Several structurally related plant lipids were isolated and their effect was assessed on the enzyme activity of group I (pancreatic and Naja mocambique venom) and group II (Crotalus atrox venom) phospholipase A2 (PLA2) enzymes, with labelled Escherichia coli as an enzyme substrate. The neutral monogalactosyldiacylglycerol (MGDG) and negatively charged diacylglyceryl α-D-glucuronide (DGGA) did not influence the enzyme activity of either group. Digalactosyldiacylglycerol (DGDG), another uncharged glycolipid, inhibited PLA2 activity in a dose-dependent manner to 60–70% of the control. Sulphoquinovosyldiacylglycerol (SQDG), which is also anionic, activated both groups of PLA2 enzyme. A similar activation was observed with the zwitterionic diacylglyceryl-O-(N,N,N-trimethylhomoserine) (DGTS) and diacylglyceryl-O-(hydroxymethyl)(N,N,N-trimethyl)-β-alanine (DGTA). DGDG, SQDG and DGTS are dispersed homogeneously with low critical micelle concentrations (CMCs). The hydrodynamic radius of neutral DGDG is an order of magnitude larger than the charged lipids SQDG and DGTS. The inhibition of pig pancreatic PLA2 by DGDG was dependent on substrate concentration. The intrinsic fluorescence spectra of the enzyme was not changed in the presence of native or hydrogenated DGDG. Thus the inhibition is most probably due to a non-specific interaction of plant lipids with the substrate. Different lengths and saturations of the fatty acyl chains of DGDG did not alter the inhibition of PLA2, whereas deacylation abrogated the inhibitory effect. Both SQDG and DGTS activated pig pancreatic PLA2 in a dose-dependent manner. Saturation of the double bonds of these lipids decreased the activating effect. The fluorescence of pig pancreatic PLA2 incubated with SQDG and DGTS was enhanced by 2-fold and 3-fold respectively, suggesting the formation of a complex between enzyme and lipids. In conclusion, the effect of different plant lipids on PLA2 activity depends on different structural elements of the polar head group and their charge as well as the degree of unsaturation of the fatty acyl chains.
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November 1996
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Research Article|
November 15 1996
Interaction of plant lipids with 14 kDa phospholipase A2 enzymes Available to Purchase
Bannikuppe S VISHWANATH;
Bannikuppe S VISHWANATH
*Division of Nephrology, Department of Medicine, Freiburgstrasse 3, Inselspital, 3010 Berne, Switzerland
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Waldemar EICHENBERGER;
Waldemar EICHENBERGER
†Department of Biochemistry, University of Berne, Berne, Switzerland
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Felix J FREY;
Felix J FREY
*Division of Nephrology, Department of Medicine, Freiburgstrasse 3, Inselspital, 3010 Berne, Switzerland
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Brigitte M. FREY
Brigitte M. FREY
‡
*Division of Nephrology, Department of Medicine, Freiburgstrasse 3, Inselspital, 3010 Berne, Switzerland
‡To whom correspondence should be addressed
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Publisher: Portland Press Ltd
Received:
April 26 1996
Revision Received:
July 09 1996
Accepted:
July 23 1996
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1996
1996
Biochem J (1996) 320 (1): 93–99.
Article history
Received:
April 26 1996
Revision Received:
July 09 1996
Accepted:
July 23 1996
Citation
Bannikuppe S VISHWANATH, Waldemar EICHENBERGER, Felix J FREY, Brigitte M. FREY; Interaction of plant lipids with 14 kDa phospholipase A2 enzymes. Biochem J 15 November 1996; 320 (1): 93–99. doi: https://doi.org/10.1042/bj3200093
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