[Lectin binding in the interphotoreceptor matrix in neuraminidase-induced retinal detachment].
Binding sites of fluorescence isocyanate-labeled lectins, peanut agglutinin (PNA) and Ricinus communis agglutinin-1 (RCA-1), were studied in the interphotoreceptor matrix (IPM) of adult rat retinas that were pretreated with an intravitreous injection of neuroaminidase. The localization of binding sites to the subretinal IPM differed significantly between the two lectins. PNA bound to the subretinal IPM components in a cord-like fashion that formed a bridge between the apical photoreceptor outer segments and the surface of the RPE. On the other hand, RCA-1 showed homogeneously prominent binding to the subretinal space IPM, the intensity of which appeared to inversely correlate with the extent of neuraminidase-induced retinal separation. The results suggest that the IPM may consist of mucin-type glycoconjugates as recognized by PNA and serum-type ones as bound by RCA-1, and that these IPM components may play different roles in the maintenance and organization of photoreceptor-RPE complex, e.g. the mucin-type for the retinal adhesion and the serum-type for the transport of metabolites.
Uehara
F
F
Department of Ophthalmology, Kagoshima University Faculty of Medicine, Japan.
Ohba
N
N
Yasumura
D
D
La Vail
M M
MM
D000818:Animals; D001665:Binding Sites; D005109:Extracellular Matrix / Q000378:metabolism; D037102:Lectins / Q000378:metabolism*; D009439:Neuraminidase; D010786:Photoreceptor Cells / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012163:Retinal Detachment / Q000139:chemically induced / Q000378:metabolism*
D037102:Lectins; D009439:Neuraminidase