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*
Centre d’Immunologie Pierre Fabre, Saint-Julien en Genevois, France;
Pharmacie Centrale, Centre Hospitalier, Hazebrouck, France; and
Institut National de la Santé et de la Recherche Médicale Unité 416, Institut Pasteur, Lille, France
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
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by immature
DC and also up-regulates IL-1
, RANTES, and macrophage-inflammatory
protein 1 but not TNF- and IL-12 mRNA expression. Histamine
activates immature DC through both the H1 and H2 receptors. However,
histamine-treated DC do not have a phenotype of fully mature cells, as
they do neither show significant changes in the expression of the
chemokine receptors, CCR5, CCR7 and CXC chemokine receptor 4, nor
expression of CD83 de novo. These data demonstrate that histamine
activates immature DC and induces chemokine production, thereby
suggesting that histamine, via stimulation of resident DC, may
participate locally in T cell stimulation and in the late inflammatory
reaction associated with allergic disorders. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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), DC migrate to the secondary lymphoid organs
(1, 2, 3). During their migration, they undergo modulations
of phenotype and function, referred to as DC maturation. They express
increased levels of surface Ags involved in T cell activation such as
costimulatory molecules (e.g., CD54 and CD86) and MHC class I and II
molecules (1, 2). They produce numerous cytokines (e.g.,
IL-1 and IL-6) and chemokines (e.g., monocyte chemoattractant
protein (MCP) 1, macrophage-inflammatory protein (MIP) 1, MIP-1,
IL-8, and RANTES) that favor lymphocyte recruitment and activation
(4, 5). Moreover, they also down-regulate the expression
of receptors for inflammatory chemokines (e.g., CCR1 and CCR5) and
up-regulate those for constitutive chemokines (i.e., CCR7 and CXC
chemokine receptor 4 (CXCR4)), therefore allowing maturing DC to
migrate from the periphery to the lymph nodes (6). At the
same time, they lose their capacity to process Ag and neoexpress some
molecules (such as CD83 on human cells). In the T cell-dependent areas
of the lymphoid organs, myeloid migratory DC have acquired potent
immunostimulatory properties and sensitize recirculating naive
Ag-specific T cells (1, 2).
Mast cells are present in tissues in proximity to surfaces that
interface the external environment. In allergic individuals, a contact
with the sensitizing allergen results in the activation of mast cells
through allergen-specific IgE bound to high-affinity IgE receptors
(Fc
RI). Activated mast cells release preformed (e.g., histamine) and
newly synthesized mediators (such as prostaglandins, leukotrienes,
cytokines, and chemokines) (7, 8). Among these mediators,
histamine elicits almost all of the pathologic processes involved in
immediate allergic reaction (such as vasodilation, smooth muscle
contraction, mucus hypersecretion, and edema formation)
(9, 10, 11, 12). Histamine also presents immunoregulatory
properties. It induces E-selectin, ICAM-1, and LFA-1 expression
(10, 13), IL-6 and IL-8 production by endothelial cells
(14, 15), and IL-1, IL-6, IL-18, and IFN-
production by
PBMC (16, 17, 18). In parallel to these proinflammatory
effects, histamine has immunosuppressive properties. It induces IL-10
and prevents LPS-induced TNF- and IL-12 production by
monocytes/macrophages (19, 20, 21, 22). Histamine exerts its
effects through three receptors, H1, H2, and H3 (10, 12).
Although H1 and H2 receptors are expressed on numerous cell types,
including lymphoid cells, monocytes, and endothelial cells, H3 is
mainly expressed in the brain where histamine functions as a
neurotransmitter. Signaling through H1 receptor involves the activation
of the phospholipase C and controls most of the effects of histamine in
allergic disorders (smooth muscle contraction and increased
vasopermeability). Signaling through H2 receptors involves cAMP
generation and controls gastric acid secretion and vasodilation
(10, 12).
