Modulation of tissue factor-factor VIIa signaling by lipid rafts and caveolae.

Objective: Coagulation factor VIIa (VIIa) binding to its cellular receptor, tissue factor (TF), not only initiates the coagulation cascade but also induces cell signaling by activating G-protein coupled protease-activated receptors. The objective of the present study is to investigate the role of lipid rafts and caveolae in modulating TF-VIIa signaling and coagulant functions.

Methods And Results: TF-VIIa coagulant function was measured in factor X activation assay and the signaling function was evaluated in phosphoinositide hydrolysis and IL-8 gene induction.

Triton X-100 inhibition of yeast plasma membrane associated NADH-dependent redox activities.

Plasma membrane (PM) vesicles isolated from the yeast Saccharomyces cerevisiae (wild-type NCIM 3078, and a MG 21290 mutant pma 1-1) were used to monitor the effect of the detergents, 3-[(3-cholamidopropyl) dimethylammonio]-1-propane sulfonate (Chaps) and Triton X-100, on (H+)-ATPase (E.C. 3.

Concanavalin A induced activity change in yeast PM-bound NADH-HCF(III) oxidoreductase.

The activity of plasma membrane bound redox enzyme, NADH-HCF(III) oxidoreductase, in wild and mutant strains of the yeast Saccharomyces cerevisiae is modulated by Con A in a dose-dependent manner. The solubilized activity is enhanced at lower concentration and inhibited at higher concentration of Con A. The enzyme in mutant strain is more sensitive to inhibition.