1. Co-localization of carnosine and glutamate in photoreceptors and bipolar cells of the frog retina
- Author
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Patrizia Panzanelli, Dario Cantino, and Marco Sassoè-Pognetto
- Subjects
Immunocytochemistry ,Glutamic Acid ,Carnosine ,Neurotransmission ,Biology ,Retina ,chemistry.chemical_compound ,medicine ,Animals ,Photoreceptor Cells ,Axon ,Neurotransmitter ,Molecular Biology ,General Neuroscience ,Glutamate receptor ,Rana esculenta ,Inner plexiform layer ,Immunohistochemistry ,Microscopy, Electron ,medicine.anatomical_structure ,chemistry ,Biochemistry ,Biophysics ,sense organs ,Neurology (clinical) ,Developmental Biology - Abstract
Immunocytochemical methods were used to visualize carnosine (β-alanyl- l -histidine)-like immunoreactivity (-LI) in the frog retina and to compare its localization with that of glutamate. Carnosine-LI was conspicuous in photoreceptors and bipolar cells. The axon terminals of labelled bipolar cells formed five bands in the inner plexiform layer. A few presumed amacrine and ganglion cells, as well as Muller cell endfeet, were also labelled. Post-embedding immunocytochemistry revealed particularly high levels of glutamate-LI in the synaptic axon terminals of bipolar cells, with a mean gold particle density 5 × higher than that of amacrine cells. Photoreceptor terminals were also labelled, but with a labelling intensity about half that of bipolar cells. Labelling of serial semithin sections showed co-localization of carnosine and glutamate in photoreceptors and bipolar cells. These findings are consistent with the notion that glutamate is the neurotransmitter of neuronal elements that transfer information vertically through the retina. We propose that carnosine may modulate GABA and/or glutamate receptors by virtue of its ability to chelate Zn 2+ and other ions.
- Published
- 1997