Because mast cells and immature DC are in close proximity throughout connective tissues (such as those from the respiratory tract and the skin), we have evaluated whether histamine released by activated mast cells may affect DC maturation.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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PBMC were isolated from healthy volunteers by standard density
gradient centrifugation on Ficoll-Paque (Amersham Pharmacia Biotech,
Uppsala, Sweden). Monocytes were purified from PBMC by positive
selection using a MACS (Miltenyi Biotec, Bergisch Gladbach, Germany)
according to the manufacturer’s instructions. Purity assessed by FACS
analysis using a FITC-labeled anti-CD13 mAb (Cymbys, Hants, U.K.)
was >98%. Monocytes were cultured in complete medium (CM) consisting
of RPMI 1640 medium supplemented with 10% FCS, 2 mM
L-glutamine, 50 U/ml penicillin, 50 µg/ml streptomycin,
10 mM HEPES, and 0.1 mM nonessential amino acids (all from Life
Technologies, Cergy Pontoise, France) at 5 x
106 cells/5 ml/well in six-well tissue culture
plates (Costar, Cambridge, MA) with 20 ng/ml IL-4 and 20 ng/ml GM-CSF
(both from R&D Systems, Abingdon, U.K.). At day 7, cells were analyzed
by FACS, as described above: only homogeneous immature DC populations
characterized by high levels of CD1a (mean fluorescence intensity (MFI)
from 100 to 800) and no CD83 expression were used. DC were then
recultured at 105 cells/200 µl/well in 96-well
flat-bottom tissue culture plates (Costar) in cytokine-containing CM
without or with different concentrations of histamine (Sigma, St.
Louis, MO). In some experiments, DC were also exposed to different
concentrations of the H1, H2, or H3 receptor antagonists, mepyramine,
cimetidine, or thioperamide (all from Sigma), respectively, for 1
h before addition of histamine. In others, immature DC were stimulated
with TNF- (R&D Systems), LPS (from Escherichia coli
isotype 0111:B4), or exposed to 10 µg/ml polymixin B sulfate
(Sigma).
Flow cytometric measurement of surface Ag expression
FACS analysis was performed using a FACSVantage cytofluorometer (Becton Dickinson, Erembodegem, Belgium) with the following mAbs: FITC-labeled anti-CD1a (Immunoquality Products, Groningen, The Netherlands), anti-CD80, anti-CD86, anti-CCR5 (all from PharMingen, San Diego, CA), anti-CD49d (Immunotech, Marseille, France), anti-CD54, anti-HLA-DR (both from Becton Dickinson), and anti-CD40 mAbs (Serotec, Oxford, U.K.). The binding of the anti-CD83 mAb (Immunotech) was revealed by FITC-labeled anti-mouse IgG Ab (Silenus, Melbourne, Australia). Control isotype mAbs were purchased from Becton Dickinson. Results are expressed as a percentage of positive cells or in MFI values after subtraction of the MFI obtained with the control mAb.
Analysis of mRNA expression by RT-PCR
The expression of the mRNA encoding for IL-1, IL-6, IL-8,
IL-10, IL-12p35, IL-12p40, IL-18, TNF-, MCP-1, MIP-1, RANTES,
CCR5, CCR7, and CXCR4 was determined by RT-PCR. After 8 and/or 30
h of culture with 10-5 M histamine, total RNA
was extracted using TRIzol reagent (Life Technologies, Rockville, MD)
and the single-strand cDNA was synthesized using 2 µg of total RNA by
RT using an oligo(dT) primer (Amersham Pharmacia Biotech). PCR were
performed with cDNA corresponding to 50 ng of total RNA and primers
designed to amplify the coding sequence of the cytokines and chemokines
(4, 5, 23). PCR was as follows: 94°C for 5 min, 30
cycles (25 cycles for IL-8 and MIP-1) 94°C for 30 s, 60°C
for 30 s, and 72°C for 1 min followed by a final extension at
72°C for 5 min. RNA integrity and cDNA synthesis were verified by
amplifying GAPDH cDNA (5'-TCCACCACCCTGTTGCTGTA-3' and
5'-ACCACAGTCCATGCCATCAC-3'). The amplified fragments were
size-separated on a 1% agarose gel and visualized by ethidium
bromide.
