Macrophage and Retinal Pigment Epithelium Phagocytosis

Macrophage and Retinal Pigment Epithelium Phagocytosis Noninflammatory monocyte macrophages use αvβ3 integrin to selectively bind apoptotic cells, initiating their phagocytic removal. In a related process, the retinal pigment epithelium (RPE) employs αvβ5 integrin to recognize spent photoreceptor outer segment particles (OS). Here, we show that apoptotic cells and OS compete for binding to these receptors, indicating that OS and apoptotic cells expose surface signals recognizable by αvβ3 and αvβ5. Particle binding to αvβ5 required protein kinase C (PKC) activation. In RPE, αvβ5 binding was maximally activated even before any phagocytic challenge and was reduced by PKC inhibitors. In macrophages, it was dormant but became activated upon PKC stimulation. PKC-activated αvβ5-mediated binding in macrophages differed from constitutive binding to the same integrin receptor in RPE cells in that the former followed much faster kinetics, similar to particle binding mediated by αvβ3. Activation of αvβ5 for particle binding correlated with its recruitment into a detergent-insoluble fraction, a process sensitive to pharmacological modulation of PKC in both types of phagocytes. Furthermore, αvβ5 but not αvβ3 particle binding required actin microfilaments. These data constitute the first evidence that noninflammatory phagocytes actively regulate the earliest phase of phagocytic clearance, particle binding, by controlling receptor activity. phagocytosis recognition integrins macrophages retinal pigment epithelium Footnotes 1used in this paper: Cyt D, cytochalasin D; OS, outer segment particle(s); PKC, protein kinase C; RPE, retinal pigment epithelium; TUNEL, terminal deoxynucleotidyl transferase–mediated dUTP nick end labeling Submitted: 7 May 1999 Revision requested 21 July 1999 Accepted: 26 July 1999 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Experimental Medicine Rockefeller University Press

Macrophage and Retinal Pigment Epithelium Phagocytosis

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Publisher
Rockefeller University Press
Copyright
© 1999 The Rockefeller University Press
ISSN
0022-1007
eISSN
1540-9538
D.O.I.
10.1084/jem.190.6.861
Publisher site
See Article on Publisher Site

Abstract

Noninflammatory monocyte macrophages use αvβ3 integrin to selectively bind apoptotic cells, initiating their phagocytic removal. In a related process, the retinal pigment epithelium (RPE) employs αvβ5 integrin to recognize spent photoreceptor outer segment particles (OS). Here, we show that apoptotic cells and OS compete for binding to these receptors, indicating that OS and apoptotic cells expose surface signals recognizable by αvβ3 and αvβ5. Particle binding to αvβ5 required protein kinase C (PKC) activation. In RPE, αvβ5 binding was maximally activated even before any phagocytic challenge and was reduced by PKC inhibitors. In macrophages, it was dormant but became activated upon PKC stimulation. PKC-activated αvβ5-mediated binding in macrophages differed from constitutive binding to the same integrin receptor in RPE cells in that the former followed much faster kinetics, similar to particle binding mediated by αvβ3. Activation of αvβ5 for particle binding correlated with its recruitment into a detergent-insoluble fraction, a process sensitive to pharmacological modulation of PKC in both types of phagocytes. Furthermore, αvβ5 but not αvβ3 particle binding required actin microfilaments. These data constitute the first evidence that noninflammatory phagocytes actively regulate the earliest phase of phagocytic clearance, particle binding, by controlling receptor activity. phagocytosis recognition integrins macrophages retinal pigment epithelium Footnotes 1used in this paper: Cyt D, cytochalasin D; OS, outer segment particle(s); PKC, protein kinase C; RPE, retinal pigment epithelium; TUNEL, terminal deoxynucleotidyl transferase–mediated dUTP nick end labeling Submitted: 7 May 1999 Revision requested 21 July 1999 Accepted: 26 July 1999

Journal

The Journal of Experimental MedicineRockefeller University Press

Published: Sep 20, 1999

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