Immunohistochemical localization of N-methyl-D-aspartate and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionate receptor subunits in the substantia nigra pars compacta of the rat
Immunohistochemical localization of N-methyl-D-aspartate and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionate receptor subunits in the substantia nigra pars compacta of the rat
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DOI:
10.1016/s0306-4522(98)00328-5
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发表时间:
1999-03-01
期刊:
影响因子:
3.3
通讯作者:
Standaert, DG
中科院分区:
文献类型:
--
作者:
Albers, DS;Weiss, SW;Standaert, DG
Ionotropic glutamate receptors in the substantia nigra pars compacta regulate the activity of dopamine neurons. We have used dual-label immunofluoresence and confocal laser microscopy to study the localization of subunits of two types of ionotropic receptors within the substantia nigra pars compacta of the rat. Immunostaining for N-methyl-D-aspartate receptor 1 and glutamate receptor 2/3 was prominent in the soma and proximal dendrites of all tyrosine hydroxylase-immunopositive cells, while only low amounts of N-methyl-D-aspartate receptor 2A and N-methyl-D-aspartate receptor 2B were present. Selective antibodies were used to determine the isoforms of N-methyl-D-aspartate receptor 1 present. Immunostaining for the N1, C1 and C2 variably spliced segments of N-methyl-D-aspartate receptor 1 were scarce in the substantia nigra pars compacta, while immunoreactivity for the alternative C2' terminus of N-methyl-D-aspartate receptor 1 was quite abundant. Staining for glutamate receptor 1 was heterogeneous; about half of the tyrosine hydroxylase immunopositive cells stained intensely, while the other half were immunonegative. The glutamate receptor 1-stained cells were concentrated in the ventral tier of the substantia nigra pars compacta. Glutamate receptor 4 was nor found in tyrosine hydroxylase-immunopositive cells within the substantia nigra pars compacta.Together, these data demonstrate that dopaminergic neurons in the substantia nigra pars compacta express primarily glutamate receptor 1, glutamate receptor 2/3 and,N-methyl-D-aspartate receptor 1 isoforms containing the alternative C2' terminus. (C) 1998 IBRO. Published by Elsevier Science Ltd.