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Anesth Analg 2003;96:518-523
© 2003 International Anesthesia Research Society

CRITICAL CARE AND TRAUMA

Adrenaline Inhibits Lipopolysaccharide-Induced Macrophage Inflammatory Protein-1{alpha} in Human Monocytes: The Role of ß-Adrenergic Receptors

Chi-Yuan Li, MD, MS*, Tz-Chong Chou, PhD{dagger}, Chian-Her Lee, MD{ddagger}, Chien-Sung Tsai, MD§, Shih-Hurng Loh, PhD||, and Chih-Shung Wong, MD, PhD*

Departments of *Anesthesiology, {ddagger}Orthopedics, and §Surgery, Tri-Service General Hospital; and {dagger}Departments of Physiology, Graduate Institute of Medical Sciences and ||Pharmacology, National Defense Medical Center, Taipei, Taiwan, Republic of China

Address correspondence and reprint requests to Chi-Yuan Li, MD, MS, Department of Anesthesiology, #325, Section 2, Cheng-Kung Road, Taipei, Taiwan, ROC. Address e-mail to cyli{at}ndmctsgh.edu.tw


   Abstract
Top
 Abstract
Introduction
 Methods
 Results
 Discussion
 References
 
Macrophage inflammatory protein-1{alpha} (MIP-1{alpha}) has an important role in the development of inflammatory responses during infection by regulating leukocyte trafficking and function. Our study was conducted to investigate the effect of adrenaline on lipopolysaccharide (LPS)-induced MIP-1{alpha} production by human peripheral blood monocytes and human monocytic THP-1 cells. Monocytes were incubated in vitro with LPS for 4 h at 37°C in the presence and absence of adrenaline and/or specific {alpha}- and ß-adrenergic receptor antagonists and agonists. The effects of adrenaline on MIP-1{alpha} synthesis were studied at the protein level by using enzyme-linked immunosorbent assays and at the messenger RNA level by using reverse transcriptase-polymerase chain reaction. Adrenaline inhibited LPS-induced MIP-1{alpha} production in a dose-dependent manner. The suppressive effect could be completely prevented by propranolol, but not by phentolamine. The specific ß-adrenergic agonist isoproterenol produced the same inhibitory effect on LPS-induced MIP-1{alpha} production, whereas the {alpha}-adrenergic agonist phenylephrine had a minimal effect. In addition, suppression of MIP-1{alpha} production was associated with an increase of intracellular cyclic adenosine monophosphate (cAMP) by the cell membrane-permeable cAMP analog dibutyryl-cAMP. Furthermore, we found that adrenaline inhibited LPS-induced MIP-1{alpha} messenger RNA expression. These findings suggest that adrenaline can modulate MIP-1{alpha} production in inflammatory diseases and sepsis.

IMPLICATIONS: Macrophage inflammatory protein-1{alpha} (MIP-1{alpha}) has an important role in the development of inflammatory responses. In this study, adrenaline was found to inhibit lipopolysaccharide-induced MIP-1{alpha} production and messenger RNA expression via ß-adrenergic receptors in human monocytes. Our results suggest that adrenaline may modulate MIP-1{alpha} production in inflammatory diseases and sepsis.


   Introduction
Top
 Abstract
 Introduction
Methods
 Results
 Discussion
 References
 
The attraction of leukocytes to tissues is essential for inflammation, infection, and immune response. This process is controlled by chemokines, which play important roles in controlling leukocyte activation and regulating leukocyte trafficking in several immune-mediated and inflammatory disorders, such as bronchial asthma, rheumatoid arthritis, and acute respiratory distress syndrome (1–5). There are four families of chemokines, based on their sequence homology and the position of the first two cysteine residues, of which there are two main subfamilies: CXC chemokines and CC chemokines (6). In general, CXC chemokines are chemotactic for neutrophils, whereas the CC chemokines are chemotactic for monocytes and lymphocytes. Macrophage inflammatory protein-1{alpha} (MIP-1{alpha}) is a CC chemokine involved in the early inflammatory stages, wound healing, and hematopoiesis (7,8). MIP-1{alpha} was initially isolated from lipopolysaccharide (LPS)-stimulated murine macrophages (9). Human and murine MIP-1{alpha} were shown to activate monocytes/macrophages and basophils; to be chemotactic for T cells, eosinophils, and monocytes; and to induce an oxidative burst in neutrophils (10–12). Increased blood MIP-1{alpha} levels were found in patients with sepsis, asthma, and heart failure (3,13,14). Moreover, studies have established the importance of MIP-1{alpha} in mediating leukocyte infiltration in certain viral infections, autoimmune diseases, allograft rejection, and other inflammatory states (15,16).

