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*
Immunology Department, Fundación Jiménez Díaz, Madrid, Spain; and
Division of Allergy, La Jolla Institute for Allergy and Immunology, San Diego CA 92121
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Abstract |
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 Top Abstract IntroductionMaterials and MethodsResultsDiscussionReferences |
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-binding protein
or Mac-2, which has been described to play an important role in some
inflammatory processes by the implication of different cells and the
increase in cell adhesion functions through laminin binding activity.
In this work we analyzed the role of galectin-3 in the modulation of
Th2 cytokines that have an important role in the development of the
inflammatory response. We have found that the addition of galectin-3 to
human eosinophils, the eosinophilic cell line EoL-3, PBMC, and an
Ag-specific T cell line (CD4+) produced a selective
inhibition of IL-5 transcription. No inhibitory effect was found on the
IL-4 mRNA transcription rate. The inhibitory effect on IL-5
transcription was reversed by incubation with lactose and using
specific Ab against galectin-3. Galectin-3 is able to induce inhibition
of the IL-5 released in the supernatants from PBMC stimulated with
phorbol 12,13-dibutyrate and anti-CD3. Similar results were
obtained when a T-specific cell line was stimulated with Ag. Also,
EoL-3 stimulated with anti-CD32 produced IL-5 protein, the
synthesis of which was partially inhibited by galectin-3. The present
results demonstrate that galectin-3 induces a selective down-regulation
of IL-5 expression in different cell types, opening important new
possibilities in the regulation of the allergic reactions. |
Introduction |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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-binding protein, Mac-2, CBP-35, CBH-30, L-29, and L-34.
Galectin-3 has two domains: the amino terminal with highly conserved
tyrosine-, proline-, and glycine-rich residues, which account for its
tendency to self-associate, and the carboxyl-terminal domain where the
carbohydrate-binding site resides (1, 2). The expression of galectin-3 was markedly elevated in proliferating cells, suggesting that galectin-3 may be a component of the cell growth-regulating system and maintains viability by a mechanism possibly involving bcl-2 protein (3, 4). More recently, galectin-3 was identified as a factor implicated in mRNA splicing (5). This lectin was also associated with tumor transformation (6). Galectin-3 may also have extracellular functions. It was found to be a major nonintegrin laminin binding protein and has been proposed to have a role in cell adhesion and inflammation (7). Galectin-3 recognizes cell surface glycoproteins on various cell types and is able to activate different groups of cells, including monocytes, macrophages, neutrophils, and eosinophils (8, 9, 10). Due to the fact that galectin-3 lacks any transmembrane domain, this protein requires the presence of a cellular counterligand(s) (carbohydrate-rich) to be attached to the membrane.
Recent findings pointed out a role for galectin-3 in IgE-mediated activation of neutrophils (11). Furthermore, galectin-3 is able to bind high affinity IgE receptor on mast cells and to activate rat basophilic leukemia cells (12). Interesting data from the literature reported the existence of galectin-3 on eosinophils from patients with eosinophilia (10).
Eosinophils play a prominent role in allergic inflammation due to the active synthesis and release of inflammatory mediators and cytokines that amplify and regulate the progression of the allergic response (13, 14). Among the long list of cytokines that eosinophils can secrete, IL-5 is known to prolong survival, differentiation, and activation of eosinophils (15).
The results presented in this paper shown a total decrease in IL-5 mRNA and a reduction in IL-5 production by human eosinophils, EoL-3, PBMC, and an Ag-specific T cell line derived from an allergic patient after treatment of cells with galectin-3, suggesting a role for galectin-3 in the homeostasis of the allergic reaction.
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Materials and Methods |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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Peripheral blood was obtained from allergic patients for eosinophils and lymphocytes after obtaining consent from the subjects and approval by the hospital ethical committee. Patients were selected by the Allergy Department of Fundación Jiménez Díaz. Eosinophils from two allergic patients were purified following a negative immunoselection technique using magnetic beads (16). PBMC from three allergic patients were isolated by density sedimentation gradient (Nycomed Pharma, Oslo, Norway). A T cell line (CD4+, CD8-) specific to the major Ag of olive pollen (Ole e 1) was obtained from a patient sensitized to olive pollen (17).
