scholarly journals The type II "receptor" as a decoy target for interleukin 1 in polymorphonuclear leukocytes: characterization of induction by dexamethasone and ligand binding properties of the released decoy receptor.

1994 ◽  
Vol 179 (2) ◽  
pp. 739-743 ◽  
Author(s):  
F Re ◽  
M Muzio ◽  
M De Rossi ◽  
N Polentarutti ◽  
J G Giri ◽  
...  
Keyword(s):  
Polymorphonuclear Leukocytes ◽  
Interleukin 1 ◽  
Soluble Form ◽  
Type I ◽  
Type Ii ◽  
Membrane Expression ◽  
Binding Properties ◽  
Signaling Function ◽  
Human Polymorphonuclear Leukocytes

Whereas the signaling function of the interleukin 1 (IL-1) receptor type I (IL-1R I) has been well documented, the type II "receptor" has been suggested to act as a decoy target for this cytokine. Since IL-1 may represent a key target of the immunomodulatory and antiinflammatory properties of glucocorticoids (GC), the aim of this study was to investigate the effects of dexamethasone (Dex) on IL-1R expression in human polymorphonuclear leukocytes (PMN), which express predominantly the type II molecule (IL-1R II). We found that Dex augments the levels of steady state transcripts encoding the IL-1R I and, most prominently, those of IL-1R II. Dex induced both transcripts via transcription-dependent mechanisms and by prolongation of the mRNAs half-lives. Inhibition of protein synthesis superinduced basal and Dex-augmented IL-1R II mRNA, whereas it completely inhibited the induction by Dex of IL-1R I transcripts. Induction of IL-1R II mRNA by Dex was associated with augmented membrane expression and release of the type II IL-1 binding molecule. This effect was mediated by the GC receptor. Other steroids (17 beta-estradiol, progesterone, and testosterone) were ineffective. The concentrations of IL-1 alpha and IL-1 receptor antagonist required to displace the binding of IL-1 beta to the soluble form of the decoy molecule induced by Dex from PMN were, respectively, 100 and 2 times higher compared with IL-1 beta. The induction by Dex of the type II receptor, a decoy molecule for IL-1, may contribute to the immunosuppressive and antiinflammatory activities of Dex.

Characterization of the human interleukin 1 receptor on human polymorphonuclear leukocytes

1988 ◽  
Vol 48 (3) ◽  
pp. 354-361 ◽  
Author(s):  
J.A. Rhyne ◽  
S.B. Mizel ◽  
R.G. Taylor ◽  
M. Chedid ◽  
C.E. McCall
Keyword(s):  
Polymorphonuclear Leukocytes ◽  
Interleukin 1 ◽  
Human Polymorphonuclear Leukocytes

scholarly journals Independent binding of interleukin-1 alpha and interleukin-1 beta to type I and type II interleukin-1 receptors.

1993 ◽  
Vol 268 (4) ◽  
pp. 2513-2524
Author(s):  
J. Slack ◽  
C.J. McMahan ◽  
S. Waugh ◽  
K. Schooley ◽  
M.K. Spriggs ◽  
...  
Keyword(s):  
Interleukin 1 ◽  
Type I ◽  
Type Ii ◽  
Interleukin 1 Beta

scholarly journals A chimeric type II/type I interleukin-1 receptor can mediate interleukin-1 induction of gene expression in T cells

1993 ◽  
Vol 268 (14) ◽  
pp. 10490-10494
Author(s):  
A. Heguy ◽  
C.T. Baldari ◽  
S. Censini ◽  
P. Ghiara ◽  
J.L. Telford
Keyword(s):  
Gene Expression ◽  
T Cells ◽  
Interleukin 1 ◽  
Type I ◽  
Type Ii

Interleukin-1 alpha stimulates dopamine release by activating type II protein kinase A in PC-12 cells

1995 ◽  
Vol 269 (6) ◽  
pp. E1083-E1088
Author(s):  
A. Joseph ◽  
A. Kumar ◽  
N. A. O'Connell ◽  
R. K. Agarwal ◽  
A. R. Gwosdow
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Dopamine Release ◽  
Interleukin 1 ◽  
Intracellular Camp ◽  
Type I ◽  
Camp Accumulation ◽  
Type Ii ◽  
Pc 12 Cells ◽  
Kinase A

