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Brief Definitive Reports

Antonio Sica^*,, Alessandra Saccani^*, Alessandro Borsatti^*, Christine A. Power^||, Timothy N.C. Wells^||, Walter Luini, Nadia Polentarutti^*, Silvano Sozzani^*, and Alberto Mantovani^*,

From the ^* Istituto di Ricerche Farmacologiche "Mario Negri", 20157 Milan, Italy; Laboratory of Molecular Biology, Istituto G. Gaslini, 16148 Genova-Quarto, Italy; Section of Pathology and Immunolgy, Department of Biotechnology, University of Brescia, 25123 Italy; ^|| Geneva Biomedical Research Institute, Glaxo Wellcome Research and Development, 1228 Plan-les-Ouates, Geneva, Switzerland.

	Abstract

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The present study was designed to investigate the effect of bacterial lipopolysaccharide (LPS) on C–C chemokine receptors (CCR) expressed in human mononuclear phagocytes. LPS caused a rapid and drastic reduction of CCR2 mRNA levels, which binds MCP-1 and -3. CCR1 and CCR5 mRNAs were also reduced, though to a lesser extent, whereas CXCR2 was unaffected. The rate of nuclear transcription of CCR2 was not affected by LPS, whereas the mRNA half life was reduced from 1.5 h to 45 min. As expected, LPS-induced inhibition of CCR2 mRNA expression was associated with a reduction of both MCP-1 binding and chemotactic responsiveness. The capacity to inhibit CCR2 expression in monocytes was shared by other microbial agents and cytokines (inactivated Streptococci, Propionibacterium acnes, and to a lesser extent, IL-1 and TNF-). In contrast, IL-2 augmented CCR2 expression and MCP-1 itself had no effect. These results suggest that, regulation of receptor expression in addition to agonist production is likely a crucial point in the regulation of the chemokine system.

The recruitment of leukocytes from the blood compartment represents one of the characteristic elements of the inflammatory process (1). Locally produced chemotactic agents are believed to play a crucial role in the activation of cells during the multistep process of leukocyte accumulation in tissues (2, 3).

In the past few years a new superfamily of chemotactic cytokines, named chemokines, has been described. The hallmark of this family are four conserved cysteine residues (4–7). According to the relative position of the first two cysteines it is possible to distinguish two main families: the C-X-C (or ) chemokines, which are primarily active on neutrophils, but show some action on T lymphocytes (4–7); and the C–C (or β) chemokines that exert their action on multiple leukocytes populations, including monocytes, basophils, eosinophils, T lymphocytes, NK and dendritic cells (4–10). Recently, a third type of protein (the C or chemokines) was described, which is active on T lymphocytes and NK cells. This protein is characterized by the absence of the first and third cysteines, but shows overall sequence identity with C–C chemokines (11, 12).

Chemokines, as well as classical chemotactic agonists, such as formylated peptides (of which FMLP is the prototype) and C5a, bind to and activate a family of rhodopsin-like GTP-binding protein-coupled seven-transmembrane domain receptors (13–15). Five receptors for C–C chemokines, now named CCR1 through 5, have been identified and cloned (14–17). In addition to recognizing chemokines, usually with some degree of promiscuity, C–C chemokine receptors act as coreceptors for primate lentiviruses such as HIV-1, HIV-2, and SIV (18–22). In particular CCR5 is a major determinant of the interaction of HIV-1 with mononuclear phagocytes (17–22).

MCP-1 is a prototypic C–C chemokine active on mononuclear phagocytes, basophils, T cells and NK cells (4, 8, 10). It is produced by a variety of cell types, including endothelial cells and cells of the monocyte-macrophage lineage, in response to diverse inflammatory signals, typically IL-1, TNF-, and bacterial LPS. MCP-1 interacts with CCR2, of which two isoforms have been cloned and termed A and B (23). In monocytes and NK cells CCR2 is expressed predominantly as B isoform, with vanishingly low levels of A transcripts (23a). In addition to MCP-1, CCR2 recognizes MCP-3 (24–26). Although the regulation of chemokine production has been extensively investigated, little is known as to whether microenvironmental signals may affect the chemokine system by modulating receptor expression (27, 28). This lack of information, and previous observations demonstrating that LPS modulates the in vitro replication as well as the establishment of productive HIV-1 infection in cultured macrophages (29–31), prompted us to investigate the possible effect of LPS on the expression of C–C chemokine receptors. Here, we report that LPS rapidly downregulates CCR2 and, to a lesser extent, CCR1 and CCR5 expression in monocytes by acting on mRNA stability.

	Materials and Methods

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Cells.
Human monocytes were separated from peripheral blood of human healthy donors by Percoll gradient centrifugation (32). Monocytes (98% pure as assessed by morphology) were resuspended at 10⁷/ml in RPMI 1640 supplemented with 10% of fetal bovine serum, 2 mM glutamine and antibiotics. All reagents contained less than 0.125 EU/ml of endotoxin as checked by Limulus Amebocyte Lysate assay (Microbiological Associates, Walkerville, MD).

