Interactions between lipopolysaccharides and blood factors on the stimulation of equine polymorphonuclear neutrophils

1998 ◽  
Vol 64 (4) ◽  
pp. 313-322 ◽  
Author(s):  
H Benbarek ◽  
G Deby-Dupont ◽  
I Caudron ◽  
S Grülke ◽  
C Deby ◽  
...  
Keyword(s):  
Polymorphonuclear Neutrophils ◽  
Stimulation Of ◽  
Blood Factors

scholarly journals Stimulation of the human neutrophil respiratory burst by formyl peptides is primed by a protein kinase inhibitor, staurosporine

Blood ◽  
1993 ◽  
Vol 82 (9) ◽  
pp. 2890-2898 ◽  
Author(s):  
C Combadiere ◽  
J el Benna ◽  
E Pedruzzi ◽  
J Hakim ◽  
A Perianin
Keyword(s):  
Protein Kinase ◽  
Respiratory Burst ◽  
Phorbol Esters ◽  
Kinase Inhibitor ◽  
Polymorphonuclear Neutrophils ◽  
Time Dependent ◽  
Signalling Pathways ◽  
Dependent Manner ◽  
Formyl Peptides ◽  
Stimulation Of

Abstract Stimulation of polymorphonuclear neutrophils (PMN) by phorbol esters or formyl peptides (fMLP) generates large quantities of superoxide anion, the so-called respiratory burst (RB), a phenomenon associated with intense phosphorylation of a 47-kD protein (p47 phox). Staurosporine, a potent protein kinase C (PKC) antagonist, inhibits both responses when PMN are stimulated by phorbol myristate acetate (PMA), suggesting a positive role of PKC. In this study, we reassessed these PMN responses in fMLP-stimulated cells and found that staurosporine had opposite effects depending on the duration of PMN treatment with staurosporine. Short PMN incubation (0.5 to 3 minutes) with 25 to 100 nmol/L staurosporine inhibited the fMLP-induced RB, whereas longer treatment (15 to 20 minutes) enhanced it by up to about 200% relative to controls. In contrast, the PMA-mediated RB was depressed by staurosporine in a time-dependent manner. A primed fMLP-induced RB was also observed after long (15 minutes) PMN treatment with 5 to 100 mumol/L H-7, whereas shorter treatment (5 minutes) resulted in a small decrease in RB. By contrast, the tyrosine kinase inhibitor genistein (2 to 80 mumol/L) depressed fMLP-induced RB whatever the duration of PMN treatment. Analysis of 32P-phosphorylated proteins in fMLP-stimulated cells showed that short PMN treatment (< 8 minutes) with staurosporine abolished the phosphorylation of the 47-kD protein, which was identified as p47 phox, whereas long treatment partially restored p47 phox phosphorylation up to approximately 50% of the control value. In PMA-stimulated PMN, phosphorylation was reduced in a time-dependent manner. Furthermore, the staurosporine-primed RB and the staurosporine- induced recovery of phosphorylation were inhibited by sphingosine but not by genistein. Thus, in addition to its known depressive effect, staurosporine markedly potentiated fMLP-stimulated RB as a function of the duration of PMN treatment. The restoration of p47 phox phosphorylation suggests that staurosporine may alter the interactions between different protein kinases, producing marked time-dependent changes in signalling pathways. These data emphasize the care that should be taken in interpreting data obtained using this kinase inhibitor that may, however, be helpful analyzing in signalling pathways.

scholarly journals Inflammatory Responses of Bovine Polymorphonuclear Neutrophils Induced by Staphylococcal Enterotoxin C via Stimulation of Mononuclear Cells

2003 ◽  
Vol 10 (6) ◽  
pp. 1011-1018 ◽  
Author(s):  
Toshinobu Kuroishi ◽  
Ken-ichi Komine ◽  
Ken-ichi Asai ◽  
Jin Kobayashi ◽  
Kouichi Watanabe ◽  
...  
Keyword(s):  
Mononuclear Cells ◽  
Inflammatory Responses ◽  
Mammary Glands ◽  
Staphylococcal Enterotoxin ◽  
Polymorphonuclear Neutrophils ◽  
Histopathological Analysis ◽  
Peripheral Blood Mononuclear ◽  
Long Time ◽  
Stimulation Of

