In-vitro enhancement of leukotriene B4 receptor expression on human neutrophils by cefadroxil

1990 ◽  
Vol 25 (4) ◽  
pp. 613-620 ◽  
Author(s):  
J. Knöller ◽  
J. Brom ◽  
W. Schönfeld ◽  
W. König
Keyword(s):  
Leukotriene B4 ◽  
Receptor Expression ◽  
Human Neutrophils ◽  
Leukotriene B4 Receptor

scholarly journals Pneumolysin Potentiates Production of Prostaglandin E2 and Leukotriene B4 by Human Neutrophils

2001 ◽  
Vol 69 (5) ◽  
pp. 3494-3496 ◽  
Author(s):  
Riana Cockeran ◽  
Helen C. Steel ◽  
Timothy J. Mitchell ◽  
Charles Feldman ◽  
Ronald Anderson
Keyword(s):  
Prostaglandin E2 ◽  
Inflammatory Responses ◽  
Pneumococcal Infection ◽  
Leukotriene B4 ◽  
Human Neutrophils ◽  
Prostaglandin E ◽  
Calcium Dependent

ABSTRACT Exposure to pneumolysin (8.37 and 41.75 ng/ml) caused a calcium-dependent increase in the generation of prostaglandin E2 and leukotriene B4 by both resting and chemoattractant-activated human neutrophils in vitro. These interactions of pneumolysin with neutrophils may result in dysregulation of inflammatory responses during pneumococcal infection.

L-selectin function is required for beta 2-integrin-mediated neutrophil adhesion at physiological shear rates in vivo

1992 ◽  
Vol 263 (4) ◽  
pp. H1034-H1044 ◽  
Author(s):  
U. H. Von Andrian ◽  
P. Hansell ◽  
J. D. Chambers ◽  
E. M. Berger ◽  
I. Torres Filho ◽  
...  
Keyword(s):  
Neutrophil Function ◽  
Leukotriene B4 ◽  
Human Neutrophils ◽  
Neutrophil Adhesion ◽  
Shear Rates ◽  
Sequence Of Events ◽  
Multistep Process ◽  
Beta 2

In vivo interactions between neutrophils and endothelial cells (EC) follow a multistep process involving two distinct neutrophil adhesion receptors. L-selectin, constitutively functional on resting neutrophils, mediates an activation-independent primary interaction resulting in rolling along the venular wall. Subsequent activation of rolling neutrophils induces upregulation and functional activation of beta 2-integrins (CD11/CD18) leading to firm attachment. Based on previous findings we hypothesized that, under shear force, rolling may be essential for successful neutrophil-EC recognition. Here we report results of our studies of human neutrophil behavior in interleukin (IL)-1-activated rabbit mesentery venules, an interaction that requires both L-selectin and beta 2-integrins. Rolling of human neutrophils is L-selection mediated; it was strongly reduced by monoclonal antibody inhibition or enzymatic removal of L-selectin. Furthermore, activation induced L-selectin shedding and, in a dose- and time-dependent fashion, rendered neutrophils unable to recognize inflamed EC despite expression of active beta 2-integrins, which promoted adhesion in vitro. Neutrophils activated for 5 min or longer lost most of their ability to roll. However, 1-3 min after activation, rolling was reduced (not abolished), and cells that were still able to roll displayed a significant tendency for a CD18-dependent transition from rolling to sticking. The whole sequence of events, rolling, sticking, and transendothelial migration, could be observed if an extravascular chemotactic stimulus was applied by superfusing mesenteries with leukotriene B4. Under such conditions, sticking and emigration was blocked when rolling was inhibited by enzymatic removal of L-selectin. Our results indicate that primary neutrophil interaction with inflamed EC through the L-selectin is a prerequisite for neutrophil function at physiological shear rates in vivo.

scholarly journals Identification and characterization of specific receptors for monocyte-derived neutrophil chemotactic factor (MDNCF) on human neutrophils.

1989 ◽  
Vol 169 (3) ◽  
pp. 1185-1189 ◽  
Author(s):  
A K Samanta ◽  
J J Oppenheim ◽  
K Matsushima
Keyword(s):  
Human Peripheral Blood ◽  
Platelet Activating Factor ◽  
Leukotriene B4 ◽  
Chemotactic Factor ◽  
Single Type ◽  
Human Neutrophils ◽  
Scatchard Analysis ◽  
Specific Receptors ◽  
Neutrophil Chemotactic Factor

Specific receptors for a recently purified and cloned monocyte-derived neutrophil chemotactic factor (MDNCF) have been identified on the surface of normal human peripheral blood neutrophils using 125I-labeled recombinant human MDNCF (125I-MDNCF). Competitive binding of 125I-MDNCF to human neutrophils reached a maximal level at 1-3 h at 4 degrees C. The Scatchard analysis showed that there are approximately 20,000 receptors per cell with a single type of high affinity binding (Kd, 8 x 10(-10) M). The receptors for MDNCF are clearly distinct from the receptors for other cytokines and chemotactic agents, e.g., IL-1 alpha, TNF-alpha, and FMLP, C5a, leukotriene B4, and platelet activating factor. Based on the SDS-PAGE analysis of chemically crosslinked 125I-MDNCF receptor complex, there are two polypeptides that bind MDNCF; the molecular weight of these two MDNCF receptors were estimated to be 67,000 and 59,000. Treatment of a promyelocytic cell line, HL60, with 1.25% DMSO for 5 d in vitro increased the number of receptors up to 7,000 receptors/cell with a Kd of 1.2 x 10(-9) M.

