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Glycoconjugates in exfoliation syndrome A lectin histochemical study of the ciliary body and lens
Author(s) -
Hietanen Jaana,
Tarkkanen Ahti
Publication year - 1989
Publication title -
acta ophthalmologica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.534
H-Index - 87
eISSN - 1755-3768
pISSN - 1755-375X
DOI - 10.1111/j.1755-3768.1989.tb01873.x
Subject(s) - glycoconjugate , lectin , lamella (surface anatomy) , canavalia ensiformis , lens (geology) , ciliary body , biology , chemistry , anatomy , biochemistry , paleontology , neuroscience
The binding of ten biotin‐coupled lectins with different carbohydrate specifities to exfoliative material and neighbouring tissues was studied in 16 formalin‐fixed and paraffin‐embedded human eyes. Eight of the eyes were exfoliation positive while the rest were exfoliation negative. Exfoliatve material reacted intensely with Lens culinaris (LCA), Canavalia ensiformis (ConA) and Ricinus communis (RCA‐I) agglutinins. Positive reaction was also seen with wheat germ (WGA), peanut (PNA) and soybean (SBA) agglutinins. The superficial zonular lamella, zonular fibers and the non‐pigmented epithelium of the ciliary body had a rather similar lectin‐binding profile to exfoliative material. The lens capsule was essentially unreactive with all the lectins used. The lens epithelium reacted faintly with ConA, LCA, WGA and RCA‐I. Pre‐treatment with neuraminidase to remove sialic acid resulted in increased binding of PNA and SBA to exfoliative material, zonular fibers and the zonular lamella, and in decreased binding of WGA to the non‐pigmented epithelium of the ciliary body, zonular fibers and the zonular lamella. The results indicate that α‐mannosyl, β‐galactosyl, N‐acetyl‐D‐glucosaminyl and N‐acetylneuaraminic acid residues are present in glycoconjugates of exfoliative material and neighbouring tissues.