A human eosinophilic leukemia cell line (EoL-3) was a generous gift from Dr. R. G. Lynch (University of Iowa, Iowa City, IA).
Reagents
Recombinant human galectin-3 (18) and anti-galectin-3 (BC210 mouse IgG, anti-human galectin-3) (19) were dialyzed against PBS and filtered with Minisart (0.20 µm pore size; Sartorius, Gottingen, Germany) before addition to the culture. No endotoxin levels were detected by the Limulus amebocyte lysate assay (BioWhittaker, Ingelheim Diagnostica y Tecnología, Barcelona, Spain). Anti-human CD32 and irrelevant control Ab anti-human CD19 were purchased from Lander Diagnostic (Madrid, Spain). Lactose (Fluka, Buchs, Switzerland), a ligand of galectin-3, was used for reversal of the inhibitory effects.
Cell culture
Cells were cultured in RPMI 1640 medium (Life Technologies, Renfrewshire, Scotland) supplemented with sodium pyruvate (5 mM), L-glutamine (2 mM), penicillin (50 U/ml), streptomycin (50 µg/ml; Flow Laboratories, Irvine, Scotland), and 10% heat-inactivated FBS (Life Technologies). The T cell line was cultured in the same medium supplemented with 5% human serum.
RT-PCR
For mRNA expression, 106 cells/ml were incubated with galectin-3 (10 µg/ml) with or without anti-galectin-3 (10 µg/ml) for 24 h. Total RNA was extracted from cells (2 x 106) using the guanidine-thiocyanate method previously described (20), and 1 µg of RNA was converted to cDNA by the reverse transcriptase enzyme reaction (AMV transcriptase-reverse, Promega, Madison, WI) in a total volume of 20 µl.
PCR was performed in a final volume of 50 µl of RT reaction product. ß-Actin, IL-4, and IL-5 (Clontech, Palo Alto, CA) were amplified following the manufacturer’s instructions. An 18-µl aliquot from each PCR reaction was electrophoresed in a 1.5% agarose gel containing 0.5% ethidium bromide. The gel was photographed under UV transillumination and submitted to Southern blot hybridization.
Southern blot hybridization
One-third of the PCR products were fractionated on a 1.5% agarose gel and blotted onto nylon Zeta-Probe membranes (Bio-Rad, Hercules, CA), using 0.4 N NaOH as transfer medium. Membranes were washed and prehybridized in saline-sodium phosphate-EDTA (SSPE), 0.1% SDS, 10x Denhart’s solution (0.2% Ficoll, 0.2% polyvinylpirrolidone, and 0.2% BSA; Pentax fraction V, Sigma, St. Louis, MO), and 0.1 mg/ml herring sperm DNA for 1 h at Tm-53 for each subject.
Oligonucleotide probes (150 ng), specific for an internal sequence of
the primers used in the amplification, were labeled with
[
-32P]ATP (Amersham) at the 5' end by 15 U of T4
polynucleotide kinase (Promega) for 1 h at 37°C in a final
volume of 20 µl. Probes were separated from nonincorporated
nucleotides by absorption using DEAE-81 cellulose (Whatman, Maidstone,
U.K.). Thereafter, the excess of unincorporated nucleotides was
discarded by a low salt solution (20 mM Tris-HCl, 1 mM EDTA (pH 8.0),
and 0.1 mM NaCl), and the radiolabeled probe was eluted with a high
salt solution (20 mM Tris-HCl, 1 mM EDTA, and 1 M NaCl). The latter was
added at 106 cpm/ml to the hybridization solution (6x
SSPE, 0.1% SDS, 5x Denhart’s solution, and 0.1 mg/ml herring sperm
DNA) for 3 h at Tm-5 in each case. After washing twice with 6x
SSC (3 M NaCl and 0.3 M sodium citrate, pH 7) for 20 min each time at
room temperature and for 10 min with 6x SSC at Tm-5 in each probe,
membranes were exposed for 12 h at -70°C.
