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Priming-induced localization of Giα2in high density membrane microdomains

Elsevier Inc.
Publication Date
DOI: 10.1016/s0006-291x(03)00057-3
  • Membrane Microdomains
  • Lipid Rafts
  • Signal Transduction
  • Neutrophils
  • Lipopolysaccharide
  • Cellular Activation
  • Recombinant Human Tumor Necrosis Factor α
  • Biology


Abstract Subcellular fractionation of human neutrophils on linear sucrose density gradients was utilized to test the hypothesis that priming regulates the subcellular and sub-plasma membrane distribution of neutrophil G-protein subunits, G iα2 and G iα3, N-formyl peptide receptor, Lyn kinase and phospholipase C β2. G iα2, but not G iα3, moved from a lighter to a higher density plasma membrane fraction. Unoccupied N-formyl peptide receptors were found throughout the plasma membrane fractions and this distribution did not change with priming. In unprimed cells G iα2 and its effector, phospholipase C β2, were segregated in different membrane compartments; priming caused G iα2 to move to the compartment in which phospholipase C β2 resided. Thus, an important component of the mechanism of priming may involve regulation of the location of G-proteins and effector molecules in plasma membrane compartments where their abilities to couple may be enhanced.

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