Recombinant interleukin-1β stimulates eicosanoid production in rat primary culture astrocytes

Hartung, Hans‐Peter; ̈fer, Ba ̈rbel Scha; Heininger, Kurt; Toyka, Klaus V.

doi:10.1016/0006-8993(89)90013-9

Cited by 79 publications

(32 citation statements)

References 49 publications

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“…In fact, IL-1␤ binding sites have been demonstrated on both astrocytes (Ban et al, 1993;Liu et al, 1994) and endothelia including postcapillary venules in the PVN nuclei and the external layer of the ME (Cunningham et al, 1992;Cunningham and De Souza, 1993;Wong and Licinio, 1994;Ericsson et al, 1995). The presence of IL-1␤ binding sites on astrocytes is consistent with the direct action of IL-1␤ on a variety of astrocyte activities (Giulian and Lachman, 1985;Giulian et al, 1988;Hartung et al, 1989;Chung and Benveniste, 1990;Gadient et al, 1990;Carman-Krzan et al, 1991;Lee et al, 1993;Liu et al, 1996) whereas those expressed on the surface of endothelia may be involved in modulation of blood perfusion rates. In contrast, microglial cells and perivascular cells provide a source of central IL-1␤ under pathological conditions (Nietro-Sampedro and Berman, 1987;Van Dam et al, 1992;Buttini et al, 1994;Yabuuchi et al, 1994) but show no detectable response to IL-1␤ in vitro or in vivo.…”

Section: Discussionmentioning

confidence: 54%

Interleukin-1? immunoreactivity in identified neurons of the rat magnocellular neurosecretory system: Evidence for activity-dependent release

Watt

Hobbs

2000

J. Neurosci. Res.

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Interleukin-1beta has been demonstrated in neurons of the rat hypothalamus, including cells of the magnocellular neurosecretory system and tuberoinfundibular system (Lechan et al., [1990] Brain Res. 514:135-140). Despite its potential importance to regulation of neuroendocrine function, however, neither the specific cell types that express interleukin-1beta or the conditions that may result in its release have yet been described. Therefore, we utilized a combination of immunocytochemical and immunoelectron microscopic localization, in conjunction with Western blot analysis, on normonatremic, hypernatremic, and lactating rats to assess the site of synthesis and potential secretion characteristics of interleukin-1beta in the rat magnocellular neurosecretory system. Interleukin-1beta immunoreactivity was localized within both oxytocin and vasopressin neurons in the paraventricular, supraoptic, accessory and periventricular hypothalamic nuclei. Additionally, interleukin-1beta immunoreactive fibers were localized in the zona interna and zona externa of the median eminence and in the neurohypophysis. Immunoelectron microscopic analysis revealed that interleukin-1beta immunoreactivity is associated with small spherical structures, distinct from neurosecretory granules, in neurosecretory axons within the neurohypophysis. Furthermore, stimulation of heightened neurosecretory activity via chronic osmotic challenge and lactation resulted in a marked diminution in levels of interleukin-1beta immunoreactivity in the neurohypophysis with a subsequent return to normal levels after cessation of the stimuli. Western blot analysis confirmed the existence of interleukin-1beta protein in the neurohypophysis and provided further evidence for reduction in levels of IL-1beta immunoreactivity after stimulation of secretory activity. These results suggest an endogenous neuronal source of interleukin-1beta exists within the rat magnocellular neurosecretory system under normal physiological conditions. The potential for activity-dependent release of IL-1beta and implications for the involvement of interleukin-1beta in regulation of neurosecretory activity are discussed.

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Section: Discussionmentioning

confidence: 54%

Interleukin-1? immunoreactivity in identified neurons of the rat magnocellular neurosecretory system: Evidence for activity-dependent release

Watt

Hobbs

2000

J. Neurosci. Res.

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“…In addition, the cytokine interleukin-1␤ has been shown to elicit TXA 2 release from astrocytes (45). Thus, a variety of physiological and pathophysiological conditions could lead to the exposure of oligodendrocytes to TXA 2 .…”

Section: Discussionmentioning

confidence: 99%

The Identification and Characterization of Oligodendrocyte Thromboxane A2 Receptors