Cytokines and Reagents.
Human recombinant IL-1β was a gift of Dr. Boraschi (Dompè, L'Aquila, Italy); TNF, from BASF/Knoll (Ludwighafen, Germany); IL-2, from Eurocetus (Milan, Italy); LPS (E. coli 055:B5) from Difco (Detroit, MI); Actinomycin D (ActD) from Sigma Chem. Co. (St. Louis, MO); MCP-1, from PeproTech Inc. (Rocky Hill, NC); inactivated Streptococci (OK432) from Chugai Pharmaceutical Co., Ltd. (Osaka, Japan); Candida Albicans from American Type Culture Collection (Rockville, MD); Glucan from Dr. N.R. Di Luzio (Tulane University School of Medicine, New Orleans, LA); P. Acnes from Wellcome Biotecnology Ltd. (Beckenham, UK).

Migration Assay.
Cell migration was evaluated using a chemotaxis microchamber technique (33) as previously described (32). 27 µl of chemoattractant solution or control medium (RPMI 1640 with 1% FCS) were added to the lower wells of a chemotaxis chamber (Neuroprobe, Pleasanton, CA). A polycarbonate filter (5-µm pore size; Neuroprobe) was layered onto the wells, covered with a silicon gasket and with the top plate. 50 µl of cell suspension (1.5 x 10⁶/ml monocytes in PBMC) were seeded in the upper chamber. The chamber was incubated at 37°C in air with 5% CO₂ for 90 min. At the end of the incubation, filters were removed, stained with Diff-Quik (Baxter s.p.a., Rome, Italy) and five high power oil-immersion fields were counted.

Receptor Binding Assays.
Competition for the binding of [¹²⁵I] MCP-1 (specific activity 2,200 Ci/mmol; Du Pont de Nemours, Bad Homburg, Germany) to Percoll-purified human monocytes was carried out as described previously (26). Monocytes (1 x 10⁷/ml) in binding medium (RPMI 1640 with 10 mg/ml bovine serum albumin; Sigma, Milan, Italy) were incubated with 1 nM of labeled cytokine in the presence of different concentrations of unlabeled cytokine at 4°C for 2 h. At the end of the incubation, cells were pelleted through a cushion of silicon oil by micro-centrifugation. The radioactivity present in the tip of the tubes and in the supernatants was evaluated by using a gamma counter. IC₅₀ values for the different ligands were calculated using "ALLFIT" program as previously described (26).

Northern Blot Analysis.
Total RNA was isolated by the guanidium isothiocyanate method as previously described (34). 15 µg of total RNA from each sample were electrophoresed under denaturing conditions, blotted onto Nytran membranes (Schleicher & Schuell Inc., Keene, NH), and cross-linked by UV irradiation. cDNAs were labeled by random priming and -[³²P]dCTP. CCR2B cDNA was obtained by PCR amplification of the reported sequence (23, 35). CCR1 and CCR5 cDNAs were obtained as previously described (16). The IL-8RB (CXCR2) cDNA clone (27) was kindly donated by Dr. Ji Ming Wang (National Cancer Institute, Frederick, MD).

Nuclear Run-off Experiments.
Nuclear run-off experiments were performed essentially as described (34). Nuclei were isolated after 4 h of stimulation. Then 60 µl of 5x run-off buffer (25 mM TrisHCl, pH 8, 12.5 mM MgCl₂, 750 mM KCl, and 1.25 mM each of ATP, CTP, and GTP), 2 µl of RNase inihibitors 1 U/µl (Perkin Elmer Cetus), 200 µCi of -[³²P]UTP 3,000 Ci/mmol (Amersham) were added to 220 µl of nuclei suspension and incubated at 30°C for 30 min. Elongated transcripts were then isolated using the guanidine/cesium procedure,with 50 µg of yeast tRNA added as carrier. The RNA pellet was resuspended in 180 µl of ice-cold TNE (NaCl 100 mM, 10 mM Tris-HCl, pH 8, 1 mM EDTA, pH 8) and denaturated adding 20 µl of 2N NaOH on ice for 10 min. The solution was neutralized by the addition of 200 µl of 0.48 M Hepes. RNA was precipitated by adding 880 µl of ethanol; the pellet was resuspended in 100 µl of H₂O and radioactivity checked with β-counter. The RNA solution was denaturated at 65°C for 5 min and hybridized at 42°C for 48 h to 5 µg of denatured DNA immobilized on nitrocellulose filters in a few milliliters of hybridization solution (200 mM NaHPO₄, pH 7.2, 1mM EDTA, pH 8, SDS 7%; deionized formamide 45%; E. coli tRNA 250 mg/ml). In a given experiment, each filter was hybridized with the same number of cpm. Filters were then washed one or two times at 37°C for 20–30 min in 40 mM NaHPO₄-SDS 1% and exposed for autoradiography.

	Results

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Inhibition of CCR2 mRNA Expression by LPS.
Human monocytes express high levels of CCR1, CCR2, and CCR5 transcripts (Fig. 1). CCR3 and 4 were undetectable by Northern analysis under these conditions (not shown). Using either a CCR2A or a CCR2B cDNA–specific probes, we detected a single 3.4-kb transcript, as previously reported (23, 23a). As shown in Fig. 1, LPS induced a dosedependent inhibition of the steady state level of CCR2 mRNA after 4 h, with a dramatic inhibition already at 1 ng/ml (Fig. 1 A) and virtually complete suppression at increasing concentrations, 10 and 100 ng/ml. Removal of the LPS after 4 h resulted in a gradual and complete restoration of the CCR2 mRNA level in 24 h (data not shown). Similar results were obtained by using the CCR2A cDNA– specific probe (data not shown). Likewise, but to a lesser extent, a significant LPS-dependent reduction of the CCR1 (Fig. 1 B) and CCR5 (C) mRNA levels was observed. In contrast, the mRNA level of CXCR2 was unaffected (Fig. 1 D).

