Domain-induced activation of human phospholipase A2 type IIA: local versus global lipid composition

Secretory human phospholipase A2 type IIA (PLA2-IIA) catalyzes the hydrolysis of the sn-2 ester bond in glycerolipids to produce fatty acids and lysolipids. The enzyme is coupled to the inflammatory response, and its specificity toward anionic membrane interfaces suggests a role as a bactericidal ag...

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Veröffentlicht in:	Biophysical journal 2006-05, Vol.90 (9), p.3165-3175
Hauptverfasser:	Leidy, Chad, Linderoth, Lars, Andresen, Thomas L, Mouritsen, Ole G, Jørgensen, Kent, Peters, Günther H
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Calorimetry, Differential Scanning Fluoresceins Group II Phospholipases A2 Humans Lipid Metabolism - physiology Lipids - chemistry Membrane Microdomains - chemistry Membrane Microdomains - metabolism Membranes Phosphatidylcholines - chemistry Phosphatidylcholines - metabolism Phosphatidylglycerols - chemistry Phosphatidylglycerols - metabolism Phospholipases A - chemistry Phospholipases A - metabolism Phospholipases A2 Protein Structure, Tertiary Snake Venoms - enzymology Snakes - physiology
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