The mechanisms of serum‐treated zymosan (STZ)‐induced oxidative metabolism by human eosinophils and the effects of IL‐5 priming

Woschnagg, Charlotte; García, Rafael Martínez

doi:10.1034/j.1398-9995.2001.00898.x

Cited by 6 publications

(6 citation statements)

References 46 publications

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“…The present work has shown that superoxide production by equine eosinophils in response to IL-5 of either equine or human origin, like that induced by histamine [12], appears to be dependent on PKC as Ro31-8220 significantly inhibited the response. This agrees with findings in human eosinophils using IL-5 [18] and STZ [19].…”

Section: Discussionsupporting

confidence: 82%

“…Similarly, conventional PKCs appear to be involved in regulating the adherence of equine eosinophils in response to human IL-5. The concentrations of Gö6976 required for effective inhibition were higher than the IC 50 reported for inhibition in a cell-free system [22], but others have also reported that mM concentrations are necessary to inhibit human eosinophil function [16,19,20]. The inhibitory effects of Gö6976 on equine eosinophil function are also consistent with the report that PKCa is involved in H1 receptor signalling in CHO cells transfected with bovine H1 receptors [27] and with the finding that, in activated cells, PKCb associates with the signal transducing beta chain of the IL-5 receptor [28].…”

Section: Discussionmentioning

confidence: 92%

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The role of protein kinase C in regulating equine eosinophil adherence and superoxide production

et al. 2005

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 92%

The role of protein kinase C in regulating equine eosinophil adherence and superoxide production

et al. 2005

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“…An interesting observation regarding staurosporine was made in a study on eosinophil oxidative metabolism by Woschnagg et al. where this inhibitor had a priming‐like effect on zymosan‐induced oxidative metabolism (10). This phenomenon was not observed when using PMA as an inducer (39).…”

Section: Discussionmentioning

confidence: 99%

“…Several inhibitors have been found to interfere with signal transduction in eosinophils and antagonize the function of these cells. Many of these inhibitors are directed against general signalling molecules in granulocytes including PI3‐kinase (Wortmannin and LY294002), protein kinase C (Staurosporine, Gö6976), protein tyrosine kinases (Genistein) and mitogen‐activated protein kinase (MEK) (PD98059) (10–16).…”

mentioning

confidence: 99%

C3b‐induced eosinophil degranulation involves PI3‐kinases and is inhibited by protein kinase C activity

Carlson¹,

Lampinen²

2010

APMIS

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Selective release of individual eosinophil granule proteins has been demonstrated in eosinophilic conditions and in vitro using different stimuli. The aim of this study was to investigate if selective release of eosinophil cationic protein (ECP), eosinophil protein X/eosinophil derived-neurotoxin (EPX/EDN) and eosinophil peroxidase (EPO) could be due to the involvement of different signal transduction pathways. Peripheral blood granulocytes from healthy donors were incubated with Wortmannin, LY294002, Genistein, Staurosporine, GÖ6976 or PD98059 prior to the induction of degranulation by C3b. The released amounts of ECP, EPO and EPX/EDN were determined by immunoassays, and related to the total cell content of respective protein. Wortmannin caused a significant, dose-dependent inhibition of all three granule proteins. LY294002 (10⁻⁶ M) also inhibited the release of all proteins. Genistein (10⁻⁶ M) inhibited the release of ECP, whereas the release of EPO was increased. However, there was a tendency towards similar concentration-dependent patterns of release of all three proteins. Staurosporine (10⁻⁷ M), GÖ6976 (10⁻⁶ M) and PD98059 (10⁻⁵ M) caused an increased release of the three proteins. PI3-kinases play an important role in the C3b-induced release of ECP, EPO and EPX/EDN, whereas protein kinase C seems to have inhibitory effects on C3b-induced degranulation.

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“…The possibility that IL-2 inhibits PI3-kinase-induced migration was not feasible to investigate by the same approach because of the inhibitory effect of both the PI3-kinase inhibitors and IL-2 on the migration. However, IL-5 is known to induce PI3-kinase activity [18,19,20], and in our previous study the inhibitory effect of IL-2 was counteracted by IL-5 [12]. This may indicate that IL-2 and IL-5 have opposite effects on the PI3-kinase pathway.…”

Section: Discussionmentioning

confidence: 88%

Albumin Stimulation of Eosinophil Migration Involves PI3-Kinases and Is Associated with Diminished Eosinophil CD49d and CD49f Expression

Lampinen

Håkansson²

2006

Int Arch Allergy Immunol

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Background: Albumin is known to induce chemokinesis and facilitate chemotaxis of human granulocytes in the Boyden chamber assay, but its mechanisms of action remain obscure. We have previously found that IL-2 inhibits albumin-stimulated eosinophil migration. The aim of this study was to identify the mechanisms behind the effects of albumin and IL-2 on the migration of human eosinophils. Methods: Purified eosinophils were preincubated with inhibitors of signal transduction molecules before incubation with or without albumin and IL-2. The migration assay was performed in a 48-well microchemotaxis chamber. The effect of albumin and IL-2 on cell size and on the surface expression of adhesion molecules was studied with flow cytometry. Results: Albumin-stimulated migration was inhibited by the PI3-kinase inhibitors wortmannin and LY-294002, but not by the PKC inhibitor RO-31-8220. IL-2 had no effect after preincubation with wortmannin or LY-294002. In contrast, the inhibitory effect of IL-2 remained after preincubation with RO-31-8220. Albumin increased the cell size as measured by forward scatter, and the expression of CD49d and CD49f decreased after incubation with albumin. IL-2 affected neither the expression of adhesion molecules nor the forward scatter. Conclusions: The stimulation of eosinophil migration by albumin is mediated by PI3-kinase, and the increase in cell size caused by albumin indicates activation of the cells. Decreased expression of CD49d and CD49f by albumin may diminish the adhesiveness of the cells, which in turn may facilitate migration. These are novel findings that indicate an active role for albumin in eosinophil migration.

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The mechanisms of serum‐treated zymosan (STZ)‐induced oxidative metabolism by human eosinophils and the effects of IL‐5 priming

Cited by 6 publications

References 46 publications

The role of protein kinase C in regulating equine eosinophil adherence and superoxide production

The role of protein kinase C in regulating equine eosinophil adherence and superoxide production

C3b‐induced eosinophil degranulation involves PI3‐kinases and is inhibited by protein kinase C activity

Albumin Stimulation of Eosinophil Migration Involves PI3-Kinases and Is Associated with Diminished Eosinophil CD49d and CD49f Expression

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