Cytokine and chemokine quantification
Day 7 DC were stimulated as described above and the
concentration of IL-6, IL-8, IL-10, IL-12, MCP-1, MIP-1, and TNF-
was determined in the 24- or 72-h cell-free culture supernatants by
ELISA (R&D Systems) (sensitivity of 0.7, 10, 0.5, 0.5, 5, 10, and 4.4
pg/ml, respectively). Results are expressed in pg/ml or in ng/ml (as
mean ± SD, n = 4).
T cell proliferation assays
Day 7 DC were washed, recultured at 2.5 x
106 cells/5 ml/well in six-well culture plates in
cytokine-containing CM, and were or were not stimulated with
10-5 M histamine or 20 ng/ml TNF-. After
24 h, DC were irradiated (3000 rad) and cultured with T cells in
quintuplicate. In MLR, DC at 2 x 102,
1 x 103, or 5 x
103 cells/200 µl/well in 96-well flat-bottom
plates were cultured with 105 allogenic T cells
purified from PBMC from healthy volunteers by rosetting with SRBC (the
purity assessed by FACS analysis using a FITC-labeled anti-CD3 mAb
was >95%). In anti-CD3 mAb proliferation assays, DC at 5 x
102, 5 x 103, 1
x 104, and 2 x 104
cells/200 µl/well in 96-well flat-bottom plates were cultured with
5 x 104 allogenic naive
(CD45RA+) or memory
(CD45RO+) CD4+ T cells and
stimulated with a suboptimal concentration (10 ng/ml) of anti-CD3
mAb. After rosetting and CD8 depletion, CD4+
CD45RA+ and CD4+
CD45RO+ T cells were purified by MACS using a
positive selection of CD45RA+ or
CD45RO+ T cells, respectively. After 3 days in
anti-CD3 mAb or 5 days in MLR assays, cells were pulsed during the
last 16 h with [3H]thymidine (0.25
µCi/well; Amersham Pharmacia Biotech). Radioactive incorporation was
measured by standard liquid scintillation counting and results are
expressed in cpm (mean of quintuplicate values) or in proliferation
index (PI) defined as followed: A/B, where
A and B are the cpm values obtained in the
presence or absence of stimulus, respectively.
Statistical analysis
Statistical analyses were performed using Student’s t test. Values of p < 0.05 were considered to be statistically significant.
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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To evaluate the effect of histamine on DC, human immature DC were
exposed to 10-8–10-4 M
histamine and CD86 expression was analyzed by flow cytometry. CD86
expression is undetectable on immature DC (<6% positive cells in day
7 monocyte-derived DC) and is induced by histamine on a percentage of
cells that increases dose dependently (Fig. 1
, A and B). One
day after exposure, CD86 expression is significant with
10-7 M histamine (11% ± 4 of CD86-positive
cells, mean% ± SD, n = 5) and maximal with 5 x
10-5 M (75% ± 10; Fig. 1B).
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(1, 2),
histamine-induced CD86 expression is transient (Fig. 1
C).
The expression of CD86 induced by 10-5 M
histamine is detectable after 6 h, maximal at 24 h (65
± 10, mean% ± SD, n = 5), and returns to basal level
at later time points. Addition of histamine at 24 h and/or 48
h failed to sustain this effect (data not shown).
As histamine and preformed TNF- are released concomitantly by mast
cells (7, 8), we then tested the addition of these
mediators together on immature DC. An additive effect of histamine and
TNF- on CD86 expression on DC is observed at any concentration used
(Fig. 1D).
Finally, the observation that polymixin B down-regulates LPS- but not
histamine-induced CD86 expression allows us to exclude contaminating
endotoxin in histamine preparation (Fig. 1E).
In conclusion, these data show that histamine activates human immature DC as assessed by the induction of CD86 expression.
Histamine transiently up-regulates costimulatory molecule expression on human immature DC
When stimulated by proinflammatory cytokines (e.g., TNF-) or
bacterial products (e.g., LPS), DC undergo a maturation process
characterized by an up-regulation of molecules related to Ag
presentation, a change in chemokine receptor expression, and the
neoexpression of the maturation marker CD83 (1, 2, 6).
