003) of channel regulation that used high speed agonist applications to outside-out macropatches. Bowie and colleagues (2003) found no change in the time constant of desensitization following modulation of homomeric GluR6 channels by extracellular treatment with Con A (Huettner, 1990), or by co-expression of the cytoplasmic PDZ domain protein PSD-95 (Garcia et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

KRIP6: A novel BTB/kelch protein regulating function of kainate receptors

Laezza

Wilding

Sequeira

et al. 2007

Molecular and Cellular Neuroscience

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Whereas many interacting proteins have been identified for AMPA and NMDA glutamate receptors, fewer are known to directly bind and regulate function of kainate receptors. Using a yeast two-hybrid screen for interacting partners of the C-terminal domain of GluR6a, we identified a novel neuronal protein of the BTB/kelch family, KRIP6. KRIP6 binds to the GluR6a C-terminal domain at a site distinct from the PDZ-binding motif and it co-immunoprecipitates with recombinant and endogenous GluR6. Co-expression of KRIP6 alters GluR6 mediated currents in a heterologous expression system reducing peak current amplitude and steady-state desensitization, without affecting surface levels of GluR6. Endogenous KRIP6 is widely expressed in brain and overexpression of KRIP6 reduces endogenous kainate receptor-mediated responses evoked in hippocampal neurons. Taken together, these results suggest that KRIP6 can directly regulate native kainate receptors and provide the first evidence for a BTB/kelch protein in direct functional regulation of a mammalian glutamate receptor.

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Section: Discussionmentioning

confidence: 99%

KRIP6: A novel BTB/kelch protein regulating function of kainate receptors

Laezza

Wilding

Sequeira

et al. 2007

Molecular and Cellular Neuroscience

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“…Kainate-preferring receptors can be distinguished from AMPA receptors by differential sensitivities to ConA and cyclothiozide (Partin et al, 1993). However, with the exception of the dorsal root ganglia in the periphery (Huettner, 1990;Pat-tin et al, 1993), responses of kainate-preferring channels have not been reported when patch clamping CNS cells in slices (Jonas and Sakmann, 1992; reviewed by Wisden and Seeburg, 1993a,b). One possible reason for this is that functional kainate receptors could be largely located on distal dendrites and so elude detection by standard patch-clamping techniques.…”

Section: Discussionmentioning

confidence: 99%

Kainate receptor gene expression in the developing rat brain

1994

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Kainate-preferring receptors are a subclass of ionotropic glutamate receptors that might play a role in brain development. The expression of the five known genes encoding kainate receptor subunits (GluR-5, -6, -7, KA-1, and KA-2) was studied by in situ hybridization during pre- and postnatal development of the rat brain. We compared the combined expression patterns of these genes with autoradiography using 3H- kainate in the developing brain from embryonic day 12 (E12) through to adult. Although mRNAs for the receptor subunits (except KA-1) can be detected at stage E12, 3H-kainic acid binding (as an index of receptor protein) is not found at this stage. However, by E14 high-affinity kainate sites are found throughout the gray matter, but particularly in spinal cord, primordial cerebellum, and ventral forebrain structures. All genes undergo a peak in their expression in the late embryonic/early postnatal period. GluR-5 expression during development shows the most interesting features because the changes are qualitative. The GluR-5 gene shows peaks of expression around the period of birth in the sensory cortex (layers II, III, and IV), in CA1 hippocampal interneurons in the stratum oriens, in the septum, and in the thalamus. GluR-6 shows a prenatal expression peak in the cingulate gyrus of the neocortex. KA-1 transcripts appear with the development of the hippocampus and remain largely confined to discrete areas such as the CA3 region, the dentate gyrus, and subiculum. KA-2 transcripts are found throughout the CNS from as early as E12 and remain constant until adulthood. The GluR-5 and GluR-6 genes are coexpressed in multiple peripheral ganglia (e.g., cranial nerve ganglia, dorsal root ganglia, and mural ganglia) at E14.

