Gelsolin-actin interaction and actin polymerization in human neutrophils.
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چکیده
منابع مشابه
Gelsolin-actin interaction and actin polymerization in human neutrophils
The fraction of polymerized actin in human blood neutrophils increases after exposure to formyl-methionyl-leucyl-phenylalanine (fmlp), is maximal 10 s after peptide addition, and decreases after 300 s. Most of the gelsolin (85 +/- 11%) in resting ficoll-hypaque (FH)-purified neutrophils is in an EGTA resistant, 1:1 gelsolin-actin complex, and, within 5 s after 10(-7) M fmlp activation, the amou...
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Human neutrophils generally function adherent to an extracellular matrix. We have previously reported that upon adhesion to laminin- or fibronectin-coated, but not uncoated, plastic there is a depolymerization of actin in neutrophils. This phenomenon was not affected by inhibitors of the more well-studied components of the signal transduction pathway, specifically, pertussis toxin, an inhibitor...
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We have used streptolysin-0 (SO)-permeabilized neutrophils to investigate the signal transduction pathway through which chemoattractants induce actin polymerization. Chemoattractants stimulate phosphorylation of various proteins and lipids but whether these phosphorylations are required for actin polymerization is not known. Addition of guanosine 5’-3-0-(thio)triphosphate (GTPyS) to SO-permeabi...
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FcyRIIIb (CD 16) is a glycosyl phosphatidylinositol (GPI) anchored low-affinity IgG receptor, exclusively expressed on human neutrophils. FcyRIIIb associates with complement receptor 3 (CR3, Mac-1, CD1 lb/CD 18), which may indirectly link FcyRIIIb to the actin cytoskeleton. Upon neutrophil activation or apoptosis, FcyRIIIb is shed from the cell surface. In all of these events, actin rearrangeme...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1990
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.110.6.1983