Stimulation and priming of human neutrophils by interleukin-8: cooperation with tumor necrosis factor and colony-stimulating factors

Interleukin-8 (IL-8) stimulated an increase in cytoplasmic-free Ca2+ ([Ca2+]i) and intracellular pH (pHi) in parallel at low concentrations (0.5 to 5 ng/mL), and stimulated O2- release and membrane depolarization in parallel at high concentrations (50 to 5,000 ng/mL). IL-8-induced O2- release was potentiated by tumor necrosis factor (TNF), granulocyte-macrophage colony-stimulating factor (GM-CSF), and granulocyte-CSF (G-CSF) in a dose-dependent manner, whereas it was inhibited by cyclic AMP agonists. These characteristics and the time- courses of the responses stimulated by IL-8 were similar to those stimulated by N-formyl-methionyl-leucyl-phenylalanine (FMLP), except that the cells stimulated by IL-8 showed shorter duration and less magnitude in some responses. In addition, IL-8 was found to be a potent priming agent and to enhance O2- release stimulated by FMLP. The priming effect of IL-8 was very rapid and was maximal within 5 minutes of preincubation. The dose-response curves for priming were identical to those for triggering of an increase in [Ca2+]i and pHi. The potency of the maximal priming effects on FMLP-induced O2- release was TNF greater than GM-CSF greater than IL-8 greater than G-CSF. The combination of IL-8 and the suboptimal concentrations of TNF or GM-CSF resulted in the additive priming effect, whereas the combination of the optimal concentration of IL-8 and the optimal concentration of TNF, GM- CSF, or G-CSF resulted in the effect of more potent priming agent alone. These findings suggest that IL-8 stimulates or primes human neutrophils according to its concentrations and cross-talks with TNF, GM-CSF, G-CSF, or FMLP at the inflammatory sites.

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Stimulation and priming of human neutrophils by interleukin-8: cooperation with tumor necrosis factor and colony-stimulating factors

Blood ◽

10.1182/blood.v78.10.2708.2708 ◽

1991 ◽

Vol 78 (10) ◽

pp. 2708-2714 ◽

Cited By ~ 94

Author(s):

A Yuo ◽

S Kitagawa ◽

T Kasahara ◽

K Matsushima ◽

M Saito ◽

...

Keyword(s):

Tumor Necrosis Factor ◽

Priming Effect ◽

Tumor Necrosis ◽

Optimal Concentration ◽

Interleukin 8 ◽

Human Neutrophils ◽

Dependent Manner ◽

Response Curves ◽

Gm Csf ◽

Necrosis Factor

Abstract Interleukin-8 (IL-8) stimulated an increase in cytoplasmic-free Ca2+ ([Ca2+]i) and intracellular pH (pHi) in parallel at low concentrations (0.5 to 5 ng/mL), and stimulated O2- release and membrane depolarization in parallel at high concentrations (50 to 5,000 ng/mL). IL-8-induced O2- release was potentiated by tumor necrosis factor (TNF), granulocyte-macrophage colony-stimulating factor (GM-CSF), and granulocyte-CSF (G-CSF) in a dose-dependent manner, whereas it was inhibited by cyclic AMP agonists. These characteristics and the time- courses of the responses stimulated by IL-8 were similar to those stimulated by N-formyl-methionyl-leucyl-phenylalanine (FMLP), except that the cells stimulated by IL-8 showed shorter duration and less magnitude in some responses. In addition, IL-8 was found to be a potent priming agent and to enhance O2- release stimulated by FMLP. The priming effect of IL-8 was very rapid and was maximal within 5 minutes of preincubation. The dose-response curves for priming were identical to those for triggering of an increase in [Ca2+]i and pHi. The potency of the maximal priming effects on FMLP-induced O2- release was TNF greater than GM-CSF greater than IL-8 greater than G-CSF. The combination of IL-8 and the suboptimal concentrations of TNF or GM-CSF resulted in the additive priming effect, whereas the combination of the optimal concentration of IL-8 and the optimal concentration of TNF, GM- CSF, or G-CSF resulted in the effect of more potent priming agent alone. These findings suggest that IL-8 stimulates or primes human neutrophils according to its concentrations and cross-talks with TNF, GM-CSF, G-CSF, or FMLP at the inflammatory sites.

