Retinal Insulin Receptor Research Articles

Retinal insulin receptors: localization using a polyclonal anti-insulin receptor antibody

Although retinal insulin receptors have recently been described biochemically, the location of these receptors within the retina is unknown. The study presented here used a polyclonal anti-insulin receptor antibody (B10), immunofluorescence and immunoelectron microscopy to determine the location of insulin receptors in bovine, monkey and human retina. It was found that antibody immunofluorescence formed discrete bands localized predominantly to photoreceptor and neuronal cell bodies. In addition to the strong association with neuronal perikarya, a lower level of antibody binding was observed in photoreceptor outer segments. In human retina, some of the antibody immunofluorescence also had a pattern that suggested B 10 binding to glial-like cells.

Retinal insulin receptors. 2. Characterization and insulininduced tyrosine kinase activity in bovine retinal rod outer segments

Bovine retinal rod outer segments (ROS) possess specific, high-affinity receptors for insulin. These receptors exhibit an insulin-stimulatable tyrosine-specific activity that is capable of phosphorylating the receptor's own beta-subunit and exogenous substrate. ROS insulin receptors exhibit heterogeneity in the apparent molecular weight of the receptor's alpha-subunit. In this regard, insulin receptors from this single cell type resemble insulin receptors obtained from whole retina, but are unlike receptors from brain and liver.

Retinal insulin receptors. 1. Structural heterogeneity and functional characterization

Neural cells of the bovine retina contain specific, high-affinity receptors for insulin. When solubilized and wheat-germ purified, these receptors exhibit a kinase activity that is capable of phosphorylating the receptor's beta-subunit (autophosphorylation) and a tyrosine-containing exogenous substrate, poly (Glu, Tyr) 4:1. Studies of the structure of retinal insulin receptors revealed the existence of two insulin receptor subpopulations. For these populations, the apparent molecular weights of the alpha-subunit were 120- and 133 kDa. This structural heterogeneity does not appear to be related to the presence of vascular contamination and stands in contrast to the brain and liver where a single alpha-subunit type was found (120 kDa for brain and 133 kDa for liver). In addition to being distinguishable by their molecular weights, the two populations of retinal insulin receptors could be distinguished in terms of (a) their solubility in Triton X-100, (b) glycosylation, and (c) recognition by anti-insulin receptor antibody. Despite these structural differences, the two populations of retinal insulin receptors appear to have similar insulin binding affinities.