Exposure of immature DC to histamine results in a marked up-regulation
of CD40, CD49d, CD54, CD80, and HLA-DR expression (Table I). As observed for CD86, histamine
transiently up-regulates these molecule expressions; the effect of
histamine is maximal after 1 day and undetectable after 4 days
(Table I).
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)
nor present veils (data not shown). At any time point analyzed,
histamine does not significantly modulate CCR5 expression as assessed
at the transcriptional (Fig. 2A) and traductional (Fig. 2B) levels nor induce CCR7 and CXCR4 mRNA expression (Fig. 2A). In contrast, LPS decreases CCR5 expression (Fig. 2B) and induces CCR7 and CXCR4 mRNA expression on immature
DC (Fig. 2A) (24).
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Histamine induces proinflammatory cytokine and chemokine production by human immature DC
Upon stimulation, DC produce proinflammatory cytokines (such as
IL-1, IL-6, IL-12, and TNF-) and chemokines involved in leukocyte
recruitment (such as MIP-1, MIP-1, IL-8, RANTES, and MCP-1)
(4, 5). We therefore tested whether histamine may
up-regulate cytokine production by DC. Histamine induces a production
of IL-8 by immature DC that is dose dependent, significant at 4 x
10-7 M and maximal at
10-5 M (Fig. 3A). Histamine also induces
IL-6, MCP-1, and MIP-1 production (Fig. 3B). Histamine
up-regulates IL-8, IL-6, MCP-1, and MIP-1 mRNA expression and also
IL-1, MIP-1, and RANTES mRNA expression (Fig. 3C).
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by DC after 24 or
72 h (Fig. 3B) nor up-regulate IL-10, p35, and p40
IL-12, IL-18, and TNF- mRNA expression after 8 h (Fig. 3C) or 16 h (data not shown). IL-10 is a cytokine that
inhibits DC maturation (25). In agreement with the absence
of detectable levels of IL-10 in the supernatant of histamine-treated
DC, neutralizing anti-IL-10 Ab does not enhance the histamine
effect on DC (data not shown).
As expected, LPS and TNF- induce the production of these cytokines
(except TNF- that did not induce IL-12 production by DC) (Fig. 3, B and C). Although immature DC constitutively
express IL-18 mRNA (4, 26), we failed in detecting IL-18
production, in the absence of T cells (27), after
stimulation with histamine, LPS, or TNF- for 24 or 72 h (data
not shown).
Thus, histamine induces the expression of the proinflammatory cytokines
IL-1 and IL-6 and of the chemokines IL-8, MCP-1, MIP-1, MIP-1,
and RANTES by human immature DC.
Histamine enhances DC accessory capacity
Based on the observation that histamine activates immature DC, we therefore tested in T cell proliferation assays whether histamine may enhance DC accessory capacities.
In anti-CD3 mAb assays, naive and memory CD4+
T cells were stimulated with a suboptimal concentration of anti-CD3
mAb and cocultured with DC either untreated or treated with histamine
or TNF- (Fig. 4, A and
B). Histamine-treated DC stimulate the proliferation of
memory T cells more efficiently than naive T cells (PI = 3.9
± 0.5 and 1.9 ± 0.2, respectively, mean ± SD,
n = 3, at 104 DC/well). As
expected, TNF--treated mature DC stimulate efficiently both naive
and memory T cell proliferation (PI = 4.5 ± 0.8 and 4.8
± 0.7; Fig. 4, A and B).
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(positive control) to stimulate the proliferation
of T cells from different donors. Histamine-treated DC stimulate
allogenic T cell proliferation although to a lower extent than
TNF--treated DC (PI = 2.8 ± 0.4 and 5.1 ± 0.8,
respectively, mean ± SD, n = 3, at
103 DC/well; Fig. 4C). Thus, histamine-treated DC present enhanced costimulatory properties as assessed by an efficient stimulation of memory T cell proliferation.
Histamine activates DC through H1 and H2 receptors
Histamine exerts its effects through three receptors, H1, H2, and
H3 (10, 12). Using specific receptor antagonists, we then
analyzed which receptor is involved in histamine-induced DC activation.
