Quercetin modulates activities of Taiwan cobra phospholipase A2 via its effects on membrane structure and membrane-bound mode of phospholipase A2 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2012-04-25

AUTHORS

Yi-Ling Chiou, Shinne-Ren Lin, Wan-Ping Hu, Long-Sen Chang

ABSTRACT

The goal of the present study is to elucidate the mechanism of quercetin on modulating Naja naja atra phospholipase A2 (PLA2) activities. Sphingomyelin inhibited PLA2 enzymatic activity and membrane-damaging activity against egg yolk phosphatidylcholine (EYPC), while cholesterol and quercetin abrogated the sphingomeyelin inhibitory effect. Quercetin incorporation led to a reduction in PLA2 enzymatic activity and membrane-damaging activity toward EYPC/sphingomyelin/cholesterol vesicles. Both cholesterol and quercetin increased detergent resistance and reduced membrane fluidity of EYPC/sphingomyelin vesicles. Quercetin reduced detergent insolubility but increased ordered lipid packing of EYPC/sphingomyelin/cholesterol vesicles. Acrylamide quenching studies and trinitrophenylation of Lys residues revealed that quercetin altered the membrane-bound mode of PLA2 differently upon absorption onto the membrane bilayers of different lipid compositions. However, 8-anilinonaphthalene sulphonate-binding assay revealed that quercetin marginally affected the interaction between active site of PLA2 with phospholipid vesicles. Collectively, our data indicate that membrane-inserted quercetin modulates PLA2 interfacial activity and membrane-damaging activity via its effects on membrane structure and membrane-bound mode of PLA2. More... »

PAGES

277-287

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12038-012-9198-2

DOI

http://dx.doi.org/10.1007/s12038-012-9198-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017582619

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22581333


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