Protein kinase C-α and -β play antagonistic roles in the differentiation process of THP-1 cells

Dieter, Peter; Schwende, H.

doi:10.1016/s0898-6568(00)00069-3

Cited by 24 publications

(28 citation statements)

References 36 publications

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“…This may be related to reports that PKCβ is necessary for chemotaxis (Carnevale) and/or that PKCβ (Dieter 2000, Wadsworth 2002) and PKCδ (Larson 2000) are each required for phagocytosis. If taken together with our demonstration that macrophage fusion exhibits multiple features of phagocytosis (McNally 2005), these reports suggest that PKCβ and PKCδ may each facilitate phagocytosis signaling (Lennartz 1999, Greenberg 2002) during macrophage fusion.…”

Section: Discussionmentioning

confidence: 56%

“…These include PKCα in Fcγ receptormediated phagocytosis (Breton 2000) and in the IgG-stimulated respiratory burst (Larsen 2000), PKCβ in the phagocytosis of latex particles (Dieter 2000), and PKCβ and PKCδ in the phagocytosis of L. monocytogenes and translocation of PKCβ to early endosomes during bacterial escape from phagocytic vesicles (Wadsworth 2002). Novel PKCs δ and ε have also been linked to IgG-stimulated phagocytosis (Larsen 2000), and the phagocytosis of apoptotic cells by monocytes/macrophages requires PKC activity (Liu 2005).…”

Section: Introductionmentioning

confidence: 99%

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Foreign body-type multinucleated giant cell formation requires protein kinase C β, δ, and ζ

McNally

MacEwan

Anderson

2008

Experimental and Molecular Pathology

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Multinucleated giant cells are a classic cellular feature of chronic inflammation, although the mechanism of macrophage fusion leading to their formation is not well understood. Here, we investigate the participation of protein kinase C (PKC) in the interleukin (IL)-4-induced fusion of human monocyte-derived macrophages and foreign body giant cell (FBGC) formation in vitro. The PKC inhibitors H-7 and calphostin C attenuated macrophage fusion, whereas H-8, which is more selective for PKA and PKG, did not. Macrophage fusion was also prevented by the phospholipase C inhibitor, Et-18-OCH 3 , the PKC isoform inhibitors GO6983 or rottlerin and by peptide inhibitors for PKC (20-28), PKCβ, or PKCζ but not by HBDDE or peptide inhibitors for PKCε or PKA. In cultures of fusing macrophages/FBGC, we detected only PKCα, β, δ, and ζ by immunoprecipitation and immunoblotting, and we also observed strong expression of these isoforms by immunocytochemistry. Our collective results suggest that the γ, ε, η, μ, θ, or ι PKC isoforms are not required in the mechanism of IL-4-induced macrophage fusion; whether PKCα is required is unclear. However, new evidence is provided that FBGC formation is supported by PKCβ, PKCδ, and PKCζ in combined diacylglycerol-dependent (PKCβ and PKCδ) and -independent (PKCζ) signaling pathways.

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Section: Discussionmentioning

confidence: 56%

Section: Introductionmentioning

confidence: 99%

Foreign body-type multinucleated giant cell formation requires protein kinase C β, δ, and ζ

McNally

MacEwan

Anderson

2008

Experimental and Molecular Pathology

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“…The sequence for PKC-␣ isoenzyme-specific antisense oligonucleotide was 5Ј-CGC CGT GGA GTC GTT GCC CG-3Ј; the sense sequence was 5Ј-CGG GCA ACG ACT CCA CGG CG-3Ј (7). The PKC-␤ antisense oligonucleotide was 5Ј-CGC AGC CGG GTC AGC ATC-3Ј; the sense sequence was 5Ј-GAT GGC TGA CCC GGC TGC G-3Ј (19). The p47phox antisense oligonucleotide was 5Ј-TTT GTC TGG TTG TCT GTG GG-3Ј; the sense sequence was 5Ј-CCC ACA GAC AAC CAG ACA AA-3Ј (20).…”

Section: Measurement Of Omentioning

confidence: 99%

“…All of the oligonucleotides were phosphorothioate modified and high-performance liquid chromatography purified. ODNs were added to the cells at the concentration of 2 mol/l (7,19,20). Statistical analysis.…”

