Regulatory Mechanism and Physiological Role of Cytosolic Phospholipase A2
نویسندگان
چکیده
منابع مشابه
Cytosolic phospholipase A₂: physiological function and role in disease.
The group IV phospholipase A2 (PLA2) family is comprised of six intracellular enzymes (GIVA, -B, -C, -D, -E, and -F) commonly referred to as cytosolic PLA2 (cPLA2)α, -β, -γ, -δ, -ε, and -ζ. They contain a Ser-Asp catalytic dyad and all except cPLA2γ have a C2 domain, but differences in their catalytic activities and subcellular localization suggest unique regulation and function. With the excep...
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 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 arachidonic acid release and cytosolic phospholipase A2 activation.
The 85-kDa cytosolic PLA2 (cPLA2) mediates agonist-induced arachidonic acid release in many cell models, including mouse peritoneal macrophages. cPLA2 is regulated by an increase in intracellular calcium, which binds to an amino-terminal C2 domain and induces its translocation to the nuclear envelope and endoplasmic reticulum. Phosphorylation of cPLA2 on S505 by mitogen-activated protein kinase...
متن کاملSuicide inhibition of canine myocardial cytosolic calcium-independent phospholipase A2. Mechanism-based discrimination between calcium-dependent and -independent phospholipases A2.
The majority of phospholipase A2 activity in myocardium is calcium-independent and selective for hydrolysis of plasmalogen substrate (Wolf, R. A., and Gross, R. W. (1985) J. Biol. Chem. 260, 7295-7303; Hazen, S. L., Stuppy, R. J., and Gross, R. W. (1990) J. Biol. Chem. 265, 10622-10630). Accordingly, identification of an inhibitor which selectively targets calcium-independent phospholipases A2 ...
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ژورنال
عنوان ژورنال: Biological and Pharmaceutical Bulletin
سال: 2004
ISSN: 0918-6158,1347-5215
DOI: 10.1248/bpb.27.1168