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Biological effects of group IIA secreted phosholipase A 2
Author(s) -
Fuentes Lucı́a,
Hernández Marita,
Nieto Marı́a Luisa,
Sánchez Crespo Mariano
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03401-4
Subject(s) - biochemistry , versican , chemistry , chondroitin sulfate , decorin , receptor , phospholipase a2 , proteoglycan , phospholipase , phospholipase c , intracellular , dermatan sulfate , microbiology and biotechnology , biology , glycosaminoglycan , enzyme , extracellular matrix
Group IIA secreted phospholipase A 2 (sPLA 2 ‐IIA) is the most abundant element in human tissues of a large family of low molecular weight phospholipases A 2 , which shows properties different from those displayed by the cytosolic phospholipase A 2 involved in the release of arachidonic acid. sPLA 2 ‐IIA behaves as a ligand for a group of receptors inside the C‐type multilectin mannose receptor family and also interacts with heparan sulfate proteoglycans such as glypican, the dermatan/chondroitin sulfate‐rich decorin, and the chondroitin sulfate‐rich versican, thus being able to internalize to specific compartments within the cell and producing biological responses. This review provides a short summary of the biological actions of sPLA 2 ‐IIA on intracellular signaling pathways.