Catalytic and non-catalytic functions of human IIA phospholipase A2
Catalytic and non-catalytic functions of human IIA phospholipase A2
Group IIA phospholipase A2 (PLA2) is a low-molecular-mass secreted PLA2 enzyme that has been identified as an acute phase protein with a role in the inflammatory response to infection and trauma. The protein is possibly unique in being highly cationic and having a global distribution of surface arginine and lysine residues. This structure supports two functions of the protein. (1) An anti-bacterial role where the enzyme is targeted to the anionic cell membrane of Gram-positive bacteria and phospholipid hydrolysis assists in bacterial killing. (2) A proposed non-catalytic role in which the protein forms supramolecular aggregates with anionic phospholipid vesicles or debris. These aggregates are then internalized via interactions with cell surface heparin sulphate proteoglycans and macropinocytosis for disposal by macrophages.
28-35
Birts, Charles N.
8689ddad-ba47-4ca6-82c5-001315dbd250
Barton, C. Howard
5dfb4e1a-d559-4b58-9036-31de1e6c9ad8
Wilton, David C.
4b995f66-ad6c-4d96-9179-c64f3b54466a
2010
Birts, Charles N.
8689ddad-ba47-4ca6-82c5-001315dbd250
Barton, C. Howard
5dfb4e1a-d559-4b58-9036-31de1e6c9ad8
Wilton, David C.
4b995f66-ad6c-4d96-9179-c64f3b54466a
Birts, Charles N., Barton, C. Howard and Wilton, David C.
(2010)
Catalytic and non-catalytic functions of human IIA phospholipase A2.
Trends in Biochemical Sciences, 35 (1), .
(doi:10.1016/j.tibs.2009.08.003).
Abstract
Group IIA phospholipase A2 (PLA2) is a low-molecular-mass secreted PLA2 enzyme that has been identified as an acute phase protein with a role in the inflammatory response to infection and trauma. The protein is possibly unique in being highly cationic and having a global distribution of surface arginine and lysine residues. This structure supports two functions of the protein. (1) An anti-bacterial role where the enzyme is targeted to the anionic cell membrane of Gram-positive bacteria and phospholipid hydrolysis assists in bacterial killing. (2) A proposed non-catalytic role in which the protein forms supramolecular aggregates with anionic phospholipid vesicles or debris. These aggregates are then internalized via interactions with cell surface heparin sulphate proteoglycans and macropinocytosis for disposal by macrophages.
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Published date: 2010
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Local EPrints ID: 156557
URI: http://eprints.soton.ac.uk/id/eprint/156557
PURE UUID: 4fc267d4-e4e5-47ec-bdb4-61ea3d482474
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Date deposited: 01 Jun 2010 10:44
Last modified: 14 Mar 2024 02:47
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