View larger version (12K): [in this window] [in a new window] [Download PPT slide]   Figure 1 Effect of LPS on the CCR2 (A), CCR1 (B), CCR5 (C) and CXCR2 (D) mRNA expression: dose-response analysis. E shows the ethidium bromide stained ribosomal RNA. A is representative of four different donors. B and C are representative of two different donors. Total RNA was purified from fresh human monocytes incubated for 4 h as indicated.

 
LPS Destabilizes CCR2 mRNA.
Having established that low concentrations of LPS cause a rapid and drastic reduction of CCR2, subsequent work was focused mainly on this receptor. To investigate the mechanism of LPS action, we estimated its effects on both mRNA stability and gene transcription (Fig. 2). ActD (1 µg/ml) was added to fresh human monocytes in the presence or absence of 100 ng/ml of LPS and total RNA was extracted at different times as indicated. In the presence of ActD the estimated half-life of the transcript was about 1.5 h (Fig. 2, lanes 2–6), while cotreatment with ActD and LPS (lanes 7–11) considerably shortened this time (45 min). To evaluate the effects of LPS on gene transcription, we used nuclear run-off analysis (Fig. 2 C). In agreement with published results (34), LPS was able to induce MCP-1 gene transcription. In contrast, LPS did not induce appreciable variations on the transcription rate of the CCR2, CCR1, and CCR5 genes. Taken together, these data indicate that the inhibitory action of LPS on CCR2 gene expression is posttranscriptional and suggest similarities of the mechanisms controlling gene expression of the three β chemokine receptors studied here.

View larger version (35K): [in this window] [in a new window] [Download PPT slide]   Figure 2 Destabilization of CCR2 mRNA by LPS. (A) effect of LPS (100 ng/ml) on the CCR2B mRNA transcript stability. Total RNA was purified from fresh human monocytes incubated for 4 h as indicated. B shows the ethidium bromide stained ribosomal RNA. (C) Nuclear runoff analysis of the MCP-1, CCR1, CCR2, and CCR5 genes. Fresh human monocytes were incubated with 100 ng/ml of LPS for different periods as indicated.

 
LPS Downregulates MCP-1 Binding and Chemotaxis.
MCP-1 is a high-affinity ligand for the CCR2 receptor (23). Therefore we measured the [¹²⁵I]MCP-1 binding in untreated and LPS-treated fresh human monocytes. As shown in Fig. 3 A, a significant time-dependent inhibition of the [¹²⁵I]MCP-1 binding was observed after LPS treatment, which resulted in 60% of reduction after 5 h. Likewise, LPS treatment induced a strong decrease in the number of monocytes migrating in response to MCP-1 (Fig. 3 B). Thus, in human monocytes the LPS-mediated inhibition of CCR2 expression results in a marked reduction of both binding and migratory response to MCP-1, with the latter being much more sensitive to the action of LPS. A stronger inhibition of chemotaxis compared to receptor binding was previously described also for IL-8 (27).

View larger version (11K): [in this window] [in a new window] [Download PPT slide]   Figure 3 Inhibition by LPS of MCP-1 binding and chemotaxis. (A) Binding. fresh human monocytes were incubated for 1–5 h in the presence or absence of 100 ng/ml of LPS before [125I]MCP-1 binding assay. Results are expressed as percent of bound on total counts. (B) Chemotaxis. Fresh human monocytes were stimulated with 100 ng/ml of LPS and chemotactic response to MCP-1 (100 ng/ml) was measured after different periods as indicated.

 
Effect of Other Microbial Agents and Cytokines on CCR2 Expression.
Having established that LPS rapidly inhibits CCR2 expression, we wanted to investigate whether other microbial agents or components and cytokines affected this chemokine receptor. We tested agents (e.g., inactivated Streptococci, Propionibacterium acnes, Candida albicans, glucan) known to affect various functions of monocytes, including chemokine production (36, 37). As shown in Fig. 4 A, CCR2 gene expression was completely suppressed either by treatment with inactivated Streptococci or P. acnes. Furthermore, the CCR2 mRNA level was also partially affected by Glucan, but not by C. albicans. Among cytokines (Fig. 4 C), we found that IL-2 stimulates CCR2 expression thus extending to monocytes recent results with T lymphocytes and NK cells (23, 28, 35). In contrast, TNF- and IL-1β reduced CCR2 expression and MCP-1 itself had no effect (not shown).

