Nitric oxide induces chemotaxis of neutrophil-like HL-60 cells and translocation of cofilin to plasma membranes

Adachi, Reiko; Matsui, Sachiko; Kinoshita, Masanao; Nagaishi, Keiko; Sasaki, Haruyo; Kimura, Tadashi; Suzuki, Kazuhiro

doi:10.1016/s0192-0561(00)00045-x

Cited by 23 publications

(14 citation statements)

References 48 publications

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“…PDE1B2 is also likely to be important for functions of the mature macrophage. For example, it is well known that agents such as NO that increase cGMP will alter neutrophil chemotaxis and migration (51)(52)(53). This effect is well established in neutrophils and has been suggested to be the case for macrophages (54,55).…”

Section: Discussionmentioning

confidence: 96%

Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation

Bender

Ostenson

Wang

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Granulocyte-macrophage colony-stimulating factor (GM-CSF) is a major regulator of monocyte to macrophage differentiation. In both humans and mice, the main phenotype of decreased GM-CSF function is pulmonary proteinosis due to aberrant function of alveolar macrophages. Recently, this cytokine has been shown to up-regulate a cyclic nucleotide phosphodiesterase, PDE1B. Two PDE1B variants with unique N-terminal sequences, PDE1B1 and PDE1B2, have been identified. Here, we report that the previously uncharacterized PDE1B2 is selectively increased by GM-CSF by stimulation of transcription at a previously unknown transcriptional start site. Analysis of the exon and intron organization of the PDE1B gene reveals that PDE1B2 has a different N-terminal sequence because of a separate first exon that is located 11.5 kb downstream from the PDE1B1 first exon. By using 5 -RACE, alignment of EST sequences, and a luciferase-reporter system, we provide evidence that PDE1B2 has a separate transcriptional start site from PDE1B1 that can be activated by monocyte differentiation. Furthermore, IL-4 treatment in the presence of GM-CSF, which shifts the differentiation from a macrophage to a dendritic cell phenotype, suppresses the up-regulation of PDE1B2. Induction of PDE1B2 is also found in T cells upon activation by PHA. Therefore, PDE1B2 may have a regulatory role in multiple immune cell types. Last, characterization of the catalytic properties of recombinant PDE1B2 shows that it prefers cGMP over cAMP as a substrate and, thus, is likely to regulate cGMP in macrophages. Also, PDE1B2 has a nearly 3-fold lower EC50 for activation by calmodulin than PDE1B1.cAMP ͉ cGMP ͉ phosphodiesterase

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Section: Discussionmentioning

confidence: 96%

Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation

Bender

Ostenson

Wang

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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“…In fact, it has been reported that the level of total cofilin and the ratio of phosphorylated and unphosphorylated cofilin differ in various tissues or cells (2,6,23,48). In addition, in the case of chemotaxis induced by nitric oxide, cofilin translocated to the plasma membrane regions but was neither phosphorylated nor dephosphorylated in neutrophillike HL-60 cells (27). It can be thought that, upon cell activation, signals leading to both phosphorylation and dephosphorylation of cofilin are generated to control appropriately the dynamics of the actin cytoskeleton in each intracellular region and at each time point.…”

Section: Discussionmentioning

confidence: 99%

“…We used opsonized zymosan (OZ) 1 as a cell stimulant, a complement C3bi-coated insoluble polysaccharide, the receptor for which is a member of the ␤ 2 integrin family (CR3, CD11b/CD18), and have reported that cofilin and phagocyte functions such as superoxide production or phagocytosis were strongly correlated with each other under the regulation by Src family tyrosine kinase and phospholipase C (24 -26). We also reported that cofilin was engaged in chemotaxis (27). Lately, by employing the method of LIM kinase 1 (LIMK1) transfection, we have demonstrated that the cofilindependent regulation of actin is implicated in superoxide production (28).…”

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confidence: 97%

Antisense Oligonucleotide to Cofilin Enhances Respiratory Burst and Phagocytosis in Opsonized Zymosan-stimulated Mouse Macrophage J774.1 Cells

