Transient expression of NADPH-diaphorase in the lateral geniculate nucleus of the ferret during early postnatal development.
Retinogeniculate projections in the ferret are refined during postnatal development so that inputs from the two eyes become segregated into eye-specific laminae, and each eye-specific lamina is further divided into sublaminae containing inputs from on-center or off-center afferents. Segregation into eye-specific laminae and on/off sublaminae is dependent on neuronal activity; sublamination depends on activation of N-methyl-d-aspartate (NMDA) receptors. By analogy with the suggested role of nitric oxide in NMDA-mediated long-term potentiation in the hippocampus, we investigated a possible role for nitric oxide in ferret retinogeniculate development. The expression of NADPH-diaphorase, a nitric oxide synthase, was examined histologically in the lateral geniculate nucleus of ferrets at several postnatal ages. At birth, neuropil is labeled in the nucleus, although no cell bodies are visible. After the first postnatal week, some labeled cells appear, predominantly in the C laminae. By three postnatal weeks, cell bodies are clearly labeled in all geniculate laminae. Staining reaches a peak in density at about four postnatal weeks, then declines such that by six postnatal weeks labeled cells are no longer visible. This transient expression of NADPH-diaphorase activity is consistent with a role for nitric oxide in the development of mature connections within the ferret lateral geniculate nucleus.
Cramer
K S
KS
Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge 02139, USA.
Moore
C I
CI
Sur
M
M
D000818:Animals; D000831:Animals, Newborn; D005289:Ferrets / Q000254:growth & development / Q000378:metabolism*; D005829:Geniculate Bodies / Q000201:enzymology* / Q000254:growth & development; D009252:NADPH Dehydrogenase / Q000096:biosynthesis*; D012160:Retina / Q000502:physiology; D013997:Time Factors; D014795:Visual Pathways / Q000502:physiology
D009252:NADPH Dehydrogenase