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Antiflammins. Anti-inflammatory activity and effect on human phospholipase A2.

Abstract
Two anti-inflammatory peptides (antiflammins) corresponding to a high amino acid similarity region between lipocortin I and uteroglobin were tested for their ability to inhibit purified human synovial fluid phospholipase A2 (HSF-PLA2). No inhibitory activity was observed, even at such high concentrations of peptides as 50 microM. When antiflammins were preincubated with the enzyme and/or the substrate, no HSF-PLA2 inhibition was detected. In vivo anti-inflammatory activity of these peptides was evaluated in several experimental models of inflammation induced by carrageenan, croton-oil, oxazolone and Naja naja naja venom phospholipase A2 (PLA2). In contrast to the in vitro results, anti-inflammatory activity was observed in all tests, except when inflammation was induced by snake venom PLA2. Taken together, our results do not support the hypothesis that the in vivo anti-inflammatory effect of antiflammins is directly related to inhibition of PLA2 activity.
AuthorsF Cabré, J J Moreno, A Carabaza, E Ortega, D Mauleón, G Carganico
JournalBiochemical pharmacology (Biochem Pharmacol) Vol. 44 Issue 3 Pg. 519-25 (Aug 04 1992) ISSN: 0006-2952 [Print] England
PMID1387313 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Annexins
  • Anti-Inflammatory Agents
  • Calcium-Binding Proteins
  • Retinoids
  • Uteroglobin
  • Phospholipases A
  • Phospholipases A2
Topics
  • Animals
  • Annexins
  • Anti-Inflammatory Agents
  • Calcium-Binding Proteins (pharmacology)
  • Capillary Permeability (drug effects)
  • Edema (chemically induced, enzymology)
  • Humans
  • Inflammation (chemically induced, enzymology)
  • Mice
  • Pancreas (enzymology)
  • Phospholipases A (antagonists & inhibitors)
  • Phospholipases A2
  • Rats
  • Rats, Inbred Strains
  • Retinoids (pharmacology)
  • Swine
  • Synovial Fluid (drug effects, enzymology)
  • Uteroglobin (pharmacology)

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