منابع مشابه
Inhibition of human cytosolic phospholipase A2 by human annexin V.
The ability of annexins, particularly annexin 1 (lipocortin 1), to inhibit phospholipase A2 (PLA2) is well known and a substrate depletion mechanism is now widely accepted as the explanation for most inhibitory studies. However, there are only a very limited number of reported studies involving annexins and the high-molecular-mass cytosolic PLA2 (cPLA2). In this study we have examined the effec...
متن کاملRegulation of cytosolic phospholipase A2 by phosphorylation.
Introduction Phospholipases catalyse the cleavage of membrane phospholipids and thereby generate second messengers that participate in intracellular signal transduction processes or act as precursors of tissue hormones. Cytosolic phospholipase Az (cPLA2) is an 85 kDa enzyme that cleaves arachidonic acid at the sn-2 position of the phospholipid [1,2]. The intracellular location of the enzyme ena...
متن کاملInhibition of phospholipase A2.
Phospholipases A2 are involved in inflammatory processes such as the liberation of free arachidonic acid from the membrane pool for the biosynthesis of eicosanoids. Inhibitors of these enzymes are proving useful in determining the biological roles of phospholipases A2 in complex cellular processes and may also have therapeutic potential. Inhibition of these lipolytic enzymes is more difficult t...
متن کاملInvolvement of cytosolic phospholipase A2 and secretory phospholipase A2 in arachidonic acid release from human neutrophils.
The purpose of this study was to define the role of secretory phospholipase A2 (sPLA2), calcium-independent PLA2, and cytosolic PLA2 (cPLA2) in arachidonic acid (AA) release from fMLP-stimulated human neutrophils. While fMLP induced the release of extracellular sPLA2 activity and AA, 70% of sPLA2 activity remained associated with the cell. Treatment with the cell-impermeable sPLA2 inhibitors DT...
متن کاملArachidonate release and prostaglandin production by group IVC phospholipase A2 (cytosolic phospholipase A2gamma).
While the role of the group IVA Ca(2+)-dependent cytosolic phospholipase A(2)alpha (cPLA(2)alpha) in arachidonic acid (AA) metabolism has been well documented, that of its paralogue, Ca(2+)-independent group IVC PLA(2) (cPLA(2)gamma), has remained uncertain. Here we show, using a transfection strategy, that cPLA(2)gamma has the ability to increase the spontaneous and stimulus-induced release of...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m009905200