Priming of neutrophils and macrophages for enhanced release of superoxide anion by the calcium ionophore ionomycin. Implications for regulation of the respiratory burst.

Finkel, Toren; Pabst, Michael J.; Suzuki, Hitoshi; Guthrie, L A; Forehand, J R; Phillips, Wayne A.; Johnston, Richard B.

doi:10.1016/s0021-9258(18)45246-5

Cited by 98 publications

(3 citation statements)

References 60 publications

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“…Increased TNF was observed in both the cardiomyocytes themselves and the interstitial cells. Indeed, locally produced TNF may be an important contributor to postischemic myocardial dysfunction, apoptosis, and/or hypertrophy (93,149,151,168,213,222,245,303).…”

Section: R578 Invited Reviewmentioning

confidence: 99%

Tumor necrosis factor in the heart

Meldrum

1998

American Journal of Physiology-Regulatory, Integrative and Comp

553

581

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The heart is a tumor necrosis factor (TNF)-producing organ. Both myocardial macrophages and cardiac myocytes themselves synthesize TNF. Accumulating evidence indicates that myocardial TNF is an autocrine contributor to myocardial dysfunction and cardiomyocyte death in ischemia-reperfusion injury, sepsis, chronic heart failure, viral myocarditis, and cardiac allograft rejection. Indeed, locally (vs. systemically) produced TNF contributes to postischemic myocardial dysfunction via direct depression of contractility and induction of myocyte apoptosis. Lipopolysaccharide or ischemia-reperfusion activates myocardial P38 mitogen-activated protein (MAP) kinase and nuclear factor kappa B, which lead to TNF production. TNF depresses myocardial function by nitric oxide (NO)-dependent and NO-independent (sphingosine dependent) mechanisms. TNF activation of TNF receptor 1 or Fas may induce cardiac myocyte apoptosis. MAP kinases and TNF transcription factors are feasible targets for anti-TNF (i.e., cardioprotective) strategies. Endogenous anti-inflammatory ligands, which trigger the gp130 signaling cascade, heat shock proteins, and TNF-binding proteins, also control TNF production and activity. Thus modulation of TNF in cardiovascular disease represents a realistic goal for clinical medicine.

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Section: R578 Invited Reviewmentioning

confidence: 99%

Tumor necrosis factor in the heart

Meldrum

1998

American Journal of Physiology-Regulatory, Integrative and Comp

553

581

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“…Ins(1,4,5)P3 causes an increase in the cytosolic free calcium concentration ([Ca2+]i) whereas diacylglycerol is an endogenous activator of protein kinase C (6, 7). Experiments with agents that modulate protein kinase C activity and [Ca2+]i indicate that these two messengers play an essential role in the stimulation of many functional activities of phagocytes, including the production of reactive oxygen intermediates by neutrophils and murine macrophages and intracellular killing of microorganisms by human monocytes (10,15,45,46). In our previous study, we observed that stimulation of the intracellular killing of Staphylococcus aureus by human monocytes by cross-linking Fc-yRI or Fc-yRII is a PLC-dependent process (47).…”

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confidence: 99%

Protein tyrosine kinase activity is essential for Fc gamma receptor-mediated intracellular killing of Staphylococcus aureus by human monocytes

et al. 1994

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Our previous study revealed that the intracellular killing of Staphylococcus aureus by human monocytes after cross-linking Fc gamma receptor I (Fc gamma RI) or Fc gamma RII is a phospholipase C (PLC)-dependent process. The aim of the present study was to investigate whether protein tyrosine kinase (PTK) activity plays a role in the Fc gamma R-mediated intracellular killing of bacteria and activation of PLC in these cells. The results showed that phagocytosis of bacteria by monocytes was not affected by the PTK inhibitors genistein and tyrphostin-47. The intracellular killing of S. aureus by monocytes after cross-linking Fc gamma RII or Fc gamma RII with anti-Fc gamma R monoclonal antibody and a bridging antibody or with human immunoglobulin G (IgG) was inhibited by these compounds in a dose-dependent fashion. The production of O2- by monocytes after stimulation with IgG or IgG-opsonized S. aureus was almost completely blocked by the PTK inhibitor. These results indicate that inhibition of PTK impairs the oxygen-dependent bactericidal mechanisms of monocytes. Genistein and tyrphostin-47, which do not affect the enzymatic activity of purified PLC, prevented activation of PLC after cross-linking Fc gamma RI or Fc gamma RII, measured as an increase in the intracellular inositol 1,4,5-trisphosphate concentration. Cross-linking Fc gamma RI or Fc gamma RII induced rapid tyrosine phosphorylation of several proteins in monocytes, one of which was identified as PLC-gamma 1, and the phosphorylation could be completely blocked by PTK inhibitors, leading to the conclusion that activation of PLC after cross-linking Fc gamma R in monocytes is regulated by PTK activity. Together, these results demonstrate that PTK activity is essential for the activation of PLC which is involved in the Fc gamma R-mediated intracellular killing of S. aureus by human monocytes.

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“…First, it has been noticed that a part of phagocytosis can be Ca 2+ -dependent, at least in human neutrophils [56][57][58]. Ca 2+ would act as a second messenger for phagocytosis and superoxide anion formation [59]. The disruption in intracellular transport caused by ionomycin may thus alter this immune function.…”

Section: Chemical Stress Induced Different Effectsmentioning

confidence: 99%