A recent study from this laboratory [A. R. Gwosdow, N. A. O'Connell, and A. B. Abou-Samra. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E461-E466, 1992] showed that the inflammatory mediator interleukin-1 alpha (IL-1 alpha) stimulates catecholamine release from primary cultures of rat adrenal cells. The present studies were conducted to determine whether 1) IL-1 alpha stimulates catecholamine/dopamine release from the adrenal medullary cell line PC-12 and 2) the adenosine 3',5'-cyclic monophosphate (cAMP)-protein kinase A (PKA) pathway is involved in IL-1 alpha-induced dopamine release from PC-12 cells. The results indicate that IL-1 alpha significantly (P < 0.05) elevated dopamine release after a 24-h incubation period. IL-1 alpha did not stimulate cAMP accumulation at any time period between 5 min and 2 h. In contrast, forskolin-treated cells elevated (P < 0.05) intracellular cAMP levels and increased dopamine release. Because IL-1 alpha did not affect cAMP accumulation, the effect of IL-1 alpha on PKA activity was investigated. IL-1 alpha increased (P < 0.05) PKA activity at 15 and 30 min and returned to control levels by 1 h. Forskolin also increased (P < 0.05) PKA activity. The type of PKA activated (P < 0.05) by IL-1 alpha was type II PKA. In contrast, forskolin activated (P < 0.05) type I and type II PKA. Inhibition of PKA with the PKA inhibitor H-8 blocked PKA activity and dopamine secretion by both IL-1 alpha and forskolin in PC-12 cells. These observations demonstrate that 1) IL-1 alpha stimulated dopamine release from PC-12 cells by activating PKA, 2) the mechanism of IL-1 alpha activation of PKA does not involve detectable increases in intracellular cAMP accumulation, and 3) IL-1 alpha activates type II PKA, which is used by IL-1 alpha to stimulate dopamine secretion from PC-12 cells.

Evaluation of an enzyme immunoassay kit for estrogen receptor measurement--report II.

1988 ◽  
Vol 34 (10) ◽  
pp. 2053-2057 ◽  
Author(s):  
S Raam ◽  
D M Vrabel
Keyword(s):  
Enzyme Immunoassay ◽  
Binding Sites ◽  
Solid Phase ◽  
Functional Characterization ◽  
Quantitative Agreement ◽  
Type I ◽  
Type Ii ◽  
Immunoreactive Protein ◽  
Estrogen Binding

Abstract We present evidence to show that monoclonal antibodies to estrogen receptors (ER) in solid phase recognize the secondary estrogen binding sites with moderate to low affinity for estradiol (E2). An excellent quantitative agreement was found in five cytosols between the ER values obtained by the enzyme immunoassay (ER-EIA) and the amount of secondary estrogen binding sites measured by the assay involving dextran-coated charcoal (Clin Chem 1986;32:1496). The immunoreactive protein recognized by the antibody-coated beads, when allowed to react with ER(+) cytosols, is shown to bind [3H]estradiol only when the ligand concentration exceeds 8 nmol/L. Further biochemical and functional characterization of the immunoreactive protein is required to establish similarities/dissimilarities between this protein, high-affinity Type I ER sites, and the secondary sites such as Type II sites.

Human aortic endothelial cells express the type I but not the type II receptor for interleukin-1 (IL-1)

1992 ◽  
Vol 153 (3) ◽  
pp. 583-588 ◽  
Author(s):  
Ann L. Akeson ◽  
Laura B. Mosher ◽  
Connie W. Woods ◽  
Kendra K. Schroeder ◽  
Terry L. Bowlin
Keyword(s):  
Endothelial Cells ◽  
Interleukin 1 ◽  
Type I ◽  
Type Ii ◽  
Aortic Endothelial Cells ◽  
Human Aortic Endothelial Cells ◽  
Aortic Endothelial

scholarly journals Release of a Potent Polymorphonuclear Leukocyte Chemoattractant Is Regulated by White-Opaque Switching in Candida albicans

2004 ◽  
Vol 72 (2) ◽  
pp. 667-677 ◽  
Author(s):  
Jeremy Geiger ◽  
Deborah Wessels ◽  
Shawn R. Lockhart ◽  
David R. Soll
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Candida Albicans ◽  
Mating Type ◽  
Related Species ◽  
Polymorphonuclear Leukocytes ◽  
White Phase ◽  
Bona Fide ◽  
Human Polymorphonuclear Leukocytes ◽  
Cell Chemotaxis

ABSTRACT Previous studies employing transmembrane assays suggested that Candida albicans and related species, as well as Saccharomyces cerevisiae, release chemoattractants for human polymorphonuclear leukocytes (PMNs). Because transmembrane assays do not definitively distinguish between chemokinesis and chemotaxis, single-cell chemotaxis assays were used to confirm these findings and test whether mating-type or white-opaque switching affects the release of attractant. Our results demonstrate that C. albicans, C. dubliniensis, C. tropicalis, C. parapsilosis, and C. glabrata release bona fide chemoattractants for PMNs. S. cerevisiae, however, releases a chemokinetic factor but not a chemoattractant. Characterization of the C. albicans chemoattractant revealed that it is a peptide of approximately 1 kDa. Whereas the mating type of C. albicans did not affect the release of chemoattractant, switching did. White-phase cells released chemoattractant, but opaque-phase cells did not. Since the opaque phase of C. albicans represents the mating-competent phenotype, it may be that opaque-phase cells selectively suppress the release of chemoattractant to facilitate mating.

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