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Rod and cone specific domains in the interphotoreceptor matrix
Author(s) -
Mieziewska Kristina E.,
van Veen Theo,
Murray John M.,
Aguirre Gustavo D.
Publication year - 1991
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/cne.903080305
Subject(s) - wheat germ agglutinin , lectin , peanut agglutinin , biology , matrix (chemical analysis) , biophysics , anatomy , microbiology and biotechnology , chemistry , chromatography
The insoluble matrix domain of the interphotoreceptor matrix (IPM) from normal dog, cat, and mouse retinae were characterized using lectin cytochemistry. The lectins WGA (wheat germ agglutinin) and PNA (peanut agglutinin) were used to label interphotoreceptor matrix microdomains in cryosections of retinal tissue and in extracted insoluble matrix. Retinal cryosections and extracted matrix were examined by epifluorescence microscopy and scanning confocal laser microscopy, the latter allowed for the removal of all background fluorescence and gave increased resolution. The insoluble matrix was extracted as a continuous sheet that was comprised of two photoreceptor‐specific matrix domains distinguished both by the size of the domains, and by differential binding of WGA and PNA lectins. Each domain encloses a photoreceptor inner and outer segment. Individual rod‐associated domains were connected into a hexagonal lattice and this pattern was regularly interrupted by the larger cone‐associated domains which have 8–10 surrounding rod domains. The PNA lectin primarily labeled the cone‐associated matrix with faint binding to the rod matrix; the WGA lectin labeled both the rod‐ and cone‐associated matrix.