View larger version (15K): [in this window] [in a new window] [Download PPT slide]   Figure 4 Effects of microbial products (A) and cytokines (C) on CCR2 mRNA expression. B and D show the ethidium bromide stained ribosomal RNA of A and C, respectively. Total RNA was purified from fresh human monocytes incubated for 4 h as indicated. (A) lane 1, untreated; lane 2, LPS 100 ng/ml; lane 3, inactivated Streptococci OK432 (0.015 KE/ml); lane 4, P. acnes (10 µg/ml); lane 5, C. albicans (100 µg/ ml); lane 6, Glucan (100 µg/ml). (C) lane 1, untreated; lane 2, IL-2 (1,000 U/ml); lane 3, LPS (100 ng/ml); lane 4, TNF- (500 U/ml); lane 5, IL-1-β (20 ng/ml).

 

	Discussion

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The results presented here show that LPS causes a drastic and rapid downregulation of the expression of CCR2, a receptor for MCP-1 and -3. The ED₅₀ of LPS was 1 ng/ml and half-maximal effect was reached with an optimal dose in 45 min. Inhibition of MCP-1 receptor expression was functionally relevant since LPS-treated monocytes showed a reduced capacity to bind and to respond to MCP-1 chemotactically. Two isoforms of CCR2 (A and B) have been cloned (23). Monocytes and activated NK cells express predominantly a 3.5-kb mRNA encoding the B form, with low levels of A transcripts (23, 35). LPS reduced expression of both isoforms (Fig. 1 and data not shown). Moreover LPS also inhibited expression of CCR1 and CCR5, though to a lesser variable extent than CCR2. The action of LPS on C–C chemokine receptors was specific in that CXCR2 was unaffected. It was previously reported that LPS does not affect the FMLP receptor in neutrophils (7, 27).

Little information is available on regulation of expression of chemokine receptors. In neutrophils, LPS and TNF- were reported to inhibit the expression of IL-8 receptors, while G-CSF increased it (27). IL-2 was shown to induce CCR2 in T lymphocytes and NK cells (23a, 28, 35), an observation confirmed here for monocytes. Interestingly, CCR2 induction in T cells was a slow process, requiring four days of exposure to the cytokine (28). The results reported here show a dramatic, rapid and differential downregulation of chemokine receptors by LPS in monocytes.

LPS did not inhibit the rate of nuclear transcription of CCR2, but did reduce the mRNA half life from 1.5 h to 45 min. This result is in agreement with the observation that the 3'-untranslated region of the mRNAs of several rhodopsin family members, contain AU-rich elements, which correlate with highly regulated short-lived mRNAs (38, 39). Chemokine receptors play a central role in HIV-1 infection (40, 41). In particular CCR5, CCR1, and CCR3 have been involved as coreceptors for macrophage-tropic HIV-1 strains (18–22). The finding that LPS and cytokines reduce expression of these coreceptors may to some extent explain the bidirectional effects of these agents on HIV infection (e.g., 29–31). More in general, they point to the feasibility of targeting C–C chemokine receptor expression, as an alternative to occupancy, to inhibit infection.

LPS and bacterial agents used in the present study, as well as IL-1 and TNF, are potent inducers of various chemokines in monocytes including MCP-1 and -3 (10). The results reported here show that these agents have divergent actions on C–C chemokine production and receptor expression in monocytes. Regulation of CCR chemokine receptor expression, in addition to agonist production, is likely a crucial point for regulation of the chemokine system. We speculate that the divergent effect of certain proinflammatory signals on agonist versus receptor expression may serve to retain mononuclear phagocytes at sites of inflammation, to prevent their reverse transmigration (42), and, possibly, to limit excessive recruitment.

	Acknowledgments

Submitted: 12 November 1996
Revised: 31 December 1996

	References

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1 Mantovani A, Bussolino F & Dejana E. Cytokine regulation of endothelial cell function, FASEB J, 1992, 6, 2591–2599.[Abstract]

2 Butcher EC. Leukocyte-endothelial cell recognition: three (or more) steps to specificity and diversity, Cell, 1991, 67, 1033–1036.[Medline]

3 Springer TA. Traffic signal for lymphocyte recirculation and leukocyte emigration: the mutistep paradigm, Cell, 1994, 76, 301–314.[Medline]

4 Baggiolini M, Dewald B & Moser B. Interleukin-8 and related chemotactic cytokines—CXC and CC chemokines, Adv Immunol, 1994, 55, 99–179.

5 Miller MD & Krangel MS. Biology and biochemistry of the chemokines: a family of chemotactic and inflammatory cytokines, Crit Rev Immunol, 1992, 12, 17–46.[Medline]

6 Schall, T.J. 1994. The Chemokines. In The Cytokine Handbook. A. Thomson, editor. Academic Press, London. 419–460.

7 Ben-Baruch A, Michiel DF & Oppenheim JJ. Signals and receptors involved in recruitment of inflammatory cells, J Biol Chem, 1995, 270, 11703–11706.[Free Full Text]

8 Sozzani S, Locati M, Zhou D, Rieppi M, Luini W, Lamorte G, Bianchi G, Polentarutti N, Allavena P & Mantovani A. Receptors, signal transduction and spectrum of action of monocyte chemotactic protein-1 and related chemokines, J Leukoc Biol, 1995, 57, 788–794.[Abstract]

9 Sozzani S, Sallusto F, Luini W, Zhou D, Piemonti L, Allavena P, Van Damme J, Valitutti S, Lanzavecchia A & Mantovani A. Migration of dendritic cells in response to formyl peptides, C5a and a distinct set of chemokines, J Immunol, 1995, 155, 3292–3295.[Abstract]

10 Mantovani, A., S. Sozzani, P. Proost, and J. Van Damme. 1996. The monocyte chemoattractant protein family. In Chemoattractant Ligands and Their Receptors. R. Horuk, editor. CRC Press, Inc., Boca Raton, FL. 169–192.

