Purchase this article with an account.
J. Liu, A.H. Milam, A. Fernandez, K.T. Keyser, J.M. Lindstrom, R.A. Stone; Localization of Nicotinic Acetylcholine Receptor Subunits in Rhesus Monkey Retina . Invest. Ophthalmol. Vis. Sci. 2003;44(13):5179.
Download citation file:
© ARVO (1962-2015); The Authors (2016-present)
Purpose: Nicotinic acetylcholine receptors (AChRs) mediate many effects of acetylcholine in the vertebrate retina. Each of the known AChR subtypes is composed of five subunits that form an acetylcholine-gated cation channel. We localized the α3 and ß2 subunits of the AChRs in rhesus monkey retina. Methods: Six post mortem eyes from four rhesus monkeys were immersion-fixed for 2-4 hrs in 2% paraformaldehyde or periodate-lysine-paraformaldehyde. Cryostat tissue sections were studied by indirect immunofluorescence, using well-characterized monoclonal antibodies to the α3 (mAbs 210 and 35) or ß2 (mAb 295 and 290) subunits of AChRs. Results: Antibodies to the α3 subunit labeled a few cells of at least two different sizes in the ganglion cell layer, many inner nuclear layer cells that distribute mostly within the innermost one or two tiers, and many cones. Two fiber bands within the inner plexiform layer also were intensely immunoreactive for the α3 subunit. The ß2 subunit was detected in many presumed ganglion cells in the ganglion cell layer but only a few cells in the inner nuclear layer. ß2 antibodies labeled two intense bands in the inner plexiform layer. The nerve fiber layer also showed strong ß2 labeling, with intense immunoreactivity terminating abruptly near the posterior margin of the lamina cribrosa. Conclusions: Rhesus monkey retina expresses both α3 and ß2 subunits of AChRs. Comparison of the labeling patterns suggests that some neurons of the primate retina could co-express the α3 and ß2 subunits within a single AChR subtype. The differences in distributions of the α3 and ß2 subunits, however, indicate that other α and ß subunits also contribute to the formation of AChRs in primate retina.
This PDF is available to Subscribers Only