Research articles

Surfactant protein A (SP-A) binds to phosphatidylserine and competes with annexin V binding on late apoptotic cells

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  • 1.Department of Pharmacology, University of Oxford, Mansfield Road, Oxford OX1 3QT, UK; 2.MRC Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; 3.University of Southampton, MP 803 Level F, South Block, Southampton General Hospital, Southampton SO16 6YD, UK;

Published date: 01 Feb 2010

Abstract

The role of surfactant protein A (SP-A) in the recognition and clearance of apoptotic cells is well established, but to date, it is still not clear which surface molecules of apoptotic cells are involved in the process. Here we present evidence that phosphatidylserine (PS) is a relevant binding molecule for human SP-A. The binding is Ca2+-dependent and is not inhibited by mannose, suggesting that the sugar-binding site of the carbohydrate recognition domain (CRD) of SP-A is not involved. Flow cytometry studies on apoptotic Jurkat cells revealed apparent inhibition of annexin V binding by increasing concentrations of SP-A in late apoptotic but not early apoptotic cells, and this was consistent for Jurkat cells and neutrophils. Supporting these data, confocal microscopy results show a co-localisation of annexin V and SP-A in late apoptotic but not early apoptotic cells. However, we cannot conclude that this inhibition is exclusively due to the binding of SP-A to PS on the cell surface, as annexin V is not wholly specific for PS and SP-A also interacts with other phospholipids that might become exposed on the apoptotic cell surface.

Cite this article

Anne Jäkel, Kenneth B. M. Reid, Howard Clark, . Surfactant protein A (SP-A) binds to phosphatidylserine and competes with annexin V binding on late apoptotic cells[J]. Protein & Cell, 2010 , 1(2) : 188 -197 . DOI: 10.1007/s13238-010-0024-z

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