11 Kelner GS, Kennedy J, Bacon KB, Kleyensteuber S, Largaespada DA, Jenkins NA, Copeland NG, Bazan JF, Moore KW, Schall TJ & Zlotnik A. Lymphotactin: A cytokine that represents a new class of chemokine, Science (Wash DC), 1994, 266, 1395–1399.[Abstract/Free Full Text]

12 Bianchi G, Sozzani S, Zlotnik A, Mantovani A & Allavena P. Migratory response of human NK cells to lymphotactin, Eur J Immunol, 1996, 26, 3238–3242.[Medline]

13 Horuk R. The interleukin-8-receptor family—from chemokines to malaria, Immunol Today, 1994, 15, 169–174.[Medline]

14 Murphy PM. The molecular biology of leukocyte chemoattractant receptors, Annu Rev Immunol, 1994, 12, 593–633.[Medline]

15 Gerard C & Gerard NP. C5A anaphylatoxin and its seven transmembrane-segment receptor, Annu Rev Immunol, 1994, 12, 775–808.[Medline]

16 Power CA, Proudfoot AEI, Magnenat E, Bacon KB & Wells TNC. Molecular cloning and characterisation of a neutrophil chemotactic protein from porcine platelets, Eur J Biochem, 1994, 221, 713–719.[Medline]

17 Samson M, Labbe O, Mollereau C, Vassart G & Parmentier M. Molecular cloning and functional expression of a new human CC-chemokine receptor gene, Biochemistry, 1996, 35, 3362–3367.[Medline]

18 Deng H K, Liu R, Ellmeier W, Choe S, Unutmaz D, Burkhart M, Di Marzio P, Marmon S, Sutton RE, Hill CM et al.. Identification of a major co-receptor for primary isolates of HIV-1, Nature(Lond), 1996, 381, 661–666.[Medline]

19 Dragic T, Litwin V, Allaway GP, Martin SR, Huang YX, Nagashima KA, Cayanan C, Maddon PJ, Koup RA, Moore JP & Paxton WA. HIV-1 entry into CD4(+) cells is mediated by the chemokine receptor CC-CKR-5, Nature(Lond), 1996, 381, 667–673.[Medline]

20 Choe H, Farzan M, Sun Y, Sullivan N, Rollins B, Ponath PD, Wu LJ, Mackay CR, Larosa G, Newman W et al.. The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates, Cell, 1996, 85, 1135–1148.[Medline]

21 Doranz BJ, Rucker J, Yi YJ, Smyth RJ, Samson M, Peiper SC, Parmentier M, Collman RG & Doms RW. A dual-tropic primary HIV-1 isolate that uses fusin and the beta-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors, Cell, 1996, 85, 1149–1158.[Medline]

22 Alkhatib G, Combadiere C, Broder CC, Feng Y, Kennedy PE, Murphy PM & Berger EA. CC CKRS: a RANTES, MIP-1 alpha, MIP-1 beta receptor as a fusion cofactor for macrophage-tropic HIV-1, Science (Wash DC), 1996, 272, 1955–1958.[Abstract]

23 Charo IF, Myers SJ, Herman A, Franci C, Connolly AJ & Coughlin SR. Molecular cloning and functional expression of two monocyte chemoattractant protein-1 receptors reveals alternative splicing of the carboxyl-terminal tails, Proc Natl Acad Sci USA, 1994, 91, 2752–2756.[Abstract/Free Full Text]

23 Polentarutti, N., P. Allavena, G. Bianchi, G. Giardina, A. Basile, S. Sozzani, A. Montovani, and M. Introna. 1997. IL-2 regulated expression of the monocyte chemotactic protein-1 receptor (CCR2) in human NK cells: characterization of a predominant 3.4 Kb transcript containing CCR2B and CCR2A sequences. J. Immunol. In press.

24 Franci C, Wong LM, Van Damme J, Proost P & Charo IF. Monocyte chemoattractant protein-3, but not monocyte chemoattractant protein-2, is a functional ligand of the human monocyte chemoattractant protein-1 receptor, J Immunol, 1995, 154, 6511–6517.[Abstract]

25 Combadiere C, Ahuja SK, Van Damme J, Tiffany HL, Gao JL & Murphy PM. Monocyte chemoattractant protein-3 is a functional ligand for CC chemokine receptors 1 and 2B, J Biol Chem, 1995, 270, 29671–29675.[Abstract/Free Full Text]

26 Sozzani S, Zhou D, Locati M, Rieppi M, Proost P, Magazin M, Vita N, Van Damme J & Mantovani A. Receptors and transduction pathways for monocyte chemotactic protein-2 and monocyte chemotactic protein-3—similarities and differences with MCP-1, J Immunol, 1994, 152, 3615–3622.[Abstract]

