|
|
Previous Article | Table of Contents | Next Article 
Actin polymerization and its relationship to locomotion and chemokinetic
response in maturing human promyelocytic leukemia cells
WH Meyer and TH Howard
We studied actin polymerization in the HL-60 human promyelocytic leukemia
cell line during induced myeloid maturation and its relationship to the
rate of locomotion (ROL). The percent G-actin (of total actin) was measured
by DNAase I inhibition, F-actin was determined by fluorescence-activated
cell sorter (FACS) analysis of nitrobenzoxadiazol (NBD)-phallacidin-stained
cells, and ROL was measured by computer-assisted analysis of the tracks of
individual cells. Uninduced HL-60 cells moved slowly (2.3 +/- 1.0
microns/min) and showed no change in ROL or in the state of actin
polymerization when stimulated by formyl-methionyl-leucyl-phenylalanine
(fMLP). Nonstimulated cells induced to differentiate with dimethylformamide
had no change in the degree of actin polymerization but exhibited a mean
(m) ROL similar to normal human polymorphonuclear leukocytes (PMN) (8.6 +/-
1.4 micron/min [HL-60 cells] v 7.8 +/- 1.8 microns/min [PMN]. When induced
HL-60 cells were stimulated with fMLP, actin polymerization occurred. The
F-actin content increased, as determined by FACS analysis of
NBD-phallacidin-stained cells, and the percentage of G-actin decreased, as
determined by a 24.5% decrease in DNAase I inhibitory activity. However,
induced HL-60 cells stimulated with fMLP did not increase their mROL. These
studies show that, unlike normal human PMN, chemotactic peptides can cause
an intracellular biochemical change that is not associated with a
chemokinetic response in induced HL-60 cells. The HL-60 cell line may be a
useful model to study the development of chemotactic peptide-mediated actin
polymerization during myeloid cell maturation.
Volume 70,
Issue 2,
pp. 363-367,
08/01/1987
Copyright © 1987 by The American Society of Hematology

CiteULike Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
P. Gaines, J. Chi, and N. Berliner
Heterogeneity of functional responses in differentiated myeloid cell lines reveals EPRO cells as a valid model of murine neutrophil functional activation
J. Leukoc. Biol.,
May 1, 2005;
77(5):
669 - 679.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
Y. Li, Q. Zhang, R. Aaron, L. Hilliard, and T. H. Howard
LSP1 modulates the locomotion of monocyte-differentiated U937 cells
Blood,
August 1, 2000;
96(3):
1100 - 1105.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
I. Fabian, D. Halperin, S. Lefter, L. Mittelman, R. T. Altstock, O. Seaon, and I. Tsarfaty
Alteration of Actin Organization by Jaspamide Inhibits Ruffling, but not Phagocytosis or Oxidative Burst, in HL-60 Cells and Human Monocytes
Blood,
June 1, 1999;
93(11):
3994 - 4005.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
M. J. Tino and J. R. Wright
Surfactant proteins A and D specifically stimulate directed actin-based responses in alveolar macrophages
Am J Physiol Lung Cell Mol Physiol,
January 1, 1999;
276(1):
L164 - L174.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
L. Feng, E. Kim, W.-L. Lee, C. J. Miller, B. Kuang, E. Reisler, and P. A. Rubenstein
Fluorescence Probing of Yeast Actin Subdomain 3/4 Hydrophobic Loop 262-274. ACTIN-ACTIN AND ACTIN-MYOSIN INTERACTIONS IN ACTIN FILAMENTS
J. Biol. Chem.,
July 4, 1997;
272(27):
16829 - 16837.
[Abstract]
[Full Text]
[PDF]
|
 |
|
|
|