DC were exposed to 10-4 M of each of the H1, H2,
or H3 receptor antagonists (mepyramine, cimetidine, or thioperamide,
respectively) 1 h before addition of 10-5 M
histamine. None of these antagonists has an effect by itself on CD86
expression or IL-8 production by DC (Fig. 5). Results show that mepyramine and
cimetidine significantly prevent histamine-induced CD86 expression
(decrease of 58% ± 6 and 72% ± 5, respectively; mean ± SD,
n = 4) and IL-8 production by DC (decrease of 86% ± 5
and 92% ± 4, respectively; Fig. 5). In contrast, no effect of
thioperamide on histamine-induced DC activation is observed (Fig. 5).
Taken together, these data show that histamine activates human DC by
acting through both H1 and H2 receptors.
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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We demonstrate for the first time that histamine up-regulates numerous
chemokine production. It induces IL-8, MCP-1, and MIP-1 production
and up-regulates MIP-1 and RANTES mRNA expression by immature DC.
All of these chemokines are involved in the recruitment of numerous
cell types including T cells, monocytes, neutrophils, and immature DC
(29, 30) and in the development of the cellular afflux
associated with the late phase reaction (31). Furthermore,
IL-8, MIP-1, RANTES, and MCP-1 recruit mast cells/basophils and
induce histamine release (29), suggesting a positive
feedback that may contribute to sustain the inflammatory reaction.
In addition, histamine acts directly on immature DC to control
proinflammatory cytokine production. In agreement with data reporting
that histamine induces IL-1 and IL-6 production by PBMC (16, 17) and IL-6 production by endothelial cells (15),
we show that histamine up-regulates the expression of the two
proinflammatory cytokines by DC. Moreover, in accordance with data
obtained using monocytes/macrophages (18, 19, 20, 21), histamine
does not induce TNF- nor IL-12 production by DC. Histamine has been
shown to induce IL-10 production by alveolar macrophages
(22). In contrast, others reported that histamine alone
did not induce IL-10 production by PBMC (18, 21). In
agreement with this study, we report no detectable effect of histamine
on IL-10 production by DC. Finally, although histamine induces IL-18
production by PBMC (18), we failed in detecting an effect
of histamine on IL-18 production by DC in the absence of T cells
(26, 27). These data point out a tight control of
proinflammatory cytokine production by histamine which may differ with
the nature of the target cells.
Several hours after an allergen challenge, some allergic patients develop a late inflammatory reaction (also named late phase reaction) characterized by a local infiltrate of eosinophils, memory T cells, and neutrophils that contribute to the tissue damage. The recruitment and activation of these inflammatory cells involve a series of events, including transendothelial migration of leukocytes and subsequent chemotactic movements, that are regulated by proinflammatory cytokines and chemokines (24). Based on the observations that histamine induces IL-8 production by endothelial cells (14) and that histamine challenge increases neutrophil, mast cell, and leukocyte numbers in the bronchoalveolar lavage from healthy subjects (32), it is now suspected that, in addition to its effects in the immediate reaction associated to allergic diseases, histamine also participates in the late inflammatory reaction. The present data show that histamine, in addition to inducing the production of the proinflammatory cytokines IL-1 and IL-6, up-regulates chemokine production by DC and thereby evidence a direct mechanism by which histamine may participate in the initiation of the inflammatory reaction.
Although histamine-treated DC have not all of the characteristics of
fully mature cells (compared with stimuli that induce DC maturation and
migration such as LPS and TNF-), they transiently express high
levels of CD86 and other costimulatory molecules. In agreement with
this observation, results from proliferation assays show that histamine
enhances the costimulatory properties of DC. Interestingly, although
histamine-treated DC are as effective as fully mature DC in stimulating
memory T cell proliferation, they only slightly enhance naive T cell
proliferation. Both of these observations are in agreement with the
fact that memory T cells require less stringent and sustained cosignals
than naive cells to be efficiently activated (33). We also
report that histamine only poorly affects the expression of the
chemokine receptors CCR5, CCR7, and CXCR4, therefore suggesting that
these DC could be unable to migrate from the periphery to the lymph
nodes (6). In contrast to naive T cells that migrate to
the lymph nodes, memory T cells are preferentially located in
peripheral tissue (34, 35). Thus, we could speculate that
histamine by activating DC may participate, at the inflammatory site,
in memory T cell restimulation (36). This is reinforced by
the observation that histamine-treated DC produce chemokines involved
in memory T cell recruitment (such as RANTES, MCP-1, and MIP-1)
(29). Taken together, our in vitro data suggest that
histamine by acting on immature DC may favor in situ-specific T cell
stimulation.
