Gelsolin-Actin Interaction and Actin Polymerization in Human Neutrophils

• Published in: The Journal of cell biology Vol. 110; no. 6; pp. 1983 - 1991
• Main Authors: Howard, T., Chaponnier, C., Yin, H., Stossel, T.
• Format: Journal Article
• Language: English
• Published: New York, NY Rockefeller University Press 01.06.1990; The Rockefeller University Press
• Subjects: Actins; Actins - metabolism; Actins - physiology; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Calcium; Calcium-Binding Proteins - analysis; Calcium-Binding Proteins - metabolism; Cell Extracts; Cells; Contractile proteins; Cytoskeleton; Dose-Response Relationship, Drug; Egtazic Acid - pharmacology; Fundamental and applied biological sciences. Psychology; Gelsolin; Holoproteins; Humans; Microfilament Proteins - analysis; Microfilament Proteins - metabolism; Microfilaments; Monomers; N-Formylmethionine Leucyl-Phenylalanine - pharmacology; Neutrophils; Neutrophils - drug effects; Neutrophils - metabolism; Neutrophils - physiology; Physiological regulation; Platelets; Polymerization; Polymers - metabolism; Proteins; Temperature; Time Factors; Human; Flow cytometry; Gel electrophoresis; Neutrophile; Actins; Polymerization; Contractile protein; Cytoskeleton; Molecular interaction; Molecular complex

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 ficollhypaque (FH)-purified neutrophils is in an EGTA r...