Induction of IL-5 production in different cell types
PBMC. To induce IL-5 production, 106 cells/ml were cultured at 37°C in 5% CO2 in the presence of 20 ng/ml phorbol 12,13-dibutyrate (PDBu; Calbiochem, La Jolla, CA) plus 10 ng/ml anti-CD3 mAb (21), with or without galectin-3 (10 µg/ml). After 36 h of culture, supernatants were collected, filtered, and stored in aliquots at -80°C until used.
Ag-specific T cell line. Cells (1 x 106) from a T cell line established from a patient sensitized to Olea europaea pollen (17) were stimulated with 25 µg/ml of specific Ag for 36 h in the presence or the absence of galectin-3. After this period, supernatants were collected and treated as described above.
EoL-3. EoL-3 cells (2 x 106/ml) were stimulated with anti-CD32 mAb at 10 µg/ml in the presence or the absence of galectin-3 (10 µg/ml). Supernatants were concentrated twofold using Ultrafree-15 (Millipore Iberica, Madrid, Spain).
Quantitation of human IL-5
ELISA was used for quantitative determination of human IL-5 in cell culture supernatants (Quantikine human IL-5 Immunoassay, R&D Systems, Minneapolis, MN). The sensitivity of the ELISA was 3.0 pg/ml (n = 20).
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Results |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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To determine whether binding of galectin-3 can regulate the
cytokine pattern of different nonstimulated immunocompetent cells,
incubation of galectin-3 (10 µg/ml) with the human eosinophilic cell
line (EoL-3), peripheral human eosinophils, and PBMC from allergic
patients was performed over a 24-h period (Fig. 1
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shows the results obtained for
IL-5 transcription using Southern blot of RT-PCR products. All three
cellular types constitutively expressed mRNA for IL-5
(lane 1). Incubation of the cells with
galectin-3 inhibited the level of IL-5 mRNA (lane
2). Different experiments were conducted to demonstrate
whether galectin-3 specifically inhibits IL-5 transcription. The
inhibitory activity of galectin-3 was not observed in the presence of
anti-galectin-3 Ab, demonstrating the specificity detected on the
effect caused by galectin-3 (lane 3).
Irrelevant mAb (anti-CD19) was used as a negative control, and it
has no effect on the galectin-3 inhibitory activity (lane
4). Furthermore, the inhibitory effect of galectin-3 was
reversed when lactose (31.2 mM), which is a ligand of galectin-3, was
added (data not shown). Lanes 5 and 6 represent a
positive and a negative control, respectively.
IL-4 mRNA transcripts were detected in all three cellular types without
any in vitro stimulation (Fig. 1, middle part, lane
1). However, addition of galectin-3 was unable to modify
the levels of IL-4 mRNA in all cases (lane 2).
Simultaneous addition of galectin-3 and anti-galectin-3 did not
change any pattern of IL-4 transcription (lane
3).
We performed a dose-response curve in the EoL-3 cell line. Galectin-3
was added from 1 to 12.5 µg/ml. IL-5 mRNA expression was not
detectable with doses >5 µg/ml (Fig. 2A). The inhibitory
effect was not observed using the same doses of galectin-3 in the
presence of anti-galectin-3 (Fig. 2B),
demonstrating a dose-dependent inhibition of IL-5 mRNA expression by
galectin-3 on these cells.
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To further analyze the effect of galectin-3 in the context of antigenic
stimulation, a CD4+ T cell line generated from an allergic
individual, specific for Ole e 1, the major Ag of O.
europaea pollen was used (17). Cells (106 cells/ml)
were incubated for 24 h with 25 µg/ml of the specific Ag, and
mRNA for IL-5 and IL-4 was determined (Fig. 4). IL-5 mRNA was detected on T cells
with or without incubation with the Ag (lanes 1 and
2). Interestingly, simultaneous addition of
Olea and galectin-3 was able to inhibit the transcription of
IL-5 (lane 3). Antigenic stimulation of the T
cell line was required to detect mRNA for IL-4. However, galectin-3 was
unable to block IL-4 mRNA on T cells stimulated with Ag. All these
results clearly show that the inhibition of IL-5 transcription caused
by galectin-3 was also effective in the context of TCR-dependent
activation.
