TAILIEUCHUNG - Báo cáo khoa học: Inactivation of annexin II tetramer by S-nitrosoglutathione

We investigated the effect of nitric oxide (NO) donors on the activities of annexin II tetramer (AIIt), a member of the Ca 2+ -dependent phospholipid-binding protein family. Incubation of purified AIIt with S-nitrosoglutathione (GSNO) led to the inhibition of AIIt-mediated liposome aggregation. This effect was dose-dependent with an IC50 of approximately 100lM. Sodium nitroprusside, another NO donor also inhibited AIIt-mediated liposome aggregation, whereas reduced glutathione, nitrate, or nitrite had no effects. . | Eur. J. Biochem. 269 4277-4286 2002 FEBS 2002 doi Inactivation of annexin II tetramer by 5-nitrosoglutathione Lin Liu1 2 Edward Enriaht2 Pena Sun1 Shwu Yar Tsai1. Praana Mehta2. David L Beckman2 B and David Mb Terrian3 1 Department of Physiological Sciences Oklahoma State University USA Departments of 2Physiology and 3 Anatomy and Cell Biology East Carolina University USA We investigated the effect of nitric oxide NO donors on the activities of annexin II tetramer AIIt a member of the Ca2 - dependent hhoshholid-d-binging J i- teia family. Incubation of purified AIIt with S-nitrosoglutathione GSNO led to the inhibition of AIIt-mediated liposome aggregation. This effect was dose-dependent with an IC50 of approximately 100 M. Sodium nitroprusside another NO donor also inhibited AIIt-mediated liposome aggregation whereas reduced glutathione nitrate or nitrite had no effects. GSNO also inhibited AIIt-mediated membrane fusion but not the binding of AIIt to the membrane. GSNO only has a modest effect on liposome aggregation mediated by annexins I III or IV. The binding of AIIt to the membrane protected the reactive sites of GSNO on AIIt. GSNO did not inhibit AIIt-mediated liposome aggregation in the presence of dithiothreitol. Taken together our results suggest that GSNO inactivates AIIt possibly via S-nitrosylation and or the formation of disulfide bonds. Keywords annexin nitric oxide S-nitrosoglutathione liposome aggregation membrane fusion. Annexins are a multigene family of Ca2 -dependent phospholipid-binding proteins and plays roles in many membrane-associated events including exocytosis endocy-tosis ion transport inflammation anticoagulation inhibition of phospholipases signal transduction Ca2 homeostasis cell-matrix cell-cell or cell-virus interaction etc. 1-7 . However most studies were carried out in vitro. Physiological functions of annexins are still unclear although progress has been made in the past several years. Annexin VI .

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