Inhibition of human cytosolic phospholipase A2 by human annexin V
نویسندگان
چکیده
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 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 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 کاملModulation of human type II secretory phospholipase A2 by sphingomyelin and annexin VI.
Conjectural results have been reported on the capacity of inflammatory secreted phospholipase A2 (sPLA2) to hydrolyse mammalian membrane phospholipids. Development of an assay based on the release of non-esterified fatty acids by the enzyme acting on the organized phospholipid mixture constituting the membrane matrix has led to the identification of two prominent effectors, sphingomyelin (SPH) ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1998
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3290369