Synthetic peptide from lipocortin I has no phospholipase A2 inhibitory activity.
Two anti-inflammatory peptides corresponding to a high amino acid similarity region between lipocortins were synthesized and tested on their ability to inhibit porcine pancreatic phospholipase A2. Kinetic assays using monomeric and aggregated phospholipids did not reveal any phospholipase A2 inhibitory activity. The peptides did not inhibit phospholipase A2 activity on monolayers of negatively charged substrate and did not prevent phospholipase A2 action on mixed micelles of 1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphocholine and sodiumdeoxycholate. Ultraviolet difference spectroscopy did not show binding of the peptides to phospholipase A2. Therefore we conclude that these anti-inflammatory peptides do not inhibit pancreatic phospholipase A2 in vitro, in contrast to the results recently published [(1988) Nature 335, 726-730].
van Binsbergen
J
J
Centre for Biomembranes and Lipid Enzymology, Utrecht, The Netherlands.
Slotboom
A J
AJ
Aarsman
A J
AJ
de Haas
G H
GH
D000595:Amino Acid Sequence; D000818:Animals; D017302:Annexins; D001665:Binding Sites; D006023:Glycoproteins / Q000138:chemical synthesis / Q000494:pharmacology*; D007700:Kinetics; D008823:Micelles; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000494:pharmacology*; D010179:Pancreas / Q000201:enzymology; D010740:Phospholipases / Q000037:antagonists & inhibitors*; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D013056:Spectrophotometry, Ultraviolet; D013552:Swine
D017302:Annexins; D006023:Glycoproteins; D008823:Micelles; D009842:Oligopeptides; D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2