In allergic patients, allergen-specific T cells and mast cells produce
IL-4, a Th2 lymphokine that plays a central role in IgE synthesis and
in the induction and maintenance of allergic responses (37, 38). MCP-1 stimulates IL-4 production by T cells, attracts
memory effector T cells, and is required for the development of a Th2
response (39, 40). In contrast, IL-12 induces IFN-
production and prevents the development of a Th2 response. The findings
that histamine induces MCP-1 production and does not affect IL-12
production suggest that histamine may contribute to maintain a Th2
polarization in allergic diseases. However, since histamine also
induces IL-18 and IFN- production by PBMC (18), whether
histamine may modulate Th1/Th2 orientation remains to be evaluated.
Nevertheless, the observation that histamine activates DC, added to
data from others showing that histamine acts on B and T cells to
increase Ag receptor-mediated responses (41), suggest a
direct role for histamine in the development of a specific immune
response. Thus, histamine may participate in the immune and
inflammatory responses associated with allergic disorders.
We report that histamine activates immature DC with an effect
significant at concentrations ranging from 10-7
to 10-4 M. Although it remains difficult to
determine precisely the concentration of histamine in the target organ,
concentrations from 10-6 to
10-4 M were reported to be comparable to those
measured in tissues after mast cell degranulation (16, 19, 42). For example, after allergen challenge, a concentration of
10-7 M was detected in nasal lavages of patients
with allergic rhinitis, and this concentration was diluted 10- to
100-fold by the lavage procedure (43). Moreover, upon
contact with the sensitizing allergen, mast cells from allergic
patients concomitantly release different mediators (such as
PGE2, histamine, and preformed TNF-) that may
act in concert to stimulate DC. TNF- synergizes with
PGE2 in inducing DC maturation in vitro
(44). We report here an additive effect between TNF-
and histamine in inducing DC activation. According to these different
points, the in vitro effects of histamine on DC described here probably
reflect its in vivo activity at the inflammatory sites. Previous
studies reported that epidermal Langerhans cells (LC) are not activated
by classical proinflammatory stimuli (45), thus avoiding
hyperresponsiveness to harmless Ags after skin damage (45, 46). In agreement with these data, we failed in activating in
vitro-generated LC (derived from CD34+ cells
(47) or monocytes (48)) by histamine (data
not shown). If we consider that in vitro-generated LC are a relevant
model, this observation suggests that, in atopic dermatitis
(49), histamine released by mast cells after allergen
exposure may act preferentially on dermal DC. Thus, these data show
that histamine is a new proinflammatory molecule that activates DC and
thereby suggests an interaction between immature DC and mast cells.
Histamine has been shown to affect cytokine production by leukocytes
and endothelial cells by acting through H1, H2, or H3 receptors. The
anti-inflammatory effects of histamine, including inhibition of
LPS-induced IL-12 and TNF- production and up-regulation of IL-10
production by PBMC, are mediated through H2 (19, 20, 21, 22); one
report also involves H3 receptors in histamine-induced IL-10 production
by macrophages (22). However, histamine has been shown to
induce IL-6 and IL-8 production by endothelial cells through both H1
and H2 receptors (14, 15). In agreement with these
findings, we observed that both H1 and H2 receptors are involved in
histamine-induced DC activation. Finally, histamine increases
TNF--induced E-selectin, ICAM-1, and LFA-1 expression on endothelial
cells through H1 receptors (13). Together, these data
suggest an inflammatory activity of histamine that is mediated through
both H1 and H2 receptors and an anti-inflammatory role for H1
receptor antagonists.