ABSTRACT To elucidate the pathological roles of staphylococcal enterotoxin C (SEC) in bovine staphylococcal mastitis, a histopathological analysis of SEC-inoculated mammary glands was performed. SEC-inoculated mammary glands exhibited interstitial inflammation, and the leukocytes that migrated into the gland were predominantly polymorphonuclear neutrophils (PMN). In the gland cistern tissues dissected from SEC-inoculated mammary glands, epithelial cellular degeneration was observed. We also investigated the physiological effects of SEC on PMN in vitro. PMN migration was induced by culture supernatant of SEC-stimulated peripheral blood mononuclear cells (S-PBMC sup) but not by that of nonstimulated PBMC (N-PBMC sup). The concentration of interleukin-8 was significantly (P < 0.05) higher in S-PBMC sup than N-PBMC sup, and a significantly (P < 0.05) higher mRNA expression of growth-regulated oncogenes was detected in SEC-stimulated PBMC than in nonstimulated PBMC. Milk PMN collected from SEC-inoculated mammary glands produced more than 2 times the amount of superoxide at 1 day postinoculation (dpi) than at 0 dpi in the presence of phorbol 12-myristate 13-acetate (PMA). PMN cultured with S-PBMC sup for 24 h also produced significantly (P < 0.05) larger amounts of superoxide than those cultured with N-PBMC sup in the presence of PMA. Moreover, S-PBMC sup induced the long-time survival of PMN. These results indicate that SEC induces the activation of PMN via the stimulation of mononuclear cells.

scholarly journals Stimulation of polymorphonuclear neutrophils by TNF muteins.

Ensho ◽  
1989 ◽  
Vol 9 (1) ◽  
pp. 25-28
Author(s):  
Ryutaro Kamijo ◽  
Ken Takeda ◽  
Kunio Konno ◽  
Masao Nagumo ◽  
Akira Hasegawa ◽  
...  
Keyword(s):  
Polymorphonuclear Neutrophils ◽  
Stimulation Of

Plasmin Is a Specific Stimulus of the 5-Lipoxygenase Pathway of Human Peripheral Monocytes

1996 ◽  
Vol 76 (04) ◽  
pp. 561-568 ◽  
Author(s):  
Ingo Weide ◽  
Bettina Tippler ◽  
Tatjana Syrovets ◽  
Thomas Simmet
Keyword(s):  
Serine Proteases ◽  
Cathepsin G ◽  
Polymorphonuclear Neutrophils ◽  
Coagulation Cascade ◽  
Human Neutrophil Elastase ◽  
Lipoxygenase Pathway ◽  
Specific Stimulus ◽  
Catalytic Center ◽  
Inflammatory Reactions ◽  
Stimulation Of

SummaryThe objective of this study was to characterize the plasmin-induced stimulation of leukotriene (LT) B4 biosynthesis in human peripheral monocytes (PM). Plasmin up to 175 × 10-3 CTA U/ml triggers a concentration-dependent release of 5-lipoxygenase-derived LTB4 while release of the cyclooxygenase products thromboxane (TX) B2 and prostaglandin (PG) E2 remained unaffected. The stimulatory effect appeared to be specific in as much as 1) it was found in PM, but not in polymorphonuclear neutrophils (PMN), 2) it requires the lysine binding sites of plasmin molecule since it was inhibited by the lysine analogues 6-aminohexanoic acid (6-AHA) and trans-4(aminometh-yl)cyclohexane-l-carboxylic acid (t-AMCA), 3) the intact catalytic center of plasmin is required since neither plasminogen nor catalytic center-blocked plasmin share the stimulatory effect of active plasmin, 4) other serine proteases such as a-chymotrypsin, human neutrophil elastase and cathepsin G did not stimulate release of detectable amounts of LTB4 from PM. In addition, catalytic center-blocked plasmin antagonized the stimulatory effect of active plasmin. Plasmin-mediated monocyte activation apparently proceeds via a pertussis toxin-sensitive G protein. Plasmin did not increase inositol (1,4,5) trisphosphate levels, but a time- and concentration-dependent stimulation of cyclic GMP formation was observed. The data show that plasmin is a specific stimulus for human peripheral monocytes. Plasmin may be an important link between the coagulation cascade and inflammatory reactions.

scholarly journals Stimulation of the human neutrophil respiratory burst by formyl peptides is primed by a protein kinase inhibitor, staurosporine

Blood ◽  
1993 ◽  
Vol 82 (9) ◽  
pp. 2890-2898 ◽  
Author(s):  
C Combadiere ◽  
J el Benna ◽  
E Pedruzzi ◽  
J Hakim ◽  
A Perianin
Keyword(s):  
Protein Kinase ◽  
Respiratory Burst ◽  
Phorbol Esters ◽  
Kinase Inhibitor ◽  
Polymorphonuclear Neutrophils ◽  
Time Dependent ◽  
Signalling Pathways ◽  
Dependent Manner ◽  
Formyl Peptides ◽  
Stimulation Of