There is increasing evidence that central nervous system activities can influence cellular immunity. It is well documented that the production of monocyte/macrophage inflammatory mediators is responsive to catecholamine action (17). The effects of adrenergic drugs on the production of cytokines have been extensively investigated. Tumor necrosis factor (TNF)-{alpha} was the first cytokine shown to be regulated by the occupation of {alpha}- or ß-adrenergic receptors by catecholamines (18). Interleukin (IL)-6 and IL-10 are influenced by adrenergic receptor stimulation both in vitro and in vivo (19,20). Nonetheless, the effects of adrenergic drugs on chemokine release have not been extensively examined. We report the effects of adrenaline on LPS-induced MIP-1{alpha} production of human peripheral blood monocytes and human monocytic THP-1 cells in vitro.


   Methods
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 Abstract
 Introduction
 Methods
Results
 Discussion
 References
 
Human monocytes were isolated from peripheral blood collected from six healthy laboratory employees after written, informed consent was obtained. Human peripheral blood monocytes were isolated by using a technique based on the OptiPrep density-gradient medium, with some modifications from a previous report (21). For each donor, the blood was collected and pooled into a 50-mL OpticulTM polypropylene conical tube (Falcon; Becton Dickinson, Bedford, MA) and centrifuged at 550g for 20 min at room temperature in a Labofuge 400R centrifuge with a swinging bucket rotor (Heraeus, Germany). Ten milliliters of buffy coat was collected and mixed with 4 mL of OptiPrep in a fresh 50-mL polypropylene conical tube. By using a disposable 9-in. glass pipette, the buffy coat/OptiPrep mixture was overlaid with 7.5 mL of a 1.078 g/mL lymphocyte-specific density layer. This layer was overlaid with 20 mL of a 1.068 g/mL solution of OptiPrep and 0.5 mL of HEPES-buffered saline. Care was taken to prevent mixing of the layers. The buffy coat/OptiPrep mixture was centrifuged at 600g for 25 min at room temperature in a Labofuge 400R centrifuge with a swinging bucket rotor; no brake was applied during deceleration. There were 3 fractions after separation, and the upper fraction contained the monocytes (>90% monocyte purity). After washing with phosphate-buffered saline (PBS), the monocytes were resuspended in RPMI 1640 medium and used for the experiments. The human monocytic cell line THP-1 (American Type Culture Collection, Rockville, MD) was cultured in RPMI 1640 medium supplemented with 10% fetal bovine serum, 100 U/mL of penicillin, and 100 µg/mL of streptomycin at 37°C and 5% CO2 in a humidified incubator. Cells were centrifuged and resuspended with fresh media in 24-well plates at a concentration of 106 cells per milliliter for 24 h before experimental use.