In conclusion, we show that histamine induces chemokine production and activates DC via both H1 and H2 receptors. Since histamine is produced mainly by mast cells/basophils, these data suggest a direct cross-talk between mast cells and DC. Moreover, the ability of histamine to induce chemokine production demonstrates that histamine is not only involved in the early changes associated with allergic diseases but is also an integral component of the inflammatory response. Its ability to enhance DC costimulatory properties suggests that histamine also favor specific T cell activation.
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Footnotes |
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2 Abbreviations used in this paper: DC, dendritic cell; MCP, monocyte chemoattractant protein; MIP, macrophage-inflammatory protein; MFI, mean fluorescence intensity; PI, proliferation index; LC, Langerhans cell.
Received for publication August 28, 2000. Accepted for publication March 6, 2001.
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 B. RYFFEL, I. COUILLIN, I. MAILLET, B. SCHNYDER, G. C. PAESEN, P. NUTTALL, and W. WESTON-DAVIES Histamine Scavenging Attenuates Endotoxin-Induced Acute Lung Injury Ann. N.Y. Acad. Sci., November 1, 2005; 1056(1): 197 - 205. [Abstract] [Full Text] [PDF]
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 Z. Pos, G. Safrany, K. Muller, S. Toth, A. Falus, and H. Hegyesi Phenotypic Profiling of Engineered Mouse Melanomas with Manipulated Histamine Production Identifies Histamine H2 Receptor and Rho-C as Histamine-Regulated Melanoma Progression Markers Cancer Res., May 15, 2005; 65(10): 4458 - 4466. [Abstract] [Full Text] [PDF]
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R. Gutzmer, C. Diestel, S. Mommert, B. Kother, H. Stark, M. Wittmann, and T. Werfel Histamine H4 Receptor Stimulation Suppresses IL-12p70 Production and Mediates Chemotaxis in Human Monocyte-Derived Dendritic Cells J. Immunol., May 1, 2005; 174(9): 5224 - 5232. [Abstract] [Full Text] [PDF]
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 F. E. R. Simons Advances in H1-Antihistamines N. Engl. J. Med., November 18, 2004; 351(21): 2203 - 2217. [Full Text] [PDF]
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D. M. Jawdat, E. J. Albert, G. Rowden, I. D. Haidl, and J. S. Marshall IgE-Mediated Mast Cell Activation Induces Langerhans Cell Migration In Vivo J. Immunol., October 15, 2004; 173(8): 5275 - 5282. [Abstract] [Full Text] [PDF]
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I. Couillin, I. Maillet, B. B. Vargaftig, M. Jacobs, G. C. Paesen, P. A. Nuttall, J. Lefort, R. Moser, W. Weston-Davies, and B. Ryffel Arthropod-Derived Histamine-Binding Protein Prevents Murine Allergic Asthma J. Immunol., September 1, 2004; 173(5): 3281 - 3286. [Abstract] [Full Text] [PDF]
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 A. Mazzoni and D. M. Segal Controlling the Toll road to dendritic cell polarization J. Leukoc. Biol., May 1, 2004; 75(5): 721 - 730. [Abstract] [Full Text] [PDF]
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A. Mazzoni, C. A. Leifer, G. E. D. Mullen, M. N. Kennedy, D. M. Klinman, and D. M. Segal Cutting Edge: Histamine Inhibits IFN-{alpha} Release from Plasmacytoid Dendritic Cells J. Immunol., March 1, 2003; 170(5): 2269 - 2273. [Abstract] [Full Text] [PDF]
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) or
exposed to 10-5 M histamine (
) or 20 ng/ml TNF-
). D, Immature DC were exposed to combinations of
increasing doses of histamine (from 10-7 to
10-5 M) and TNF-
) of 10 µg/ml polymixin B. B–E, CD86
expression was analyzed by FACS after 24 h (B,
D, and E) or at different time points
(C). B–E, Results are expressed in
percentage of CD86-expressing cells as mean ± SD of five separate
experiments (B, C, and E)
or as one representative of three experiments (D).