Proinflammatory mediators elicit secretion of the intracellular B-lymphocyte stimulator pool (BLyS) that is stored in activated neutrophils: implications for inflammatory diseases

Blood ◽  
2005 ◽  
Vol 105 (2) ◽  
pp. 830-837 ◽  
Author(s):  
Patrizia Scapini ◽  
Antonio Carletto ◽  
Bernardetta Nardelli ◽  
Federica Calzetti ◽  
Viktor Roschke ◽  
...  
Keyword(s):  
Healthy Subjects ◽  
B Lymphocyte ◽  
De Novo ◽  
Inflammatory Responses ◽  
Leukotriene B4 ◽  
Human Neutrophils ◽  
Immunogold Electron Microscopy ◽  
Proinflammatory Mediators ◽  
B Lymphocyte Stimulator

Abstract We have recently shown that granulocyte–colony-stimulating factor (G-CSF)– and interferon-γ (IFN-γ)–activated human neutrophils accumulate and release remarkable amounts of soluble B-lymphocyte stimulator (BLyS) in vitro. In this study, we provide evidence that neutrophils migrating into skin window exudates (SWEs) developed in healthy volunteers and in patients with rheumatoid arthritis (RA), synthesized, and released BLyS in response to locally produced G-CSF. Accordingly, the concentrations of soluble BLyS in SWEs were significantly more elevated than in serum. Because the levels of SWE BLyS, but not SWE G-CSF, were higher in patients with RA than in healthy subjects, we examined the effect of CXCL8/IL-8, C5a, and other proinflammatory mediators that dramatically accumulate in RA SWEs and in inflamed synovial fluids. We show that CXCL1/GROα, CXCL8/IL-8, C5a, immune complexes, tumor necrosis factor-α (TNF-α), leukotriene B4, N-formyl-methionyl-leucyl-phenylalanine (fMLP), and lipopolysaccharide (LPS), which by themselves do not induce BLyS de novo synthesis, act as potent secretagogues for BLyS, which is mainly stored in Golgi-related compartments within G-CSF–treated neutrophils, as determined by immunogold electron microscopy. This action is pivotal in greatly amplifying neutrophil-dependent BLyS release in SWEs of patients with RA compared with healthy subjects. Collectively, our data uncover a novel mechanism that might dramatically exacerbate the release of BLyS by neutrophils during pathologic inflammatory responses.

Human monocytes express functional receptors for granulocyte colony– stimulating factor that mediate suppression of monokines and interferon-γ

Blood ◽  
2000 ◽  
Vol 95 (1) ◽  
pp. 270-276 ◽  
Author(s):  
Eva-Maria Boneberg ◽  
Lars Hareng ◽  
Florian Gantner ◽  
Albrecht Wendel ◽  
Thomas Hartung
Keyword(s):  
Flow Cytometry ◽  
Whole Blood ◽  
Receptor Expression ◽  
Human Neutrophils ◽  
Enzyme Linked Immunosorbent Assay ◽  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Ifn Γ ◽  
Stimulating Factor

In a double-blind, placebo-controlled, randomized study, 10 healthy men received either a single dose of 480 μg granulocyte colony-stimulating factor (G-CSF) or saline. Blood taken from the volunteers was stimulated with 10 μg/mL endotoxin and released cytokines were measured by enzyme-linked immunosorbent assay. Expression of G-CSF receptors on leukocytes was examined by flow cytometry and reverse transcriptase-polymerase chain reaction. Functional activity of these receptors was tested by challenging isolated leukocyte populations to release cytokines with endotoxin in the presence of G-CSF. The G-CSF treatment attenuated the release of the proinflammatory cytokines tumor necrosis factor (TNF)-, interleukin (IL)-12, IL-1β, and interferon (IFN)-γ in ex vivo lipopolysaccharide (LPS)-stimulated whole blood. In blood from untreated volunteers the presence of G-CSF in vitro also attenuated the LPS-stimulated release of these cytokines. G-CSF in vitro also attenuated TNF- release from elutriation-purified monocytes. In the presence of 10 ng/mL recombinant TNF-, the attenuation of LPS-inducible IFN-γ release by G-CSF was blunted in whole blood. However, G-CSF had no such effect on IFN-γ release from isolated lymphocytes stimulated with anti-CD3 or a combination of TNF- and IL-12. G-CSF receptor expression was detected in human neutrophils and monocytes but not in lymphocytes by means of RT-PCR as well as flow cytometry. These results indicate that G-CSF receptors expressed on monocytes are functional in modulating monokine release. We conclude that the attenuation of IFN-γ release from lymphocytes is not a direct effect of G-CSF on these cells but is rather due to the inhibition of monocytic IL-12 and TNF- release by G-CSF. (Blood. 2000;95:270-276)

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