Cloning of a phospholipase A2-activating protein.
AUTOR(ES)
Clark, M A
RESUMO
Recently we have described the isolation and biochemical characterization of a phospholipase A2-activating protein (PLAP). We have cloned this protein and found it to be expressed as a 2.5-kilobase mRNA. The steady-state levels of PLAP mRNA are induced in smooth muscle and endothelial cells following treatment with leukotriene D4. The increased message levels coincide with increased amounts of PLAP. Synthetic antisense DNA was used to block the synthesis of PLAP and this treatment effectively blocked the activation of phospholipase A2 and the increased generation of prostanoids in smooth muscle and endothelial cells treated with leukotriene D4.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=51884Documentos Relacionados
- Cholera toxin induces synthesis of phospholipase A2-activating protein.
- Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A2-activating Protein*
- Characterization of a Helicobacter pylori neutrophil-activating protein.
- A Ras-GTPase-activating protein SH3-domain-binding protein.
- IRA2, an upstream negative regulator of RAS in yeast, is a RAS GTPase-activating protein.