After 4-h treatments with LPS (serotype O111:B4; Sigma Chemical Co., St. Louis MO) and/or various concentrations of adrenergic agonists or antagonists (adrenaline, propranolol, phentolamine, isoproterenol, phenylephrine, and dibutyryl cyclic adenosine monophosphate (cAMP) were all obtained from Sigma), supernatants were stored at -70°C until assay. The MIP-1{alpha} concentration was determined by using sandwich enzyme-linked immunosorbent assays. Briefly, each well of a high-binding-efficiency 96-well enzyme-linked immunosorbent assay plate was coated with mouse anti-human MIP-1{alpha} monoclonal antibody (R&D Systems Inc., Minneapolis, MN) (100 µL at 4 µg/mL) in PBS at room temperature overnight. Then the plate was washed three times with PBS containing 0.05% Tween 20 (PBS-T). Residual binding sites were blocked with 1% bovine serum albumin (200 µL per well; Sigma) in PBS with 0.05% NaN3 and incubated for 2 h at room temperature. After washing with PBS, standard MIP-1{alpha} solution or cell supernatants (50 µL per well in PBS containing 3% bovine serum albumin) were added in duplicate to the coated wells, incubated for 2 h at room temperature, and washed again with PBS-T. Then, the plates were incubated with biotinylated goat anti-human MIP-1{alpha} detection antibodies (100 µL in 40 ng/mL) for 2 h at room temperature. After a wash with PBS, 100 µL of streptavidin horseradish peroxidase (1:20,000 dilution of a 1.25 mg/mL solution) was added and incubated for 20 min at room temperature. After a triple wash with PBS, 100 µL of substrate solution containing 1:1 mixture of H2O2 and tetramethylbenzidine was added and incubated another 20 min at room temperature. The reaction was stopped by adding 50 µL of stop solution (1 mol/L of H2SO4). Optical densities were read at a wavelength of 450 nm on an MRX microplate reader (Dynatech, Guernsey, UK).

After 2-h treatments with LPS (0.1 µg/mL) and various concentrations of adrenaline, total RNA was extracted from THP-1 cell pellets by using the single-step guanidinium thiocyanate-phenol-chloroform method (RNAzol B; Biotecx Laboratories, Houston, TX). The RNA was washed twice in ethanol and precipitated, and the amount of total RNA was quantified by spectrophotometry at 260 nm (Uvikon 940 spectrophotometer; Kontron, Zurich, Switzerland). A total of 100 ng of RNA per sample was reverse-transcribed with Moloney murine leukemia virus reverse transcriptase (PerkinElmer, Norwalk, CT) and oligodeoxythymidine-primed according to the manufacturer’s instructions. The reaction mixture was incubated at 42°C for 50 min for the reverse transcription reaction.

In brief, polymerase chain reaction (PCR) was performed with 25 pmol of each primer in a total volume of 50 µL. The reaction buffer consisted of 50 mmol/L of Tris-HCl, 0.02 mol/L of (NH4)2SO4, 1.5 mmol/L of MgCl2, 0.2 mmol/L of deoxynucleoside triphosphate, and 5 U of Taq DNA polymerase. A minimum of 3 different complementary DNA concentrations served as templates for amplification through 25 to 30 cycles of denaturation (30 s at 94°C), primer annealing (30 s at 58°C), and DNA extension (45 s at 72°C) in a GeneAmp PCR System 9600 (PerkinElmer). All amplifications were performed with a single set of gene-specific sense and antisense oligonucleotide primers. Primers were designed to flank at least one intron. Amplification of messenger RNA (mRNA) for the housekeeping gene glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used as an internal quality standard. The primer sequences were as follows: MIP-1{alpha} sense, 5'-CTGCCCTTGCTGTCCTCCTCTG-3'; MIP-1{alpha} antisense, 5'-CTGCCGGCTTGGCTTGGTTA-3'; GAPDH sense, 5'-GGGGAGCCAAAAGGGTCATCAT- CT-3'; and GAPDH antisense, 5'-GAGGGGCCATCCA- CAGTCTTCT-3'.

Amplified products were electrophoresed on 2% agarose gel and stained with ethidium bromide, and a 123-base pair DNA ladder (Life Technologies, Rockville, MD) was used as a molecular weight marker. The sample products were visualized with ultraviolet transillumination, and the gel was photographed. Total RNA from the LPS (1 µg/mL)-activated monocytic THP-1 cell line was used as the positive control. The experimental condition and the number of cycles of PCR were predetermined to ensure that the amount of MIP-1{alpha} and the number of housekeeping gene (GAPDH) fragments were in the linear range of amplification. GAPDH was used as the standard to control for variations in RNA isolation.

