Guanidination of notexin alters its membrane-damaging activity in response to sphingomyelin and cholesterol View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2010-10-25

AUTHORS

Pei-Hsiu Kao, Yi-Ling Chiou, Shinne-Ren Lin, Long-Sen Chang

ABSTRACT

To elucidate the contribution of phospholipase A2 (PLA2) activity of notexin to its ability to perturb membranes, comparative studies on the interaction of notexin and guanidinated notexin (Gu-notexin) with egg yolk phosphatidylcholine (EYPC), EYPC/egg yolk sphingomyelin (EYSM) and EYPC/EYSM/cholesterol vesicles were conducted. EYSM notably reduced the membrane-damaging activity of notexin against EYPC vesicles, but had an insignificant influence on that of Gu-notexin. Unlike the effects noted with notexin, inactivation of PLA2 activity by EDTA led to a reduction in the ability of Gu-notexin to induce EYPC/EYSM vesicle leakage and to increase Gu-notexin-induced membrane permeability of EYPC/EYSM/cholesterol vesicles. The geometrical arrangement of notexin and Gu-notexin in contact with either EYPC/EYSM vesicles or EYPC/EYSM/cholesterol vesicles differed. Moreover, global conformation of notexin and Gu-notexin differed in either Ca2+-bound or metal-free states. These results indicate that notexin and Gu-notexin could induce membrane permeability without the involvement of PLA2 activity, and suggest that guanidination alters the membrane-bound mode of notexin on damaging phospholipid vesicles containing sphingomyelin and cholesterol. More... »

PAGES

583-593

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12038-010-0067-6

DOI

http://dx.doi.org/10.1007/s12038-010-0067-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029097379

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21289441


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