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[Binding of amaranthin in human retina]
F Uehara1, M Sameshima, K Unoki
1Department of Ophthalmology, Kagoshima University Faculty of Medicine.
Nippon Ganka Gakkai Zasshi
|March 1, 1995
Summary
Amaranthin binds to human retina photoreceptors, including cones and rods. This indicates the presence of specific sugar structures, Gal beta 1,3 GalNAc and sialic acid Gal beta 1,3 GalNAc, on these retinal cells.
Area of Science:
- Ophthalmology
- Glycobiology
- Neuroscience
Background:
- The human retina contains complex glycoconjugates crucial for photoreceptor function.
- Specific carbohydrate structures mediate cell-cell interactions and signaling in the retina.
Purpose of the Study:
- To investigate the binding of amaranthin to human retinal tissues.
- To identify the specific carbohydrate sequences recognized by amaranthin in the retina.
- To determine the distribution of these glycoconjugates on retinal cells.
Main Methods:
- Avidin biotinylated peroxidase complex method was used for detection.
- Amaranthin, a lectin specific for Gal beta 1,3 GalNAc and sialic acid Gal beta 1,3 GalNAc, was employed.
- Immunohistochemical staining of human retinal sections.
Main Results:
- Amaranthin demonstrated binding to cone and rod photoreceptors.
- Binding was also observed in the inner plexiform layer, ganglion cells, and nerve fibers.
- Peanut agglutinin, specific for Gal beta 1,3 GalNAc, selectively bound to cones.
Conclusions:
- O-glycoside-linked glycoconjugates are present on the surfaces of both cone and rod photoreceptors.
- Gal beta 1,3 GalNAc and sialic acid Gal beta 1,3 GalNAc are terminal sugars of these glycoconjugates on rods and cones, respectively.
- These findings contribute to understanding retinal cell surface composition and potential functions.