27 Lloyd AR, Biragyn A, Johnston JA, Taub DD, Xu LL, Michiel D, Sprenger H, Oppenheim JJ & Kelvin DJ. Granulocyte-colony stimulating factor and lipopolysaccharide regulate the expression of interleukin 8 receptors on polymorphonuclear leukocytes, J Biol Chem, 1995, 270, 28188–28192.[Abstract/Free Full Text]

28 Loetscher P, Seitz M, Baggiolini M & Moser B. Interleukin-2 regulates CC chemokine receptor expression and chemotactic responsiveness in T lymphocytes, J Exp Med, 1996, 184, 569–577.[Abstract/Free Full Text]

29 Pomerantz RJ, Feinberg MB, Trono D & Baltimore D. Lipopolysaccharide is a potent monocyte/macrophage-specific stimulator of human immunodeficiency virus type 1 expression, J Exp Med, 1990, 172, 253–261.[Abstract/Free Full Text]

30 Bernstein MS, Tong-Starksen SE & Locksley RM. Activation of human monocyte-derived macrophages with lipopolysaccharide decreases human immunodeficiency virus replication in vitro at the level of gene expression, J Clin Invest, 1991, 88, 540–545.[Medline]

31 Kornbluth RS, Oh PS, Munis JR, Cleveland PH & Richman DD. Interferons and bacterial lipopolysaccharide protect macrophages from productive infection by human immunodeficiency virus in vitro, J Exp Med, 1989, 169, 1137–1151.[Abstract/Free Full Text]

32 Sozzani S, Luini W, Molino M, Jílek P, Bottazzi B, Cerletti C, Matsushima K & Mantovani A. The signal transduction pathway involved in the migration induced by a monocyte chemotactic cytokine, J Immunol, 1991, 147, 2215–2221.[Abstract]

33 Falk W, Goodwin RH Jr & Leonard EJ. A 48well microchemotaxis assembly for rapid and accurate measurement of leukocyte migration, J Immunol Methods, 1980, 33, 239–245.[Medline]

34 Sica A, Wang JM, Colotta F, Dejana E, Mantovani A, Oppenheim JJ, Larsen CG, Zachariae CO & Matsushima K. Monocyte chemotactic and activating factor gene expression induced in endothelial cells by IL-1 and tumor necrosis factor, J Immunol, 1990, 144, 3034–3038.[Abstract]

35 Allavena P, Bianchi G, Giardina P, Polentarutti N, Zhou D, Introna M, Sozzani S & Mantovani A. Migratory response of human NK cells to monocyte-chemotactic proteins, Methods, 1996, 10, 145–149.[Medline]

36 Colotta F, Re F, Polentarutti N, Sozzani S & Mantovani A. Modulation of granulocyte survival and programmed cell death by cytokines and bacterial products, Blood, 1992, 80, 2012–2020.[Abstract/Free Full Text]

37 Barlin E, Leser H-L, Resch K & Gemsa D. In vivo activation of macrophages by Corynebacterium parcum, pyran copolymer and glucan, Int Arch Allergy Appl Immunol, 1981, 66, 180–182.

38 Shaw G & Kamen R. A conserved AU sequence from the 3' untranslated region of GM-CSF mRNA mediates selective mRNA degradation, Cell, 1986, 46, 659–667.[Medline]

39 Collins S, Caron MG & Lefkowitz RJ. Regulation of adrenergic receptor responsiveness through modulation of receptor gene expression, Annu Rev Physiol, 1991, 53, 497–508.[Medline]

40 Schmidtmayerova H, Sherry B & Bukrinsky M. Chemokines and HIV replication, Nature (Lond), 1996, 382, 767, .[Medline]

41 Bates P. Chemokine receptors and HIV-1: an attractive pair? , Cell, 1996, 86, 1–3.[Medline]

42 Randolph GJ & Furie MB. Mononuclear phagocytes egress from an in vitro model of the vascular wall by migrating across endothelium in the basal to apical direction: role of intracellular adhesion molecule 1 and the CD11/ CD18 integrins, J Exp Med, 1996, 183, 451–462.[Abstract/Free Full Text]