Human monocytic THP-1 cells in 200 µL were cultured in triplicate in a 96-well flat-bottom microtiter plate (Costar, Cambridge, MA) at 2 x 105 cells per well in RPMI medium containing 10% fetal bovine serum. To determine the cytotoxic effect of adrenaline, THP-1 cells were incubated for 24 h with variable concentrations of adrenaline with LPS in RPMI medium, the cell numbers were counted, and viability was evaluated with the trypan blue exclusion assay.

All data are presented as mean ± SEM. All statistical comparisons were performed with one-way analysis of variance. For multiple comparisons, the Student-Newman-Keuls test was conducted. P < 0.05 was accepted as indicative of significant differences between the groups. Calculations were performed with SigmaStat software (Jandel Scientific, Erkrath, Germany).


   Results
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 Abstract
 Introduction
 Methods
 Results
Discussion
 References
 
Initial experiments examined the production of MIP-1{alpha} from human monocytic THP-1 cells (106 cells per milliliter) after exposure to LPS (0.1 µg/mL) at 37°C. The kinetics of MIP-1{alpha} production after the administration of LPS were examined. The release of MIP-1{alpha} increased with time and reached the maximum 4 h after LPS challenge, then decreased gradually (Fig. 1). Therefore, in all subsequent experiments, supernatants were harvested at 4 h. Human monocytic THP-1 cells cultured in medium alone produced a low level of MIP-1{alpha} (129 ± 69 pg/mL). In contrast, a high level of MIP-1{alpha} production induced by LPS (0.1 µg/mL) was found in both human peripheral blood monocytes and THP-1 cells; this was inhibited by adrenaline in a dose-dependent manner (Fig. 2). Maximal inhibition was seen at the largest adrenaline concentration, which reduced MIP-1{alpha} levels to 48.2% and 30.6% in human peripheral blood monocyte and THP-1 cells, respectively.



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  		Figure 1. Kinetics of lipopolysaccharide-induced macrophage inflammatory protein (MIP)-1{alpha} production in human monocytic THP-1 cells. Values are expressed as the mean ± SEM of five independent experiments.

 


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  		Figure 2. Effect of adrenaline on lipopolysaccharide (LPS)-induced macrophage inflammatory protein (MIP)-1{alpha} production. Human peripheral blood monocytes (upper panel) and THP-1 cells (lower panel) were incubated for 4 h at 37°C with LPS (0.1 µg/mL) in the presence of adrenaline (0.1–100 µmol/L). Values are expressed as mean ± SEM (n = 5 or 6). *P < 0.05; **P < 0.01 compared with LPS alone (n = 5 or 6).

 
To examine the inhibition of MIP-1{alpha} production by adrenaline via the effect on {alpha}- or ß-adrenergic receptors, THP-1 cells were incubated for 4 h at 37°C with LPS (0.1 µg/mL) plus adrenaline (10 µmol/L), with various concentrations of either phentolamine (an {alpha}-antagonist) or propranolol (a nonspecific ß-antagonist). Phentolamine failed to alleviate the inhibitory effect of adrenaline. In contrast, propranolol (10 µmol/L) completely reversed it (Fig. 3). To gain further evidence that the inhibition of MIP-1{alpha} production by adrenaline was achieved by ß-adrenergic stimulation, THP-1 cells were incubated with LPS (0.1 µg/mL) in the presence and absence of phenylephrine (an {alpha}-adrenergic agonist) or isoproterenol (a nonselective ß1 and ß2 agonist). Phenylephrine had minimal effects on LPS-induced MIP-1{alpha} release. Isoproterenol caused a dose-dependent reduction of LPS-induced MIP-1{alpha} production (Fig. 4). At a concentration of 1 µmol/L, isoproterenol significantly suppressed MIP-1{alpha} production to 20.7% ± 6.4% of those observed after incubation with LPS alone.



