Surfactant protein A (SP-A) binds to phosphatidylserine and competes with annexin V binding on late apoptotic cells
Surfactant protein A (SP-A) binds to phosphatidylserine and competes with annexin V binding on late apoptotic cells
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.
surfactant proteins, phosphatidylserine, apoptotic cells
188-197
Jäkel, Anne
c9ee0d55-1b38-4eeb-8afd-f65633ce6d16
Reid, Kenneth B. M.
67b83320-96f6-41d0-ab1d-99430f39f904
Clark, Howard
70550b6d-3bd7-47c6-8c02-4f43f37d5213
February 2010
Jäkel, Anne
c9ee0d55-1b38-4eeb-8afd-f65633ce6d16
Reid, Kenneth B. M.
67b83320-96f6-41d0-ab1d-99430f39f904
Clark, Howard
70550b6d-3bd7-47c6-8c02-4f43f37d5213
Jäkel, Anne, Reid, Kenneth B. M. and Clark, Howard
(2010)
Surfactant protein A (SP-A) binds to phosphatidylserine and competes with annexin V binding on late apoptotic cells.
Protein & Cell, 1 (2), .
(doi:10.1007/s13238-010-0024-z).
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.
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Published date: February 2010
Keywords:
surfactant proteins, phosphatidylserine, apoptotic cells
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Local EPrints ID: 158121
URI: http://eprints.soton.ac.uk/id/eprint/158121
ISSN: 1674-800X
PURE UUID: c397c32f-8afb-4d38-83ce-8ee6390e25a7
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Date deposited: 15 Jun 2010 13:12
Last modified: 14 Mar 2024 01:49
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Author:
Anne Jäkel
Author:
Kenneth B. M. Reid
Author:
Howard Clark
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