Calretinin co-localizes with the NMDA receptor subunit NR1 in cholinergic amacrine cells of the rat retina.
Immunohistochemistry was used to verify whether choline-acetiltransferase colocalizes with calcium-binding proteins and NMDA receptor subunit NR1 in the rat retina. Whereas calbindin and parvalbumin were not observed in cholinergic amacrine cells, calretinin and NR1 were very frequently colocalized with ChAT. Calretinin/NR1-positive cells were also shown, suggesting that calretinin in cholinergic cells of the rat may be related to the buffering of excess intracellular calcium generated by activation of NMDA receptors.
Araki
C M
CM
Department of Histology and Embryology, Institute of Biomedical Sciences, University of São Paulo, Av. Prof. Lineu Prestes 1524, SP 05508-900, São Paulo, Brazil.
Hamassaki-Britto
D E
DE
D000109:Acetylcholine / Q000378:metabolism*; D000818:Animals; D064032:Calbindin 2; D064026:Calbindins; D002795:Choline O-Acetyltransferase / Q000378:metabolism; D009474:Neurons / Q000166:cytology* / Q000378:metabolism*; D010320:Parvalbumins / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D016194:Receptors, N-Methyl-D-Aspartate / Q000378:metabolism*; D012160:Retina / Q000166:cytology* / Q000378:metabolism*; D064030:S100 Calcium Binding Protein G / Q000378:metabolism*
D000109:Acetylcholine; D064032:Calbindin 2; D064026:Calbindins; D002795:Choline O-Acetyltransferase; D010320:Parvalbumins; D016194:Receptors, N-Methyl-D-Aspartate; D064030:S100 Calcium Binding Protein G; C576512:Calb2 protein, rat