Adachi

Takeuchi

Suzuki

2002

Journal of Biological Chemistry

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Phagocytes play a central role in the host defense system, and the relationship between the mechanism of their activation and cytoskeletal reorganization has been studied. We have previously reported a possible involvement of cofilin, an actin-binding protein, in phagocyte functions through its phosphorylation/dephosphorylation and translocation to the plasma membrane regions. In this work, we have obtained a new line of evidence showing an important role of cofilin in phagocyte functions using the mouse macrophage cell line J774.1 and an antisense oligonucleotide to cofilin. Upon stimulation with opsonized zymosan (OZ), cofilin was phosphorylated, and it accumulated around phagocytic vesicles. As the antisense oligonucleotide to cofilin, a 20-mer S-oligo corresponding to the sequence including the AUG translational initiation site was found to be effective. In the cells treated with the antisense oligonucleotide, the amount of cofilin was less than 30% of that in the control cells, and the level of F-actin was two or three times higher than that in the control cells before and throughout the cell activation. In the antisense oligonucleotide-treated cells, OZ-triggered superoxide production was three times faster than that in the control cells. Furthermore, phagocytosis of OZ was enhanced by the antisense. These results show that cofilin plays an essential role in the control of phagocyte function through regulation of actin filament dynamics.Phagocytes, including neutrophils and macrophages, are at rest in the absence of any stimulant; but, when activated by invading microorganisms or harmful substances, they play a central role in host defense systems through chemotaxis, adhesion, phagocytosis, superoxide production, degranulation, and the release of cytokines or lipid mediators. The mechanism of phagocyte activation has been studied in terms of protein phosphorylation and cytoskeletal reorganization (1). Originally we found that cofilin, an actin-and phosphatidylinositol 4,5-bisphosphate-binding protein, is rapidly dephosphorylated upon cell activation and translocated to plasma membrane regions in neutrophil-like HL-60 cells (2). These findings have been confirmed by other groups (3-5). Cofilin is a widely distributed protein highly conserved among various species and plays an essential role in the control of actin filament dynamics (6 -8). It has been well investigated in, for example, Dictyostelium (9 -11), yeast (12-14), Xenopus egg (15-17), mammalian neural cells (18 -20), and immune cells (21-23). Cofilin can be phosphorylated at Ser-3, and only the unphosphorylated form of cofilin can bind actin and depolymerize or sever the actin filament. It is also proposed that cofilin is involved in the turnover of actin filament.To date we have studied the relation between cofilin and phagocyte functions. We used opsonized zymosan (OZ) 1 as a cell stimulant, a complement C3bi-coated insoluble polysaccharide, the receptor for which is a member of the ␤ 2 integrin family (CR3, CD11b/CD18), and have reported that co...

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“…A number of studies have demonstrated that dephosphorylated cofilin localizes to the leading edge of migrating leukocytes, where actin polymerization is ongoing (Adachi et al, 2000;Nishita, 2005). The important role of cofilin in regulating actin assembly during chemotaxis is also highlighted by the observation that leukocytes with defects in cofilin dephosphorylation (downstream of Rac2) or in which cofilin is knocked down are unable to generate free F-actin barbed ends downstream of chemoattractant receptors (Jovceva et al, 2007;Sun et al, 2007).…”

Section: Translocation Of Dephosphorylated Cofilin To the Leading Edgementioning

confidence: 99%

A common cofilin activity cycle in invasive tumor cells and inflammatory cells

Rheenen

Condeelis

Glogauer

2009

Journal of Cell Science

110

119

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In many cell types, the formation of membrane protrusions and directional migration depend on the spatial and temporal regulation of the actin-binding protein cofilin. Cofilin, which is important for the regulation of actin-polymerization initiation, increases the number of actin free barbed ends through three mechanisms: its intrinsic actin-nucleation activity; binding and severing of existing actin filaments; and recycling actin monomers from old filaments to new ones through its actin-depolymerization activity. The increase in free barbed ends that is caused by cofilin initiates new actin polymerization, which can be amplified by the actin-nucleating ARP2/3 complex. Interestingly, different cell systems seem to have different mechanisms of activating cofilin. The initial activation of cofilin in mammary breast tumors is dependent on PLCγ, whereas cofilin activation in neutrophils is additionally dependent on dephosphorylation, which is promoted through Rac2 signaling. Although the literature seems to be confusing and inconsistent, we propose that all of the data can be explained by a single activity-cycle model. In this Opinion, we give an overview of cofilin activation in both tumor cells and inflammatory cells, and demonstrate how the differences in cofilin activation that are observed in various cell types can be explained by different starting points in this single common activity cycle.

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Nitric oxide induces chemotaxis of neutrophil-like HL-60 cells and translocation of cofilin to plasma membranes

Cited by 23 publications

References 48 publications

Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation

Selective up-regulation of PDE1B2 upon monocyte-to-macrophage differentiation

Antisense Oligonucleotide to Cofilin Enhances Respiratory Burst and Phagocytosis in Opsonized Zymosan-stimulated Mouse Macrophage J774.1 Cells

A common cofilin activity cycle in invasive tumor cells and inflammatory cells

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