Aleuria lectin remains bound to its receptors during rapid axonal transport in retinal ganglion cells

Neurochem Int. 1989;15(2):185-9. doi: 10.1016/0197-0186(89)90099-5.

Abstract

Plasma membrane glycoproteins responsible for adsorptive endocytosis and fast axonal transport of Aleuria lectin in the rabbit retina were purified. Following vitreal injections of Aleuria lectin, the lectin together with its endogenous receptors, were isolated from the retina by immunoaffinity chromatography on anti-Aleuria lectin antibodies. It was found that a high molecular weight (?320 kDa), membrane-bound, fucosylated polypeptide was the principal receptor for Aleuria lectin in the retina. Using the same experimental technique, glycoproteins carrying Aleuria lectin from the retina to the optic nerve terminals were isolated from the optic nerves and lateral geniculate bodies. It was shown that the Aleuria lectin remained bound to its principal retinal receptor during rapid axonal transport. The results suggest that there may exist a pathway where intrinsic glycoproteins of the retinal plasma membrane may be routed to the axonal and synaptic compartments of the retinal ganglion cell.