A comparison of the priming effect of phorbol myristate acetate and phorbol dibutyrate on fMet-Leu-Phe-induced oxidative burst in human neutrophils

Gaudry, Muriel; Combadière, Christophe; Marquetty, Claude; Hakim, Jacques

doi:10.1016/0162-3109(90)90006-z

Cited by 11 publications

(4 citation statements)

References 35 publications

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“…An earlier study (33) and findings from this study show that PDBu, in contrast to PMA, up-regulated CD32A-dependent ligand-binding function. Although these two phorbol esters have been shown to transduce similar signals in many cell types, differences in their action on neutrophils have been reported (49,50). It has been shown that PMA and PDBu differ in their use of cytosolic protein kinase C in generating superoxide anion in neutrophils (49).…”

Section: Discussionmentioning

confidence: 99%

“…PDBu and PMA also differ in their ability to prime neutrophils for fMLP-induced superoxide anion generation (49). The difference in priming has been attributed to the specific effect of PDBu on fMLP binding to its receptor (50). Although, at present, the mechanisms underlying the opposing effects of these two phorbol esters on Fc␥Rs are not clear, these previous reports on the difference in signaling to neutrophils by PMA and PDBu suggest that the differential effect of phorbol esters have on Fc␥Rs ligand binding could be due to the difference in signaling mechanisms.…”

Section: Discussionmentioning

confidence: 99%

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Signal-Specific Activation and Regulation of Human Neutrophil Fcγ Receptors

Nagarajan

Fifadara

Selvaraj

2005

The Journal of Immunology

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FcγRs with the ITIM domain have been shown to regulate the inflammatory signal delivered by the ITAM-containing FcγRs. In this study, we demonstrate that the function of human neutrophil FcγR type IIA (CD32A) is regulated in a distinct manner by different cell activation signals at the ligand-binding stage. Activation of neutrophils with fMLP up-regulated the ligand-binding function of CD32A, whereas PMA-mediated activation completely abolished ligand binding without altering CD32A expression. Furthermore, PMA treatment also abolished CD16B-dependent ligand binding irrespective of the level of expression. The effect of PMA was cell type specific, because the ligand-binding function of CD32A expressed on cultured cells such as K562 and CHO-CD32A transfectants was not affected by PMA. Interestingly, phorbol 12,13-dibutyrate, another phorbol ester, and IL-8 up-regulated CD32A-dependent ligand-binding function. These results demonstrate that regulation of CD32A-dependent ligand binding in human neutrophils is not only cell type specific but also activation signal specific. Moreover, these results suggest the possibility that signals delivered to neutrophils by various inflammatory stimuli can exert opposing effects on the function of human FcγRs, representing a novel inside-out regulatory mechanism of FcγR ligand binding.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Signal-Specific Activation and Regulation of Human Neutrophil Fcγ Receptors

Nagarajan

Fifadara

Selvaraj

2005

The Journal of Immunology

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“…However, it is known that divalent cations (especially calcium ions) play an important regulatory role in a variety of cell types and an increase in intracellular calcium levels is a key element in stimulus-response coupling [39] , particularly in PMN activation [40][41][42] .…”

Section: Discussionmentioning

confidence: 99%

Anti-Inflammatory Activity of Thymol: Inhibitory Effect on the Release of Human Neutrophil Elastase

et al. 2006

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Elastase, a serine proteinase released by activated human neutrophils, can degrade a wide variety of biomacromolecules including elastin, and is considered a marker of inflammatory diseases. As the logical strategy to protect tissue is to inhibit excessive elastase activity, experimental and clinical researches have concentrated on trying to find efficient elastase inhibitors. As thymol, one of the major components of thyme oil with a phenolic structure, has been credited with a series of pharmacological properties, that include antimicrobial and antioxidant effects, the aim of this study was to explore whether it can also interfere with the release of elastase by human neutrophils stimulated with the synthetic chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine (fMLP). After the neutrophils were incubated with increasing amounts of thymol (2.5, 5, 10, 20 µg/ml), elastase release was initiated by fMLP and measured using MeO-Suc-Ala-Ala-Pro-Val-MCA. The results showed that thymol inhibited fMLP-induced elastase release in a concentration-dependent manner, with the effects of 10 and 20 µg/ml being statistically significant. The behavior of cytosolic calcium mobilization revealed by fura-2 closely resembled that of elastase, thus suggesting that they may be related. The hydrophobic nature of thymol means that it can approach ion channel proteins through the lipid phase of the membrane, alter the local environment of calcium channels and thus inhibit capacitative calcium entry. In brief, thymol inactivates calcium channels machinery, thus triggering a corresponding reduction in elastase. The antibacterial and antimycotic activity of thymol is already well known, but our findings that it inhibits elastase extend our knowledge of the anti-inflammatory activity of this interesting molecule that is already credited with antioxidant activity. These two latter characteristics make thymol a molecule that can have helpful effects in controlling the inflammatory processes present in many infections.

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“…The intracellular signalling pathways and mechanisms that regulate the function of human PMNs responses to pro-inflammatory stimuli are only partially understood, but it is known that divalent cations (especially calcium ions) play an important regulatory role in a variety of cell types and that increased intracellular calcium levels is a key element of stimulusresponse coupling [Suda et al 2005], particularly in PMN activation [Gandry et al 1990;Lew et al 1985Lew et al , 1984. The intracellular release of calcium depletes the level of stored calcium, and this simultaneously triggers calcium influx by increasing membrane permeability, thus restoring the intracellular calcium level [Khalfi et al 1996;Truett et al 1988].…”

Section: Discussionmentioning

confidence: 99%

Effects of sulphurous water on human neutrophil elastase release

Braga

Sasso

Culici

et al. 2010

Ther Adv Respir Dis

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Previous claims concerning the activity of sulphurous water have been based on the patients' subjective sense of wellbeing and on symptomatic (or general) clinical improvements that are not easy to define or quantify exactly. Our findings indicate that, in addition to its known mucolytic and antioxidant activity, sulphurous water also has an anti-elastase activity that may help to control the inflammatory processes of upper and lower airway diseases.

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A comparison of the priming effect of phorbol myristate acetate and phorbol dibutyrate on fMet-Leu-Phe-induced oxidative burst in human neutrophils

Cited by 11 publications

References 35 publications

Signal-Specific Activation and Regulation of Human Neutrophil Fcγ Receptors

Signal-Specific Activation and Regulation of Human Neutrophil Fcγ Receptors

Anti-Inflammatory Activity of Thymol: Inhibitory Effect on the Release of Human Neutrophil Elastase

Effects of sulphurous water on human neutrophil elastase release

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