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  		Figure 3. Effect of the ß-adrenergic antagonist propranolol and {alpha}-adrenergic antagonist phentolamine on the adrenaline (10 µmol/L)-induced suppression of macrophage inflammatory protein (MIP)-1{alpha} production by THP-1 cells after 4 h of incubation with lipopolysaccharide (LPS; 0.1 µg/mL). ++P < 0.01 compared with the LPS control; **P < 0.01 reversed by the ß-adrenergic antagonist against the adrenaline-induced suppression of MIP-1{alpha} production (n = 5 or 6).

 


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  		Figure 4. Dose-response effect of isoproterenol and phenylephrine on macrophage inflammatory protein (MIP)-1{alpha} production induced by lipopolysaccharide (LPS; 0.1 µg/mL) from THP-1 cells. Data are expressed as a percentage of the response to LPS alone. *P < 0.05; **P < 0.01 compared with the LPS control (n = 5 or 6).

 
Adrenergic stimulation increases intracellular cAMP levels (18,22). We studied the effect of cAMP analog dibutyryl-cAMP to clarify whether the inhibitory effect of adrenaline was cAMP dependent. Dibutyryl cAMP decreased LPS-induced MIP-1{alpha} release in a concentration-dependent manner, with a maximal inhibitory effect at 100 µM (Fig. 5); the release of MIP-1{alpha} was significantly reduced to 35.3% ± 2.8% of that observed after incubation with LPS alone.



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  		Figure 5. Effect of the membrane-permeable cyclic adenosine monophosphate (cAMP) analog dibutyryl-cAMP (db-cAMP) on the release of macrophage inflammatory protein (MIP)-1{alpha} from THP-1 cells stimulated by lipopolysaccharide (LPS; 0.1 µg/mL) for 4 h. Data are expressed as a percentage of the response to LPS alone. **P < 0.01 compared with the LPS control (n = 5 or 6).

 
To investigate whether inhibition of MIP-1{alpha} by adrenaline occurred at the transcription level, we examined the content of MIP-1{alpha} mRNA in THP-1 cells incubated with LPS in the presence or absence of adrenaline. Adrenaline caused a significant dose-dependent decrease in MIP-1{alpha} mRNA levels determined at 2 h after LPS (Fig. 6). On the basis of analysis of THP-1 cells treated with different concentrations of adrenaline and stained with trypan blue, there was no significant effect of adrenaline on cell survival and proliferation (data not shown).



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  		Figure 6. Adrenaline suppressed macrophage inflammatory protein (MIP)-1{alpha} messenger RNA expression. THP-1 cells were stimulated with lipopolysaccharide (LPS; 0.1 µg/mL), with medium alone (control), or with adrenaline (0.1, 1, or 10 µmol/L). Reverse transcriptase-polymerase chain reaction with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and MIP-1{alpha} primers was performed on total RNA extracts 2 h after the initiation of culture.

 

   Discussion
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 Abstract
 Introduction
 Methods
 Results
 Discussion
References
 
Recruitment of inflammatory and immune cells to the sites of tissue injury or infection is crucial for host defense. This response is regulated, at least in part, by a network of locally released mediators called "chemokines." An increase in blood MIP-1{alpha} level has been found in patients with sepsis, asthma, and heart failure (3,13,14). This study clearly demonstrated that in vitro (1) adrenaline ({alpha} and ß agonist) caused dose-dependent inhibition of MIP-1{alpha} production in human blood monocytes and THP-1 cells. This inhibitory effect could be completely reversed by the ß-antagonist propranolol (2); isoproterenol (a nonselective ß1 and ß2 agonist) produced the same inhibitory effect on LPS-stimulated MIP-1{alpha} production. These results suggest that ß-adrenergic receptors play a key role in mediating the inhibitory effect of adrenaline on LPS-induced MIP-1{alpha} production.

Our study is the first to show that adrenaline, as well as isoproterenol, attenuates LPS-stimulated MIP-1{alpha} production in human monocytes. As already recognized, TNF-{alpha} production is regulated by the occupation of {alpha}- or ß-adrenergic receptors by catecholamines (18). Similarly, some other cytokines are influenced by stimulating adrenergic receptors. In a murine model, Hasko et al. (23) found that pretreatment of RAW264.7 macrophages with adrenaline and noradrenaline decreased the MIP-1{alpha} release induced by LPS. Thus, catecholamines are important endogenous regulators of MIP-1{alpha} expression of inflammation. Nonetheless, phenylephrine ({alpha}-adrenergic agonist) reduced LPS-stimulated MIP-1{alpha} release slightly. The reason for this effect is unclear; it seems that the inhibitory effect probably reflects a nonspecific property of the compound.

