ISSN:
0886-1544
Keywords:
myosin phosphorylation
;
actin polymerization
;
chemotactic factors
;
leukocytes
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Medicine
Notes:
Changes in the state of polymerization of actin and phosphorylation of myosin have been observed in polymorphonuclear leukocytes (PMNs) soon after the addition of the chemotactic peptide N-formylnorleucylleucylphenylalanine. At a time when the cells are observed to extend many ruffles or lamellipodia from their surface, the fraction of the cellular actin present in a monomeric form is decreased by about 25% as assayed by the ability of the G-actin to inhibit DNAase. These changes are temporally correlated with an increase in the staining by nitrobenzooxadiazole (NBD)-phallacidin, a probe that binds F-actin selectively. The NBD-phallacidin staining is observed in the surface ruffles. When the peptide concentration is decreased by addition of a tenfold excess of buffer, cells withdraw their surface ruffles and form blebs. These changes correlate with an increase in the G-actin levels detected with the DNAase inhibition assay. An increase in phosphorylation of the 20,000-dalton light chain of myosin is also observed in leukocytes stimulated by addition of chemotactic peptide. These observations of changes in cytoskeletal proteins of PMNs provide a beginning for further studies on the regulation of cell motility by chemotactic factors.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/cm.970030406
Permalink