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Effect Of Montelukast On The Production Of Interleukin-8 And Tumor Necrosis Factor By Human Neutrophils Activated With The Chemoattractant, FMLF, And The Cysteinyl Leukotriene, LTD4, Individually And In Combination

10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a4073 ◽

2011 ◽

Author(s):

Charles Feldman ◽

Annette J. Theron ◽

Helen C. Steel ◽

Corli Gravett ◽

Ronald Anderson

Keyword(s):

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Interleukin 8 ◽

Human Neutrophils ◽

Cysteinyl Leukotriene ◽

Necrosis Factor

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Tumor necrosis factor-α-mediated signal transduction in human neutrophils: Involvement of sphingomyelin metabolites in the priming effect of tnf-α on the fMLP-stimulated superoxide production

Life Sciences ◽

10.1016/s0024-3205(99)00587-1 ◽

1999 ◽

Vol 66 (3) ◽

pp. 245-256 ◽

Cited By ~ 31

Author(s):

Masayuki Niwa ◽

Osamu Kozawa ◽

Hiroyuki Matsuno ◽

Yutaka Kanamori ◽

Akira Hara ◽

...

Keyword(s):

Signal Transduction ◽

Tumor Necrosis Factor ◽

Priming Effect ◽

Tumor Necrosis ◽

Tumor Necrosis Factor Α ◽

Superoxide Production ◽

Human Neutrophils ◽

Tnf Α ◽

Factor Α ◽

Necrosis Factor

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INTERFERON-?? AND BACTERIAL LIPOPOLYSACCHARIDE ACT SYNERGISTICALLY ON HUMAN NEUTROPHILS ENHANCING INTERLEUKIN-8, INTERLEUKIN-1??, TUMOR NECROSIS FACTOR-??, AND INTERLEUKIN-12 P70 SECRETION AND PHAGOCYTOSIS VIA UPREGULATION OF TOLL-LIKE RECEPTOR 4

Shock ◽

10.1097/01.shk.0000239765.80033.37 ◽

2007 ◽

Vol 27 (3) ◽

pp. 226-231 ◽

Cited By ~ 22

Author(s):

Michal Pearl-Yafe ◽

Ina Fabian ◽

Drora Halperin ◽

Edith Flatau ◽

Sara Werber ◽

...

Keyword(s):

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Interleukin 1 ◽

Interleukin 8 ◽

Bacterial Lipopolysaccharide ◽

Interleukin 12 ◽

Human Neutrophils ◽

Toll Like Receptor ◽

Toll Like Receptor 4 ◽

Necrosis Factor

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Tumor necrosis factor primes neutrophils for hypochlorous acid production

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.1989.257.6.l338 ◽

1989 ◽

Vol 257 (6) ◽

pp. L338-L345 ◽

Cited By ~ 2

Author(s):

Z. W. She ◽

M. D. Wewers ◽

D. J. Herzyk ◽

A. L. Sagone ◽

W. B. Davis

Keyword(s):

Tumor Necrosis Factor ◽

Tumor Necrosis ◽

Cytochalasin B ◽

Hypochlorous Acid ◽

Tnf Alpha ◽

Human Neutrophils ◽

Dependent Manner ◽

Lag Period ◽

Dose Dependent ◽

Necrosis Factor

Tumor necrosis factor (TNF) has a weak direct effect on neutrophil oxidative metabolism and primes neutrophils for oxidant release in response to other stimuli. We examined the effect of recombinant human TNF alpha (rTNF alpha) on production of hypochlorous acid (HOCl) by human neutrophils. TNF alone, even at concentrations of 1,000 U/ml, did not stimulate HOCl production. In contrast, rTNF alpha, in a dose-dependent manner, primed neutrophils for HOCl production in response to the weak agent unopsonized zymosan. rTNF alpha concentrations as low as 10 U/ml resulted in a fivefold increase in HOCl in this system. rTNF alpha-primed cells also exhibited increased phagocytosis. Priming in this model system occurred regardless of whether cells were preincubated with rTNF alpha before addition of zymosan or coincubated with both rTNF alpha and zymosan. rTNF alpha priming for HOCl production could not be washed away and required a lag period of approximately 10 min. rTNF alpha priming was not dependent on extracellular Ca2+ and Mg2+. Preincubation experiments demonstrated that rTNF alpha priming was not inhibited by the microfilament blocker cytochalasin B. Although the mechanism remains unclear, these findings demonstrate that rTNF alpha has an important priming effect on the neutrophil myeloperoxidase pathway.

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