Proteinaceous inhibitors of phospholipase A2 purified from inflammatory sites in rats.
AUTOR(ES)
Suwa, Y
RESUMO
We have purified two phospholipase A2 inhibitory proteins (37 and 33 kDa) from peritoneal fluid of dexamethasone-treated rats. The extracellular phospholipase A2 found in inflammatory sites differed from the exocrine phospholipase A2 in susceptibility to these endogenous inhibitors; both proteins inhibited the activity of the extracellular phospholipase A2 purified from sites of inflammation but did not affect appreciably the activity of either porcine pancreatic or Naja naja venom phospholipase A2. The amino acid sequence of the NH2-terminal portion of the purified proteins did not resemble that of lipocortins so far reported, but it was almost identical to that of parts of human or mouse complement component C3. These findings may indicate that degraded products of C3 are involved in the regulation of activity of a class of mammalian phospholipase A2.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=53695Documentos Relacionados
- Glucocorticoid deficiency increases phospholipase A2 activity in rats.
- Liver cirrhosis induces renal and liver phospholipase A2 activity in rats.
- Alpha-type phospholipase A2 inhibitors from snake blood
- Endogenous phospholipase A2 inhibitors in snakes: a brief overview
- Pathophysiological role of secretory type I and II phospholipase A2 in acute pancreatitis: an experimental study in rats.