Abstract | PURPOSE OF REVIEW: RECENT FINDINGS: Amongst the 10 mammalian sPLA2 isozymes, sPLA2-X, -V, -IIF and -III exhibit much more potent PC-hydrolyzing activity than do the others, and can release free fatty acids and lysophospholipids from the PC-rich outer leaflet of the cellular plasma membrane. In particular, sPLA2-X and sPLA2-V hydrolyze PC in lipoproteins far more efficiently than does sPLA2-IIA. Moreover, sPLA2-X promotes foam cell formation in vitro and is expressed in the atherosclerotic arterial walls of apolipoprotein E deficient mice in vivo. SUMMARY: PC-hydrolyzing sPLA2 isozymes, particularly sPLA2-V and sPLA2-X, are attractive candidates for proatherosclerotic factors that may act in place of sPLA2-IIA. However, their expression in human atherosclerotic lesions requires confirmation by specific methods that can distinguish between the different sPLA2 isozymes.
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Authors | Makoto Murakami, Ichiro Kudo |
Journal | Current opinion in lipidology
(Curr Opin Lipidol)
Vol. 14
Issue 5
Pg. 431-6
(Oct 2003)
ISSN: 0957-9672 [Print] England |
PMID | 14501581
(Publication Type: Journal Article, Review)
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Chemical References |
- Fatty Acids
- Isoenzymes
- Lipoproteins
- Lysophosphatidylcholines
- Phosphatidylcholines
- Proteoglycans
- Phospholipases A
- Group II Phospholipases A2
- Group X Phospholipases A2
- PLA2G10 protein, human
- Phospholipases A2
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Topics |
- Animals
- Arteries
(enzymology)
- Arteriosclerosis
(enzymology, etiology)
- Fatty Acids
(metabolism)
- Group II Phospholipases A2
- Group X Phospholipases A2
- Humans
- Inflammation
(enzymology, etiology)
- Isoenzymes
(classification, metabolism)
- Lipoproteins
(metabolism)
- Lysophosphatidylcholines
(metabolism)
- Phosphatidylcholines
(metabolism)
- Phospholipases A
(classification, metabolism)
- Phospholipases A2
- Proteoglycans
(metabolism)
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