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• Hu, Y., Hu, X., Boumsell, L., Ivashkiv, L. B. (2008). IFN-{gamma} and STAT1 Arrest Monocyte Migration and Modulate RAC/CDC42 Pathways. J. Immunol. 180: 8057-8065 [Abstract] [Full Text]  
• Silva, T.A., Garlet, G.P., Fukada, S.Y., Silva, J.S., Cunha, F.Q. (2007). Chemokines in Oral Inflammatory Diseases: Apical Periodontitis and Periodontal Disease. JDR 86: 306-319 [Abstract] [Full Text]  
• Chunsong, H., Yuling, H., Li, W., Jie, X., Gang, Z., Qiuping, Z., Qingping, G., Kejian, Z., Li, Q., Chang, A. E., Youxin, J., Jinquan, T. (2006). CXC Chemokine Ligand 13 and CC Chemokine Ligand 19 Cooperatively Render Resistance to Apoptosis in B Cell Lineage Acute and Chronic Lymphocytic Leukemia CD23+CD5+ B Cells. J. Immunol. 177: 6713-6722 [Abstract] [Full Text]  
• Heesen, M., Renckens, R., de Vos, A. F., Kunz, D., van der Poll, T. (2006). Human Endotoxemia Induces Down-Regulation of Monocyte CC Chemokine Receptor 2. CVI 13: 156-159 [Abstract] [Full Text]  
• Mandal, P., Novotny, M., Hamilton, T. A. (2005). Lipopolysaccharide Induces Formyl Peptide Receptor 1 Gene Expression in Macrophages and Neutrophils via Transcriptional and Posttranscriptional Mechanisms. J. Immunol. 175: 6085-6091 [Abstract] [Full Text]  
• Sen, Y., Yongyi, B., Yuling, H., Luokun, X., Li, H., Jie, X., Tao, D., Gang, Z., Junyan, L., Chunsong, H., Zhang, X., Youxin, J., Feili, G., Boquan, J., Jinquan, T. (2005). V{alpha}24-Invariant NKT Cells from Patients with Allergic Asthma Express CCR9 at High Frequency and Induce Th2 Bias of CD3+ T Cells upon CD226 Engagement. J. Immunol. 175: 4914-4926 [Abstract] [Full Text]  
• Srivastava, M., Jung, S., Wilhelm, J., Fink, L., Buhling, F., Welte, T., Bohle, R. M., Seeger, W., Lohmeyer, J., Maus, U. A. (2005). The Inflammatory versus Constitutive Trafficking of Mononuclear Phagocytes into the Alveolar Space of Mice Is Associated with Drastic Changes in Their Gene Expression Profiles. J. Immunol. 175: 1884-1893 [Abstract] [Full Text]  
• Pettersson, A., Sabirsh, A., Bristulf, J., Kidd-Ljunggren, K., Ljungberg, B., Owman, C., Karlsson, U. (2005). Pro- and anti-inflammatory substances modulate expression of the leukotriene B4 receptor, BLT1, in human monocytes. J. Leukoc. Biol. 77: 1018-1025 [Abstract] [Full Text]  
• Tao, D., Shangwu, L., Qun, W., Yan, L., Wei, J., Junyan, L., Feili, G., Boquan, J., Jinquan, T. (2005). CD226 Expression Deficiency Causes High Sensitivity to Apoptosis in NK T Cells from Patients with Systemic Lupus Erythematosus. J. Immunol. 174: 1281-1290 [Abstract] [Full Text]  
• Maus, U. A., Wellmann, S., Hampl, C., Kuziel, W. A., Srivastava, M., Mack, M., Everhart, M. B., Blackwell, T. S., Christman, J. W., Schlondorff, D., Bohle, R. M., Seeger, W., Lohmeyer, J. (2005). CCR2-positive monocytes recruited to inflamed lungs downregulate local CCL2 chemokine levels. Am. J. Physiol. Lung Cell. Mol. Physiol. 288: L350-L358 [Abstract] [Full Text]  
• Qiuping, Z., Jei, X., Youxin, J., Wei, J., Chun, L., Jin, W., Qun, W., Yan, L., Chunsong, H., Mingzhen, Y., Qingping, G., Kejian, Z., Zhimin, S., Qun, L., Junyan, L., Jinquan, T. (2004). CC Chemokine Ligand 25 Enhances Resistance to Apoptosis in CD4+ T Cells from Patients with T-Cell Lineage Acute and Chronic Lymphocytic Leukemia by Means of Livin Activation. Cancer Res. 64: 7579-7587 [Abstract] [Full Text]  
• Schecter, A. D., Berman, A. B., Yi, L., Ma, H., Daly, C. M., Soejima, K., Rollins, B. J., Charo, I. F., Taubman, M. B. (2004). MCP-1-dependent signaling in CCR2-/- aortic smooth muscle cells. J. Leukoc. Biol. 75: 1079-1085 [Abstract] [Full Text]  
• Postma, B., Poppelier, M. J., van Galen, J. C., Prossnitz, E. R., van Strijp, J. A. G., de Haas, C. J. C., van Kessel, K. P. M. (2004). Chemotaxis Inhibitory Protein of Staphylococcus aureus Binds Specifically to the C5a and Formylated Peptide Receptor. J. Immunol. 172: 6994-7001 [Abstract] [Full Text]  
• Han, K. H., Hong, K.-H., Park, J.-H., Ko, J., Kang, D.-H., Choi, K.-J., Hong, M.-K., Park, S.-W., Park, S.-J. (2004). C-Reactive Protein Promotes Monocyte Chemoattractant Protein-1--Mediated Chemotaxis Through Upregulating CC Chemokine Receptor 2 Expression in Human Monocytes. Circulation 109: 2566-2571 [Abstract] [Full Text]  
