Document Detail

Differences between group X and group V secretory phospholipase A(2) in lipolytic modification of lipoproteins.
MedLine Citation:
PMID:  22706677     Owner:  NLM     Status:  MEDLINE    
Secretory phospholipases A(2) (sPLA(2)s) are a diverse family of low molecular mass enzymes (13-18 kDa) that hydrolyze the sn-2 fatty acid ester bond of glycerophospholipids to produce free fatty acids and lysophospholipids. We have previously shown that group X sPLA(2) (sPLA(2)-X) had a strong hydrolyzing activity toward phosphatidylcholine in low-density lipoprotein (LDL) linked to the formation of lipid droplets in the cytoplasm of macrophages. Here, we show that group V sPLA(2) (sPLA(2)-V) can also cause the lipolysis of LDL, but its action differs remarkably from that of sPLA(2)-X in several respects. Although sPLA(2)-V released almost the same amount of fatty acids from LDL, it released more linoleic acid and less arachidonic acid than sPLA(2)-X. In addition, the requirement of Ca(2+) for the lipolysis of LDL was about 10-fold higher for sPLA(2)-V than sPLA(2)-X. In fact, the release of fatty acids from human serum was hardly detectable upon incubation with sPLA(2)-V in the presence of sodium citrate, which contrasted with the potent response to sPLA(2)-X. Moreover, sPLA(2)-X, but not sPLA(2)-V, was found to specifically interact with LDL among the serum proteins, as assessed by gel-filtration chromatography as well as sandwich enzyme-immunosorbent assay using anti-sPLA(2)-X and anti-apoB antibodies. Surface plasmon resonance studies have revealed that sPLA2-X can bind to LDL with high-affinity (K(d) = 3.1 nM) in the presence of Ca(2+). Selective interaction of sPLA(2)-X with LDL might be involved in the efficient hydrolysis of cell surface or intracellular phospholipids during foam cell formation.
Shigeki Kamitani; Katsutoshi Yamada; Shigenori Yamamoto; Yoshikazu Ishimoto; Takashi Ono; Akihiko Saiga; Kohji Hanasaki
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Publication Detail:
Type:  Journal Article     Date:  2012-06-13
Journal Detail:
Title:  Cellular & molecular biology letters     Volume:  17     ISSN:  1689-1392     ISO Abbreviation:  Cell. Mol. Biol. Lett.     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-06-18     Completed Date:  2012-12-31     Revised Date:  2013-04-04    
Medline Journal Info:
Nlm Unique ID:  9607427     Medline TA:  Cell Mol Biol Lett     Country:  Poland    
Other Details:
Languages:  eng     Pagination:  459-78     Citation Subset:  IM    
Department of Molecular Bacteriology, RIMD, Osaka University, 3-1, Yamada-oka, Suita-shi, Osaka, 565-0871, Japan.
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MeSH Terms
Arachidonic Acid* / chemistry,  metabolism
Calcium / chemistry
Citrates / chemistry
Group V Phospholipases A2 / chemistry,  metabolism*
Group X Phospholipases A2 / chemistry,  metabolism*
Linoleic Acid* / chemistry,  metabolism
Lipoproteins, HDL* / chemistry,  metabolism
Lipoproteins, LDL* / chemistry,  metabolism
Phospholipids / chemistry,  metabolism
Protein Binding
Serum / chemistry,  metabolism
Surface Plasmon Resonance
Reg. No./Substance:
0/Citrates; 0/Lipoproteins; 0/Lipoproteins, HDL; 0/Lipoproteins, LDL; 0/Phospholipids; 1Q73Q2JULR/sodium citrate; 2197-37-7/Linoleic Acid; 506-32-1/Arachidonic Acid; 7440-70-2/Calcium; EC V Phospholipases A2; EC X Phospholipases A2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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