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The amount of IL-5 released from supernatants was quantified by
ELISA to check the inhibitory effects of galectin-3 (Table I). PBMC from three allergic patients
(no. 1, 2, and 3) were stimulated with PDBu plus anti-CD3 mAb with
and without galectin-3. In all three experiments, the levels of IL-5
produced were significantly lower in the presence of galectin-3. The
percent inhibition ranged between 35 and 83%. When anti-galectin-3
was present, a partial reversal was obtained in all three experiments
(Table I), demonstrating that galectin-3 is able to effectively inhibit
the amount of IL-5 released in the supernatants even after a strong
activation signal.
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).
Production of IL-5 from the eosinophilic cell line EoL-3 was only
obtained using anti-CD32 as the stimulus, increasing the number of
cells per well (2 x 106 cells/ml) and concentrating
the supernatants twofold. Under these conditions, we obtained a 43%
inhibition of the release in the presence of galectin-3 (Table I).
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Discussion |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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Expression of galectin-3 was detected by various inflammatory cells, including monocytes, macrophages, neutrophils, and eosinophils (8, 9, 10), but not on B and T lymphocytes, although recently the presence of galectin-3 was reported in HTLV-1-infected T cells (22).
Galectin-3 has a predominant cytosolic distribution; however, it can also be expressed on the cell surface and secreted by various cellular types. Several functions have been ascribed to galectin-3; among them, galectin-3 has an important role in inflammation and host defense, stimulates superoxide production in neutrophils, monocytes, and macrophages (11), and can also participate in the IgE-dependent eosinophil cytotoxicity against parasites (10). Galectin-3 binds to a small number of glycoprotein species on the surface of rat basophilic leukemia cells, and one of them is the high affinity IgE receptor and causes serotonin release from rat basophilic leukemia cells (23).
One of the major findings of the present work is that galectin-3 specifically and completely inhibits the transcription of IL-5 without any detectable effect on the production of IL-4. This may be explained by the finding that IL-4 and IL-5 genes are differentially regulated (24).
In a time-dependent experiment we found that the inhibition of IL-5
mRNA produced by galectin-3 is total at 24 h and remains for at
least another 10 h, but a partial decrease in the message is
observed as early as 10 h after the beginning of culture (Fig. 3).
This partial inhibition obtained at 10 h after the addition of
galectin-3 points toward a direct effect of the lectin on the
transcriptional elements of IL-5 and rules out the possibility of an
indirect effect through the action of galectin-3 on another cytokine or
mediators that, in turn, induce the decrease in IL-5 gene
expression.
Interestingly, the modified transcriptional rate of IL-5 was restored by simultaneous addition of galectin-3 and anti-galectin-3, showing the specificity of the reaction. Probably, galectin-3 interacts directly in an inhibitory cascade, targeting the IL-5 gene transcription machinery. Lactose, a ligand for galectin-3, also totally reverses the effect of the lectin, indicating, as in the case of reversal by the Ab, the specificity of the galectin action.
The observation that galectin-3 acts not only on eosinophils but also in PBMC and a human T cell line specific for the major Ag of olive pollen suggests that the inhibitory mechanism of galectin-3 constitutes a general mechanism not only ascribed to eosinophils. Furthermore, galectin-3 does not promote any detectable apoptotic mechanisms in our conditions, ruling out a possible cytotoxic effect of the recombinant human galectin-3 used in our cultures.
We think that galectin-3 inhibition of IL-5 synthesis is at the nuclear level, by inhibition of the production of the primary transcript, because we have observed complete blockade of IL-5 mRNA. Our present work is related to the possible effect of galectin-3 on negative regulatory elements in the promoter region that can influence the transcriptional activity of the IL-5 gene (25).
In relation to the synthesis and release of IL-5 by different cells
(Table I), we have observed different patterns of production and
inhibition by galectin-3 depending on the stimuli and cell type used.
First of all, we observed no IL-5 protein released in the absence of
any stimuli, even in cells from allergic patients. When we use
anti-CD3 and PDBu for PBMC (21), specific Ag for the T cell line,
or anti-CD32 for the eosinophilic cell line, we found IL-5 in the
supernatants. When we subsequently added galectin-3, this production
was inhibited, reaching 100% in Ag-specific T cells and a lesser
inhibition (
50%) in other cells.