Blackman¹,

Dawson²,

Antonakis³

et al. 1998

Journal of Biological Chemistry

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The presence of functional thromboxane A 2 receptors in neonatal rat oligodendrocytes and human oligodendroglioma cells was investigated using immunocytochemistry, ligand affinity chromatography, radioligand binding analysis, immunoblot analysis, and calcium mobilization studies. Immunocytochemical studies revealed the presence of receptor protein on both oligodendrocytes and human oligodendroglioma cells. Ligand affinity chromatography allowed for the purification of a protein with an electrophoretic mobility (55 kDa) indistinguishable from human platelet thromboxane A 2 receptors. This affinity purified protein was immunoreactive against a polyclonal anti-thromboxane A 2 receptor antibody. Intact human oligodendroglioma cells specifically bound Thromboxane A 2 (TXA 2 ) 1 is a bioactive arachidonic acid metabolite with thrombotic, vasospastic, and bronchospastic properties (1-3). It has been implicated in a variety of physiological and pathophysiological states (4). The receptor for TXA 2 has been purified (5, 6), cloned, and sequenced, and the structure of the gene indicates that this receptor is a member of the seven transmembrane domain, G-protein-coupled receptor superfamily. The receptor protein has been located in a variety of tissues including blood platelets (7), vascular smooth muscle (8, 9), vascular endothelium (10), placenta (11), and kidney (12) and appears to be directly involved in the regulation of intracellular calcium levels (13). In this regard, previous studies have provided evidence that the TXA 2 receptor protein is coupled to at least one G-protein, i.e. G q in platelets (14, 15) and astrocytes (16), and appears to modulate phospholipase C-␤ activity resulting in activation of the inositol triphosphate second messenger system (17, 18).Although highly specific agonists and antagonists have proven to be of significant value in characterizing TXA 2 receptors in a number of different cell lines, little information is currently available concerning their existence or function in the central nervous system. To a large extent, this has been due to the presence of high lipid concentrations in central nervous system tissue. Thus, nonspecific binding has obscured the demonstration of receptor binding in solubilized brain, due to the lipophilic nature of TXA 2 receptor ligands. In addition, the heterogeneity of cell types in the central nervous system has complicated attempts at receptor localization at a cellular level.Based on these limitations, previous studies have employed cultured cell systems in an effort to investigate the presence of TXA 2 receptors in the central nervous system. In these experiments, it was demonstrated that cultured rabbit astrocytes were capable of specifically binding the TXA 2 ligand ONO . These results, therefore, provided evidence that at least one cellular component of the central nervous system possesses TXA 2 receptor activity. However, since astrocytes are ubiquitously distributed in the brain, it has not been possible to ascribe a specific or unique function for...

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“…Since rapid activation of PKC occurs in endothelial cells upon stimulation with thrombin, 20,21 and since PMA is a direct activator of PKC, it may be reasonable to speculate that the cellular mechanisms of IL-8 production by thrombin and PMA have common points, especially downstream of PKC activation. There is argument [22][23][24] as to whether PKC is involved in cellular signallings by IL-1b. However, PKC is seemingly not involved in IL-8 production by IL-1b, since calphostin-C did not affect the action of IL-1b.…”

Section: Discussionmentioning

confidence: 99%

Thrombin stimulates production of interleukin‐8 in human umbilical vein endothelial cells

et al. 1996

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SUMMARYInterleukin-8 (IL-8) is regarded as an important mediator of inflammation because of its potent and specific chemotactic activity on neutrophils. In the present investigation, human umbilical vein endothelial cells (HUVEC) stimulated with thrombin were found to produce IL-8, in a dose-and timedependent manner. After stimulation with 10 U/ml thrombin for 24 hr, the level of IL-8 in the conditioned medium was 14 ng/ml, or enough to elicit PMN chemotaxis in vitro. Northern blot analysis revealed that thrombin as well as IL-1b elevates the level of IL-8 mRNA preceding the formation of IL-8 protein.A synthetic peptide SFLLRN [human thrombin receptor-activating peptide (TRAP)] was found to mimic the action of thrombin. Preincubation with anti-thrombin compounds such as hirudin and antithrombin-III-heparin almost completely suppressed the action of thrombin without affecting the actions of other stimuli including IL-1b, phorbol 12-myristate 13-acetate (PMA) and TRAP. Diisopropylfluorophosphate-treated thrombin did not stimulate IL-8 production. Calphostin-C, a protein kinase C (PKC) inhibitor, attenuated the production of IL-8 by thrombin, TRAP and PMA, but left the action of IL-1b unchanged. These results strongly suggest that catalytic activation of thrombin receptor by thrombin results in PKC-dependent IL-8 production accompanied by an increase in IL-8 mRNA level.

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Recombinant interleukin-1β stimulates eicosanoid production in rat primary culture astrocytes

Cited by 79 publications

References 49 publications

Interleukin-1? immunoreactivity in identified neurons of the rat magnocellular neurosecretory system: Evidence for activity-dependent release

Interleukin-1? immunoreactivity in identified neurons of the rat magnocellular neurosecretory system: Evidence for activity-dependent release

The Identification and Characterization of Oligodendrocyte Thromboxane A2 Receptors

Thrombin stimulates production of interleukin‐8 in human umbilical vein endothelial cells

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