Natural, high-mannose glycoproteins inhibit ROS binding and ingestion by RPE cell cultures.

Abstract:

:Previous studies have suggested that a mannose receptor mediates the phagocytic uptake of effete rod outer segments by retinal pigment epithelial cells. In the present study, the effect of adding a soluble ligand for the mannose receptor, horseradish peroxidase, was examined. Cultured retinal pigment epithelial cells from Long Evans rats were preincubated with various concentrations of horseradish peroxidase for 20 min followed by a challenge of FITC-labeled bovine rod outer segments for 3 h. Both counts of total rod outer segments (bound and ingested) and ingested rod outer segments were determined. Rod outer segment uptake was reduced, in a concentration-dependent fashion, by an average of 60% of control values when horseradish peroxidase was added to retinal pigment epithelial cultures. Similarly, total rod outer segment values were reduced to 50% of controls in the presence of at least a 10 micrograms ml-1 horseradish peroxidase concentration. Horseradish peroxidase inhibition of retinal pigment epithelial phagocytic capacity was reversible. Other high mannose glycoproteins, such as invertase, beta-glucoronidase, and ovalbumin, were equally effective in preventing rod outer segment ingestion by retinal pigment epithelial cells. These data further support the hypothesis that a mannose receptor on the retinal pigment epithelial apical surface facilitates phagocytosis of rod outer segments.

journal_name

Exp Eye Res

authors

Lutz DA,Guo Y,McLaughlin BJ

doi

10.1016/s0014-4835(05)80144-7

subject

Has Abstract

pub_date

1995-10-01 00:00:00

pages

487-93

issue

4

eissn

0014-4835

issn

1096-0007

journal_volume

61

pub_type

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