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“…Some excitatory amino acids, however, that are not related structurally to kainate, including 5-bromowillardiine (Agrawal & Evans, 1986) and some derivatives of 2-(carboxycyclopropyl)glycine (CCG) , also cause considerable depolarization of the dorsal root fibre, and 5-bromowillardiine is much more potent than kainate in causing depolarization of the dorsal root fibre. Therefore, they have been regarded as kainate-type agonists (Watkins et al, 1990a;Ishida et al, 1991 (Agrawal & Evans, 1986) and the dorsal root ganglion (Huettner, 1990) while it did not occur in the spinal motoneurone. Therefore, the difference in degree of development of receptor desensitization between both preparations may play a key role for a difference in the rank order of the depolarizing activity, but the existence of different types of kainate receptors is also strongly suggested.…”

Section: Cross Desensitization Between Kainate Derivativesmentioning

confidence: 99%

“…At present, highly specific antagonists for kainate receptors are not yet available, therefore, it is difficult to classify electrophysiologically these derivatives as pure kainate agonists, but it has been reported that dorsal root C fibres of immature rats are directly depolarized by kainic acid, whereas quisqualate and (± )-2-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) are much less active than kainate, and Nmethyl-D-aspartate (NMDA) does not cause depolarization of the dorsal root even at higher concentrations (Davies et al, 1979;Agrawal & Evans, 1986;Huettner, 1990), although the pharmacological properties of the dorsal root C fibre depolarization have been reported to be not always identical to those of spinal motoneurones (Evans et al, 1987;Shinozaki, 1991). Therefore, we have compared the neuropharmacological properties of depolarizations induced by kainoids in spinal motoneurones and dorsal root fibres of the newborn rat.…”

Section: Introductionmentioning

confidence: 99%

Novel kainate derivatives: potent depolarizing actions on spinal motoneurones and dorsal root fibres in newborn rats

Ishida

Shinozaki²

1991

British J Pharmacology

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1Neuropharmacological actions of several kainate derivatives (kainoids) were examined for electrophysiological effects in the isolated spinal cord and the dorsal root fibre of the newborn rat. 2 Some kainoids caused depolarization of the motoneurone much more effectively than kainic acid or domoic acid and others were weaker. The rank order of the depolarizing activities of the kainoids tested here is as follows: 442-methoxyphenyl)-2-carboxy-3-pyrrolidineacetic acid (MFPA) > acromelic acid A > domoic acid _ 4-(2-hydroxyphenyl)-2-carboxy-3-pyrrolidineacetic acid (HFPA) _ acromelic acid B > kainic acid. 3 In the isolated dorsal root fibre, domoic acid caused the most significant depolarization. There were distinct differences with regard to the rank order of the depolarizing activity between the motoneurone and the dorsal root fibre. The rank order in the dorsal root fibre is domoic acid > acromelic acid B > 5-bromowillardiine _ MFPA > acromelic acid A > HFPA > kainic acid. 4 Significant desensitization of kainate receptors was observed in the isolated dorsal root fibre during prolonged application of L-glutamate, kainate and its derivatives. Cross desensitization was also observed among these excitatory amino acids. Receptors desensitized by kainate did not respond to MFPA, HFPA and acromelic acids, suggesting that these kainate derivatives activated common kainate receptors in the dorsal root fibre.5 In both motoneurones and dorsal root fibres, 6-cyano-7-nitroquinoxaline-2,3-dione (CNQX) effectively depressed the depolarization induced by kainoids, and neither 3-[(±)-2-carboxypiperazin-4-yl]propyl-1-phosphonic acid (CPP) nor picrotoxin blocked or affected the depolarization, but there were some differences in pharmacological potencies of glutamate antagonists between both preparations. 6 MFPA, HFPA and acromelic acids should provide valuable pharmacological tools for analysis of physiological functions of excitatory amino acids, in particular, as specific agonists for some subtypes of kainate receptors.

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Glutamate receptor channels in rat DRG neurons: Activation by kainate and quisqualate and blockade of desensitization by con A

Cited by 399 publications

References 58 publications

KRIP6: A novel BTB/kelch protein regulating function of kainate receptors

KRIP6: A novel BTB/kelch protein regulating function of kainate receptors

Kainate receptor gene expression in the developing rat brain

Novel kainate derivatives: potent depolarizing actions on spinal motoneurones and dorsal root fibres in newborn rats

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