Section: Measurement Of Omentioning

confidence: 99%

α-Tocopherol Decreases Superoxide Anion Release in Human Monocytes Under Hyperglycemic Conditions Via Inhibition of Protein Kinase C-α

et al. 2002

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“…It has been reported that the depletion of PKC-b inhibited fMLP-induced phosphorylation of p47 phox and superoxide anion generation in differentiated HL-60 cells (Korchak et al, 1998), and neutrophils from PKC-b knockout mice markedly reduced the level of superoxide production (Dekker et al, 2000). Antisense-PKCa-transfected THP-1 cells showed a decreased release of superoxide anion (Dieter & Schwende, 2000). Moreover, the requirement of PKC-d in the regulation of NADPH oxidase activity in neutrophils has been reported recently (Brown et al, 2003).…”

Section: Y-h Kuan Et Almentioning

confidence: 88%

Artocarpol A stimulation of superoxide anion generation in neutrophils involved the activation of PLC, PKC and p38 mitogen‐activated PK signaling pathways

Kuan

Lin

Tsao

et al. 2005

British J Pharmacology

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1 Artocarpol A (ART), a natural phenolic compound isolated from Artocarpus rigida, stimulated a slow onset and long-lasting superoxide anion generation in rat neutrophils, whereas only slightly activated the NADPH oxidase in a cell-free system. 2 Pretreatment of neutrophils with pertussis toxin (1 mg ml À1 ), 50 mM 2 0 -amino-3 0 -methoxyflavone (PD 98059), or 1 mM 1,4-diamino-2,3-dicyano-1,4-bis(2-aminophenylthio)butadiene (U0126) had no effect on ART-stimulated superoxide anion generation. ART (30 mM) did not induce extracellular signal-regulated kinase (ERK) phosphorylation. 3 4-(4-Fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-1H-imidazole (SB 203580) markedly attenuated the ART-stimulated superoxide anion generation (IC 50 value of 4.370.3 mM). Moreover, ART induced p38 mitogen-activated PK (MAPK) phosphorylation and activation. 4 The superoxide anion generation in response to ART was also substantially inhibited in a Ca 2 þ -free medium, and by pretreatment with 1 mM 1-[6-((17b-3-methoxyestra-1,3,5(10)-trien-17-yl)amino)-hexyl]-1H-pyrrole-2,5-dione (U-73122) and 100 mM 2-aminoethyldiphenyl borate (2-APB). ART (30 mM) stimulated the [Ca 2 þ ] i elevation in the presence or absence of external Ca 2 þ , and also increased the D-myo-inositol 1,4,5-trisphosphate formation. 5 2-[1-(3-Dimethylaminopropyl)-1H-indol-3-yl]-3-(1H-indol-3-yl)-maleimide (GF 109203X) greatly inhibited the ART-stimulated superoxide anion generation (IC 50 value of 7.871.0 nM). ART increased the recruitment of PKC-a, -bI, and -bII to the plasma membrane of neutrophils, and stimulated Ca 2 þ -dependent PKC activation in the cytosol preparation. 6 ART induced the phosphorylation of p47 phox , which was attenuated by GF 109203X. Moreover, ART evoked the membrane association of p47 phox , which was inhibited by GF 109203X and SB 203580. 7 These results indicate that the ART stimulation of superoxide anion generation involved the activation of p38 MAPK, PLC/Ca 2 þ , and PKC signaling pathways in rat neutrophils.

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Protein kinase C-α and -β play antagonistic roles in the differentiation process of THP-1 cells

Cited by 24 publications

References 36 publications

Foreign body-type multinucleated giant cell formation requires protein kinase C β, δ, and ζ

Foreign body-type multinucleated giant cell formation requires protein kinase C β, δ, and ζ

α-Tocopherol Decreases Superoxide Anion Release in Human Monocytes Under Hyperglycemic Conditions Via Inhibition of Protein Kinase C-α

Artocarpol A stimulation of superoxide anion generation in neutrophils involved the activation of PLC, PKC and p38 mitogen‐activated PK signaling pathways

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