TY - JOUR
T1 - Priming-induced localization of Giα2 in high density membrane microdomains
AU - Keil, Michael L.
AU - Solomon, Naveenraj L.
AU - Lodhi, Irfan J.
AU - Stone, Kimberley C.
AU - Jesaitis, Algirdas J.
AU - Chang, Peter S.
AU - Linderman, Jennifer J.
AU - Omann, Geneva M.
N1 - Funding Information:
This work was supported by the Office of Research and Development, Medical Research Service, Department of Veteran Affairs, the Arthritis Foundation, National Science Foundation Grant BES 9410403, and PHS Grant RO1 AI22735.
PY - 2003/2/21
Y1 - 2003/2/21
N2 - 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, Giα2 and Giα3, N-formyl peptide receptor, Lyn kinase and phospholipase Cβ2. Giα2, but not Giα3, 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 Giα2 and its effector, phospholipase Cβ2, were segregated in different membrane compartments; priming caused Giα2 to move to the compartment in which phospholipase Cβ2 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.
AB - 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, Giα2 and Giα3, N-formyl peptide receptor, Lyn kinase and phospholipase Cβ2. Giα2, but not Giα3, 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 Giα2 and its effector, phospholipase Cβ2, were segregated in different membrane compartments; priming caused Giα2 to move to the compartment in which phospholipase Cβ2 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.
KW - Cellular activation
KW - Lipid rafts
KW - Lipopolysaccharide
KW - Membrane microdomains
KW - Neutrophils
KW - Recombinant human tumor necrosis factor α
KW - Signal transduction
UR - http://www.scopus.com/inward/record.url?scp=0037458967&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(03)00057-3
DO - 10.1016/S0006-291X(03)00057-3
M3 - Article
C2 - 12589792
AN - SCOPUS:0037458967
SN - 0006-291X
VL - 301
SP - 862
EP - 872
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -