Specialization of the interphotoreceptor matrices around cone and rod photoreceptor cells in the monkey retina, as revealed by lectin cytochemistry.
The binding sites of two lectins, peanut agglutinin (PNA) and wheat germ agglutinin (WGA), in the interphotoreceptor matrix (IPM) and photoreceptor plasma membranes of the Japanese monkey (Macaca fuscata) retina were localized using a pre-embedding staining method with ferritin-conjugated (Fer) lectins as well as a postembedding staining method with fluorescence-labeled (FITC) lectins. FITC-PNA, but not WGA, stained cylindrical domains of the IPM around cone outer and inner segments, while the IPM around rods stained with FITC-WGA but not PNA. When the intact (not detached) retinal tissues were incubated with Fer-lectin, the lectin generally labeled neither the IPM nor photoreceptor plasma membranes, but labeled only those structures in detached portions occurring at the edges of occasional retinal tissue blocks. Thus, the neural retinas physically isolated from the retinal pigment epithelium (RPE) were utilized principally here. Ultrastructurally, the IPM in the intact retina consisted of granular and filamentous materials; the IPM in the isolated neutral retina also retained those components, although somewhat loosely organized, and the IPM around cones appeared to be preserved better than did the IPM around rods. Fer-PNA bound to the IPM associated with cones, but not rods; Fer-WGA bound to the rod- but not cone-associated IPM. The ferritin particles were found to lie close to the granular and filamentous materials. Those photoreceptor-associated IPMs extended to the apical surface of the RPE in detached portions or to the apical villi of the RPE which were frequently found in the isolated neural retinas. Also, Fer-PNA labeled the cone, but not rod, plasma membranes; Fer-WGA bound heavily to the plasma membranes of rod and cone outer segments, but sparsely to those of their inner segments. These results suggest that the IPM comprises chemically and physically differential domains specialized for cone and rod photoreceptor cells, and that these specialized IPM are structurally so stable that may be involved in isolating photoreceptor cells physicochemically from each other and in the interactions between the photoreceptors and the RPE, such as retinal adhesion.
Department of Ophthalmology, Faculty of Medicine, Kagoshima University, Japan.
M
M
Sameshima
F
F
Uehara
N
N
Ohba
D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000648:ultrastructure; D005109:Extracellular Matrix / Q000648:ultrastructure*; D005293:Ferritins / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*; D008251:Macaca; D008854:Microscopy, Electron; D019887:Peanut Agglutinin; D010786:Photoreceptor Cells / Q000648:ultrastructure*; D010857:Pigment Epithelium of Eye / Q000648:ultrastructure; D014909:Wheat Germ Agglutinins / Q000378:metabolism
D037102:Lectins; D019887:Peanut Agglutinin; D014909:Wheat Germ Agglutinins; D005293:Ferritins