Sphingomyelinase D activity in model membranes: structural effects of in situ generation of ceramide-1-phosphate.

PloS One
Roberto P StockLuis A Bagatolli

Abstract

The toxicity of Loxosceles spider venom has been attributed to a rare enzyme, sphingomyelinase D, which transforms sphingomyelin to ceramide-1-phosphate. The bases of its inflammatory and dermonecrotic activity, however, remain unclear. In this work the effects of ceramide-1-phosphate on model membranes were studied both by in situ generation of this lipid using a recombinant sphingomyelinase D from the spider Loxosceles laeta and by pre-mixing it with sphingomyelin and cholesterol. The systems of choice were large unilamellar vesicles for bulk studies (enzyme kinetics, fluorescence spectroscopy and dynamic light scattering) and giant unilamellar vesicles for fluorescence microscopy examination using a variety of fluorescent probes. The influence of membrane lateral structure on the kinetics of enzyme activity and the consequences of enzyme activity on the structure of target membranes containing sphingomyelin were examined. The findings indicate that: 1) ceramide-1-phosphate (particularly lauroyl ceramide-1-phosphate) can be incorporated into sphingomyelin bilayers in a concentration-dependent manner and generates coexistence of liquid disordered/solid ordered domains, 2) the activity of sphingomyelinase D is clearly influence...Continue Reading

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Citations

Mar 19, 2014·Toxicon : Official Journal of the International Society on Toxinology·Luiza Helena GremskiSilvio Sanches Veiga
Sep 26, 2013·Langmuir : the ACS Journal of Surfaces and Colloids·Charng-Yu Lin, Ling Chao
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Oct 26, 2016·Chemistry and Physics of Lipids·Carolyn M ShireyRobert V Stahelin

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Methods Mentioned

BETA
ISS
FCS
Fluorescence
fluorescence microscopy
FRET
fluorescence correlation spectroscopy
light scattering

Software Mentioned

LAURDAN GP
LAURDAN
SimFCS
CONTIN
SimFCS for

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