In regard to IL-5 production by eosinophils, there is controversy in the literature. The presence of mRNA for IL-5 in these cells has been demonstrated using in situ hybridization or RT-PCR (26). However, evidence for the secretion of IL-5 protein by eosinophils has only been documented by Dubucquoi et al. (27) after immune complex stimulation.
We have been unable to demonstrate IL-5 synthesis in the supernatants
of unstimulated eosinophils. Only by previous stimulation of FcRII
(CD32), by doubling the number of cells in culture, and by using
concentrated supernatants was IL-5 demonstrated (Table I). This
production was also partially inhibited by galectin-3.
There is a difference between the experimental conditions for the study
of the inhibitory activity of galectin-3 on IL-5 message and IL-5
production. In the first case, the inhibition was 100%; the inhibitory
effect was partial when measured in terms of IL-5 synthesis (Table I).
In both cases, the experimental conditions were different. In the case
of mRNA detection (Figs. 1 and 2), cells were without any stimulation,
and in the case of IL-5 detection in the supernatants (Table I), cells
were given different stimuli. Therefore, it seems difficult to adjust
the experimental conditions of galectin-3 inhibition in the case of
strongly stimulated and nonstimulated cells. For these reason, data for
mRNA and IL-5 synthesis should not be compared. Only in the case of a
selective stimulation using Ag in a specific T cell line was inhibition
100%, as in the case of mRNA.
mRNAs for granulocyte-macrophage CSF (GM-CSF) and IL-3 have been
reported in in vitro stimulated eosinophils (28, 29). Nevertheless,
unstimulated EoL-3 cells, human eosinophils, and PBMC from allergic
patients were incubated with and without galectin-3, and the results
were consistently negative with regard to the mRNA for IFN-, GM-CSF,
and IL-3 and were positive for the internal controls (data not
shown).
The data presented here raise some interesting questions. It is well known that the allergic-inflammatory response is defined by a Th2 response closely connected to migration of eosinophils to the inflammatory focus and to a selective release of different inflammatory mediators. The fact that galectin-3 directly shut down the IL-5 pathway opens new possibilities in the regulation of the Th2-dependent allergic reaction. Migration of eosinophils to the inflammatory focus is directed mainly by IL-5 and IL-3, GM-CSF, and eotaxin, some of which are released from Th2 cells (30, 31). The fact that galectin-3 is able to regulate IL-5 levels suggests that they can operate in the differentiation, activation, and posterior migration of eosinophils, resulting in a negative feedback mechanism that may regulate the number of eosinophils in the inflammatory reaction.
In summary, the results presented here describe for the first time the role of galectin-3 in the regulation of a Th2-allergic response. Further investigations will be needed to elucidate which mechanisms are involved in this process.
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Acknowledgments |
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Footnotes |
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2 Address correspondence and reprint requests to Dr. Carlos Lahoz, Immunology Department, Fundación Jiménez Díaz, 28040 Madrid, Spain. E-mail address:
3 Abbreviations used in this paper: Tm-5, melting temperature -5°C; PDBu, phorbol 12,13-dibutyrate; GM-CSF, granulocyte-macrophage colony-stimulating factor.
Received for publication October 14, 1997. Accepted for publication February 13, 1998.
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References |
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TopAbstractIntroductionMaterials and MethodsResultsDiscussionReferences |
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BP) of the S-type lectin family: role in IgE-dependent activation. J. Exp. Med. 177:243.BP) expressed by human eosinophils: implication in IgE-dependent eosinophil cytotoxicity. Eur. J. Immunol. 23:3230.[Medline]
BP/Mac-2), stimulates superoxide production by neutrophils. J. Immunol. 154:3479.[Abstract]
BP, a ß-galactoside-binding animal lectin, recognizes IgE receptor (FcRI) and activates mast cells. Biochemistry 32:7644.[Medline]
BP, an IgE-binding endogenous lectin. Cell. Immunol. 156:1.[Medline]
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