Your browser doesn't support javascript.
loading
c-Fos is a surface pressure-dependent diverter of phospholipase activity.
Borioli, Graciela A; Fanani, María L; Caputto, Beatriz L; Maggio, Bruno.
Afiliação
  • Borioli GA; Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Pabellón Argentina, Ciudad Universitaria, Córdoba, Argentina. gborioli@dpb.fcq.unc.edu.ar
Biochem Biophys Res Commun ; 295(4): 964-9, 2002 Jul 26.
Article em En | MEDLINE | ID: mdl-12127989
c-Fos, a transcription factor, associates to endoplasmic reticulum and modulates phospholipid biosynthesis. Its surface thermodynamic properties allow it to differentially interact with phospholipid monolayers with a selective dependence on the lipid polar head group and the lateral surface pressure. We explored the c-Fos ability to modulate phospholipid degradation by phospholipases (ppPLA2, Bacillus cereus PLC, and sphingomyelinase) using the monolayer technique. Experiments conducted under constant packing conditions show that c-Fos modulates phospholipase activity in a finely tuned way, depending on the membrane intermolecular packing. Surface lateral pressures above 12-16 mN/m induce c-Fos to activate phospholipase A2 and sphingomyelinase, and abolish phospholipase C activity. The effects of c-Fos on other steps of the catalytic process, lag-time and extent, are synergic with those on activity. We show for the first time that c-Fos participates in modulating phospholipid degradation and that it can affect the formation of lipid second messenger products by PLA2, PLC, and sphingomyelinase.
Assuntos
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases Tipo C / Fosfolipases A / Esfingomielina Fosfodiesterase / Proteínas Proto-Oncogênicas c-fos Limite: Animals Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2002 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases Tipo C / Fosfolipases A / Esfingomielina Fosfodiesterase / Proteínas Proto-Oncogênicas c-fos Limite: Animals Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2002 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos