Essential role for MFG-E8 as ligand for alphavbeta5 integrin in diurnal retinal phagocytosis.

ABSTRACT: The integrin receptor alphavbeta5 controls two independent forms of interactions of the retinal pigment epithelium (RPE) with adjacent photoreceptor outer segments that are essential for vision. Alphavbeta5 localizes specifically to apical microvilli of the RPE and contributes to retinal adhesion that maintains RPE contacts with intact outer segments at all times. Additionally, alphavbeta5 synchronizes diurnal bursts of RPE phagocytosis that clear photoreceptor outer segment fragments (POS) shed in a circadian rhythm. Dependence of retinal phagocytosis and adhesion on alphavbeta5 receptors suggests that the extracellular matrix ensheathing RPE microvilli contains ligands for this integrin. Here we studied mice lacking expression of functional MFG-E8 to test the contribution of this integri

SUBMITTER: Nandrot EF 

PROVIDER: S-EPMC1924559 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature