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Journal of Histochemistry and Cytochemistry, Vol. 47, 1533-1540, December 1999, Copyright © 1999, The Histochemical Society, Inc.

ARTICLE

Human Ocular Drusen Possess Novel Core Domains with a Distinct Carbohydrate Composition

Robert F. Mullinsa and Gregory S. Hagemana
a The University of Iowa Center for Macular Degeneration, Department of Ophthalmology and Visual Sciences, The University of Iowa, Iowa City, Iowa

Correspondence to: Gregory S. Hageman, Dept. of Ophthalmology and Visual Sciences, U. of Iowa, 11190E PFP, 200 Hawkins Drive, Iowa City, IA 52240.

Ocular drusen are extracellular deposits that form between the retinal pigmented epithelium (RPE) and Bruch's membrane. Although the presence of large and/or numerous drusen in the macula is a significant risk factor for development of age-related macular degeneration (AMD), a major cause of irreversible blindness, little is known about their origin or composition. We have expanded on our previous investigations related to drusen-associated glycoconjugates by examining lectin binding patterns after removal of terminal sialic acid residues. Strikingly, intense and distinct labeling of drusen subdomains is revealed by Arachea hypogea agglutinin (PNA) after neuraminidase treatment. PNA binding is confined to discrete domains within both hard and soft drusen. These "cores" are positioned centrally within drusen and are typically juxtaposed to Bruch's membrane. Only one core per druse is observed. PNA labeling of drusen cores does not co-localize with associated lipids and is abrogated by digestion with O-glycosidase but not N-glycosidase. The association of cores with small drusen suggests that they may participate in drusen biogenesis. (J Histochem Cytochem 47:1533–1539, 1999)

Key Words: macular degeneration, drusen, glycoconjugates, lectins, peanut agglutinin


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