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.
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Authors | F Cabré, J J Moreno, A Carabaza, E Ortega, D Mauleón, G Carganico |
Journal | Biochemical pharmacology
(Biochem Pharmacol)
Vol. 44
Issue 3
Pg. 519-25
(Aug 04 1992)
ISSN: 0006-2952 [Print] England |
PMID | 1387313
(Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Annexins
- Anti-Inflammatory Agents
- Calcium-Binding Proteins
- Retinoids
- Uteroglobin
- Phospholipases A
- Phospholipases A2
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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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