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Introduction of NAD decreases fMLP‐induced actin polymerization in chicken polymorphonuclear leukocytes ‐ The role of intracellular ADP‐ribosylation of actin for cytoskeletal organization
Author(s) -
Terashima Masaharu,
Shimoyama Makoto,
Tsuchiya Mikako
Publication year - 1999
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549900201663
Subject(s) - nad+ kinase , adp ribosylation , actin , chemistry , biochemistry , cytoskeleton , actin remodeling , actin binding protein , microbiology and biotechnology , chemotaxis , intracellular , actin cytoskeleton , biology , cell , enzyme , receptor
We reported previously that the arginine‐specific. ADP‐ribosyltransferase in chicken polymorphonuclear leukocytes specifically modified actin, thereby inhibiting actin polymerization in vitro. In the present study, we investigated the effect of ADP‐ribosylation on actin polymerization in situ. In the leukocytes, the introduction of NAD inhibited the increase in filamentous actin contents induced by a chemotactic peptide formyl‐methionyl‐leucyl‐phenylalanine, while introduction of NAD together with novobiocin, a specific inhibitor for ADP‐ribosyltransferase, did not. These results suggest that ADP‐ribosylation regulates the formation of filamentous actin by the covalent modification of the protein in vivo.