The signal transduction mechanism for ß-adrenoceptors involves the activation of adenyl cyclase and an increase in intracellular cAMP. An increase of cAMP, via ß-adrenoceptors, seems to be an important mechanism for the modulation of cytokines (22). Through the use of membrane-permeable cAMP analogs (dibutyryl-cAMP) in LPS-stimulated THP-1 cells, a significant reduction of MIP-1{alpha} level was observed in our study. Therefore, the increase in cAMP levels is directly connected to the inhibition of MIP-1{alpha} production by ß-adrenoreceptor agonists in human monocytic THP-1 cells.

We found that adrenaline inhibited LPS-induced MIP-1{alpha} mRNA expression, suggesting that adrenaline might act at a transcriptional level in human monocytic THP-1 cells. Thus, the molecular level of MIP-1{alpha} inhibition by adrenaline appears to be at the transcriptional level. Nuclear factor-{kappa}B, an important transcriptional factor, has been implicated in the regulation of many inflammatory genes, including the TNF-{alpha} and IL-8 genes (24). Farmer and Pugin (25) previously showed that LPS-induced nuclear factor-{kappa}B activation and nuclear translocation were inhibited by ß agonists. Adrenaline and the ß agonist isoproterenol may interfere with this pathway, which inhibits LPS-induced MIP-1{alpha} production. However, further study is needed for proof.

Knowledge of the effect of catecholamines on cytokine production in sepsis is important not only because endogenous circulating catecholamine levels increase in response to endotoxemia, but also because catecholamine therapy is beneficial in the management of patients with septic shock. Several studies have shown an increase of plasma epinephrine concentrations in patients with trauma or septic shock (26). Moreover, postoperative adrenaline infusions of 0.03 µg · kg-1 · min-1 for patients receiving coronary artery bypass grafting demonstrated blood concentrations approximately 6 x 10-6 M (27), which was similar to the epinephrine concentration used in this study (0.1–100 µM). In acutely septic patients, MIP-1{alpha} is among the major cytokines found circulating in the blood (14). Our study demonstrated that adrenaline attenuates the LPS-induced release of MIP-1{alpha} in human blood monocytes via stimulation of ß-adrenergic receptors. These results exemplify the tight interaction between the cytokine network and the central nervous system. It suggests that in acute sepsis, adrenaline inhibits the continuing production of MIP-1{alpha} as part of a negative-feedback mechanism. Our findings may have important clinical implications: both adrenaline and ß-adrenoceptor agonists are widely used in the therapy of different diseases, such as septic shock and asthma. It is well known from the literature, and our data also indicate, that these drugs modulate cytokine production in response to pathogenic agents that may affect the immune response.

In conclusion, we demonstrated in vitro that adrenaline inhibits MIP-1{alpha} production in human monocytes. The site of this regulation is at the transcriptional level, and the mechanism is likely to involve an increase of intracellular cAMP via ß-adrenergic receptor stimulation.


   Acknowledgments
 
Supported by grants from Tri-Service General Hospital (TSGH-C90-61) and the National Science Council (NSC 89-2314-B-016-093), Taiwan, Republic of China.

The authors are grateful to Fu-Ming Tsai and Ping-Ching Hsu for their skillful technical assistance.


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 Introduction
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Accepted for publication October 9, 2002.




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Right arrow Pharmacology
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Lippincott, Williams & Wilkins Anesthesia & Analgesia® is published for the International Anesthesia Research Society® by Lippincott Williams & Wilkins with the assistance of Stanford University Libraries' HighWire Press®. Copyright 2006 by the International Anesthesia Research Society. Online ISSN: 1526-7598   Print ISSN: 0003-2999 HighWire Press