Stimulation of polymorphonuclear neutrophils (PMN) by phorbol esters or formyl peptides (fMLP) generates large quantities of superoxide anion, the so-called respiratory burst (RB), a phenomenon associated with intense phosphorylation of a 47-kD protein (p47 phox). Staurosporine, a potent protein kinase C (PKC) antagonist, inhibits both responses when PMN are stimulated by phorbol myristate acetate (PMA), suggesting a positive role of PKC. In this study, we reassessed these PMN responses in fMLP-stimulated cells and found that staurosporine had opposite effects depending on the duration of PMN treatment with staurosporine. Short PMN incubation (0.5 to 3 minutes) with 25 to 100 nmol/L staurosporine inhibited the fMLP-induced RB, whereas longer treatment (15 to 20 minutes) enhanced it by up to about 200% relative to controls. In contrast, the PMA-mediated RB was depressed by staurosporine in a time-dependent manner. A primed fMLP-induced RB was also observed after long (15 minutes) PMN treatment with 5 to 100 mumol/L H-7, whereas shorter treatment (5 minutes) resulted in a small decrease in RB. By contrast, the tyrosine kinase inhibitor genistein (2 to 80 mumol/L) depressed fMLP-induced RB whatever the duration of PMN treatment. Analysis of 32P-phosphorylated proteins in fMLP-stimulated cells showed that short PMN treatment (< 8 minutes) with staurosporine abolished the phosphorylation of the 47-kD protein, which was identified as p47 phox, whereas long treatment partially restored p47 phox phosphorylation up to approximately 50% of the control value. In PMA-stimulated PMN, phosphorylation was reduced in a time-dependent manner. Furthermore, the staurosporine-primed RB and the staurosporine- induced recovery of phosphorylation were inhibited by sphingosine but not by genistein. Thus, in addition to its known depressive effect, staurosporine markedly potentiated fMLP-stimulated RB as a function of the duration of PMN treatment. The restoration of p47 phox phosphorylation suggests that staurosporine may alter the interactions between different protein kinases, producing marked time-dependent changes in signalling pathways. These data emphasize the care that should be taken in interpreting data obtained using this kinase inhibitor that may, however, be helpful analyzing in signalling pathways.

Sex-specific differences in the regulation of inducible nitric oxide synthase by bisphenol A in neutrophils

2018 ◽  
Vol 38 (2) ◽  
pp. 239-246 ◽  
Author(s):  
W Ratajczak-Wrona ◽  
K Nowak ◽  
M Garley ◽  
M Tynecka ◽  
E Jablonska
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Bisphenol A ◽  
Inducible Nitric Oxide Synthase ◽  
Polymorphonuclear Neutrophils ◽  
No Production ◽  
Nuclear Fraction ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide ◽  
Stimulation Of

The aim of the study was to evaluate the effect of bisphenol A (BPA) on nitric oxide (NO) production and inducible nitric oxide synthase (iNOS) expression by neutrophils with regard to sex and nuclear factor-κB (NF-κB) pathway participation in this process. This study demonstrated that BPA intensifies the production of NO and the expression of iNOS in the cytoplasmic fraction of neutrophils of women as well as men. In addition, an enhanced expression of NF-κB in the cytoplasmic and nuclear fraction of neutrophils exposed to BPA was observed in the cells of both sexes. The lipopolysaccharide (LPS) stimulation of neutrophils of both sexes led to an intensification of NO production and expression of all tested proteins. However, simultaneous stimulation of neutrophils of both men and women with LPS and BPA decreased the production of NO and expression of iNOS and NF-κB in both fractions compared to the cells exposed only to xenoestrogen. Moreover, expression of iNOS and NF-κB was higher in female neutrophils than in male cells. This study demonstrated that BPA affects the production of NO with the participation of iNOS by human polymorphonuclear neutrophils. This process is associated with the activation of the NF-κB pathway. In addition, different activity of NF-κB in neutrophils, observed with respect to sex, indicates a different role of this pathway in female and male cells.

Neutrophils stimulated by apolipoprotein(a) generate fragments that are stronger inhibitors of plasmin formation than apo(a)

2004 ◽  
Vol 92 (11) ◽  
pp. 1066-1075 ◽  
Author(s):  
Leila Lamanuzzi ◽  
El Mostafa Mtairag ◽  
Gabriella Pepe ◽  
Eduardo Anglés-Cano
Keyword(s):  
Aminocaproic Acid ◽  
Polymorphonuclear Neutrophils ◽  
Plasminogen Activation ◽  
Inflammatory Lesions ◽  
Apolipoprotein A ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Human Pmns ◽  
Stimulation Of ◽  
Pronounced Inhibition

SummaryApolipoprotein(a), the plasminogen-like component of lipoprotein(a), is transformed into fragments by polymorphonuclear neutrophils (PMNs) elastase. Since stimulated PMNs express urokinase-type plasminogen activator (uPA), we sought to investigate the relevance of apo(a) fragmentation on plasminogen activation by neutrophils. Freshly isolated human PMNs stimulated by a 10 kringle recombinant apo(a), r-apo(a), activate plasminogen in a specific and saturable manner (Km = 476 ± 42 nM, Vmax = 896 ± 18 pmol min-1). This activation is prevented by amiloride, an inhibitor of u-PA, and ɛ-aminocaproic acid, ɛ-ACA, a lysine analogue that blocks plasminogen binding to PMNs. Stimulation of PMNs by apo(a) results in the formation of elastase-derived apo(a) fragments. These fragments produce a concentration-dependent decrease in the formation of plasmin. Addition of elastase inhibitors to PMNs prevented degradation of apo(a) and partially restored the formation of plasmin. In a similar manner, isolated r-apo(a) fragments were able to produce a 100% decrease in plasmin generation as compared to intact r-apo(a). These data indicate that apo(a) fragments produce a more pronounced inhibition in the generation of cellbound plasmin by uPA than the parent apo(a). These effects of apo(a) and its fragments were neutralised by a monoclonal antibody directed against the lysine-binding site of apo(a). This mechanism may be of biological relevance to the effects of Lp(a) in conditions where PMNs accumulate and release elastase, i.e. thrombus lysis and inflammatory lesions.

Lack of hypoxic stimulation of VEGF secretion from neutrophils and platelets

2000 ◽  
Vol 279 (2) ◽  
pp. H817-H824 ◽  
Author(s):  
Petra Koehne ◽  
Carsten Willam ◽  
Evelyn Strauss ◽  
Ralf Schindler ◽  
Kai-Uwe Eckardt ◽  
...  
Keyword(s):  
Tissue Injury ◽  
Polymorphonuclear Neutrophils ◽  
Protein Synthesis Inhibitor ◽  
Low Oxygen ◽  
Vegf Mrna ◽  
Synthesis Inhibitor ◽  
Hypoxic Conditions ◽  
Endothelial Growth Factor ◽  
Vegf Release ◽  
Stimulation Of

Low oxygen (O2) is the key stimulus for expression of vascular endothelial growth factor (VEGF) in several adherent cells. Whether hypoxia also directs the release of VEGF protein from neutrophils (polymorphonuclear neutrophils; PMN) and platelets has not been investigated. We therefore compared VEGF release of platelets, PMN, and human vascular smooth muscle cells (HSMC) in response to hypoxia with that to activators of cellular degranulation. In contrast to HSMC, VEGF release from PMN and platelets or VEGF mRNA expression in PMN was not stimulated under hypoxic conditions (1% O2). Hypo- or hyperthermia and acidosis, other conditions potentially associated with ischemic and inflammatory tissue injury, also did not stimulate VEGF secretion from PMN. However, stimulation of platelets with thrombin and of PMN with phorbol 12-myristate 13-acetate induced a time-dependent release of VEGF, peaking after 30 and 60 min, respectively. This was blocked by the degranulation inhibitor pentoxifylline but not by the protein-synthesis inhibitor cycloheximide. We conclude that rapid release of VEGF from platelets and PMN may occur independently of oxygenation during inflammation and hemostasis.

scholarly journals Inhibitory effect of curcuminoids and tetrahydrocurcuminoids on equine activated neutrophils and myeloperoxidase activity

2008 ◽  
pp. 577-587
Author(s):  
T Franck ◽  
S Kohnen ◽  
S Grulke ◽  
P Neven ◽  
Y Goutman ◽  
...  
Keyword(s):  
Chemical Structure ◽  
Inhibitory Effect ◽  
Original Method ◽  
Polymorphonuclear Neutrophils ◽  
Myeloperoxidase Activity ◽  
Ros Production ◽  
Inhibitory Effects ◽  
Inflammatory Reactions ◽  
Activated Neutrophils ◽  
Stimulation Of

In the horse, the inflammation response to various pathologies (intestinal strangulations, laminitis, etc.) involves an excessive stimulation of the polymorphonuclear neutrophils releasing reactive oxygen species (ROS) and myeloperoxidase (MPO). The aim of the present work was to study the effect of natural polyphenols, curcuminoids and tetrahydrocurcuminoids (THC) on isolated stimulated equine neutrophils and on the activity of purified MPO. The ROS production and the release of MPO by activated neutrophils were measured by chemiluminescence and ELISA techniques, respectively. The activity of purified MPO was measured by studying its nitration, chlorination or oxidation capacity and by using an original method called SIEFED allowing the study of drug interaction with the enzyme without interferences of the medium. Curcuminoids and THC had dosedependent inhibitory effects on ROS production and MPO release by activated neutrophils and on purified MPO activity. We suggest that the higher efficacy of curcuminoids versus THC could be explained, at least partially, by its chemical structure: the conjugated double bounds and the plane structure of curcuminoids made easier the neutralization of the radical species generated by activated neutrophils and the interaction of the drug with the active site of MPO. These inhibitory effects of curcuminoids on the oxidant activity of equine neutrophils and on MPO activity open therapeutic perspectives in equine pathologies with excessive inflammatory reactions.

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