• Parker, L. C., Whyte, M. K. B., Vogel, S. N., Dower, S. K., Sabroe, I. (2004). Toll-Like Receptor (TLR)2 and TLR4 Agonists Regulate CCR Expression in Human Monocytic Cells. J. Immunol. 172: 4977-4986 [Abstract] [Full Text]  
• Schioppa, T., Uranchimeg, B., Saccani, A., Biswas, S. K., Doni, A., Rapisarda, A., Bernasconi, S., Saccani, S., Nebuloni, M., Vago, L., Mantovani, A., Melillo, G., Sica, A. (2003). Regulation of the Chemokine Receptor CXCR4 by Hypoxia. JEM 198: 1391-1402 [Abstract] [Full Text]  
• Qiuping, Z., Qun, L., Chunsong, H., Xiaolian, Z., Baojun, H., Mingzhen, Y., Chengming, L., Jinshen, H., Qingping, G., Kejian, Z., Zhimin, S., Xuejun, Z., Junyan, L., Jinquan, T. (2003). Selectively Increased Expression and Functions of Chemokine Receptor CCR9 on CD4+ T Cells from Patients with T-Cell Lineage Acute Lymphocytic Leukemia. Cancer Res. 63: 6469-6477 [Abstract] [Full Text]  
• Jinquan, T., Jacobi, H. H., Jing, C., Millner, A., Sten, E., Hviid, L., Anting, L., Ryder, L. P., Glue, C., Skov, P. S., Jarman, E., Lamberth, K., Malling, H.-J., Poulsen, L. K. (2003). CCR3 Expression Induced by IL-2 and IL-4 Functioning as a Death Receptor for B Cells. J. Immunol. 171: 1722-1731 [Abstract] [Full Text]  
• Sabroe, I., Prince, L. R., Jones, E. C., Horsburgh, M. J., Foster, S. J., Vogel, S. N., Dower, S. K., Whyte, M. K. B. (2003). Selective Roles for Toll-Like Receptor (TLR)2 and TLR4 in the Regulation of Neutrophil Activation and Life Span. J. Immunol. 170: 5268-5275 [Abstract] [Full Text]  
• Jiankuo, M., Xingbing, W., Baojun, H., Xiongwin, W., Zhuoya, L., Ping, X., Yong, X., Anting, L., Chunsong, H., Feili, G., Jinquan, T. (2003). Peptide Nucleic Acid Antisense Prolongs Skin Allograft Survival by Means of Blockade of CXCR3 Expression Directing T Cells into Graft. J. Immunol. 170: 1556-1565 [Abstract] [Full Text]  
• Baker, C. A., Martin, D., Manuelidis, L. (2002). Microglia from Creutzfeldt-Jakob Disease-Infected Brains Are Infectious and Show Specific mRNA Activation Profiles. J. Virol. 76: 10905-10913 [Abstract] [Full Text]  
• Cui, Y., Le, Y., Yazawa, H., Gong, W., Wang, J. M. (2002). Potential role of the formyl peptide receptor-like 1 (FPRL1) in inflammatory aspects of Alzheimer's disease. J. Leukoc. Biol. 72: 628-635 [Abstract] [Full Text]  
• Menten, P., Saccani, A., Dillen, C., Wuyts, A., Struyf, S., Proost, P., Mantovani, A., Wang, J. M., Van Damme, J. (2002). Role of the autocrine chemokines MIP-1{alpha} and MIP-1{beta} in the metastatic behavior of murine T cell lymphoma. J. Leukoc. Biol. 72: 780-789 [Abstract] [Full Text]  
• Verani, A., Sironi, F., Siccardi, A. G., Lusso, P., Vercelli, D. (2002). Inhibition of CXCR4-Tropic HIV-1 Infection by Lipopolysaccharide: Evidence of Different Mechanisms in Macrophages and T Lymphocytes. J. Immunol. 168: 6388-6395 [Abstract] [Full Text]  
• Locati, M., Deuschle, U., Massardi, M. L., Martinez, F. O., Sironi, M., Sozzani, S., Bartfai, T., Mantovani, A. (2002). Analysis of the Gene Expression Profile Activated by the CC Chemokine Ligand 5/RANTES and by Lipopolysaccharide in Human Monocytes. J. Immunol. 168: 3557-3562 [Abstract] [Full Text]  
• Cui, Y.-H., Le, Y., Gong, W., Proost, P., Van Damme, J., Murphy, W. J., Wang, J. M. (2002). Bacterial Lipopolysaccharide Selectively Up-Regulates the Function of the Chemotactic Peptide Receptor Formyl Peptide Receptor 2 in Murine Microglial Cells. J. Immunol. 168: 434-442 [Abstract] [Full Text]  
• Vaday, G. G., Schor, H., Rahat, M. A., Lahat, N., Lider, O. (2001). Transforming growth factor-{beta} suppresses tumor necrosis factor {alpha}-induced matrix metalloproteinase-9 expression in monocytes. J. Leukoc. Biol. 69: 613-621 [Abstract] [Full Text]  
• Kito, K., Morishita, K., Nishida, K. (2001). MCP-1 receptor binding affinity is up-regulated by pre-stimulation with MCP-1 in an actin polymerization-dependent manner. J. Leukoc. Biol. 69: 666-674 [Abstract] [Full Text]  
• Weber, C., Weber, K. S. C., Klier, C., Gu, S., Wank, R., Horuk, R., Nelson, P. J. (2001). Specialized roles of the chemokine receptors CCR1 and CCR5 in the recruitment of monocytes and TH1-like/CD45RO+ T cells. Blood 97: 1144-1146 [Abstract] [Full Text]  
• Cheng, S. S., Lai, J. J., Lukacs, N. W., Kunkel, S. L. (2001). Granulocyte-Macrophage Colony Stimulating Factor Up-Regulates CCR1 in Human Neutrophils. J. Immunol. 166: 1178-1184 [Abstract] [Full Text]  
• Vaday, G. G., Hershkoviz, R., Rahat, M. A., Lahat, N., Cahalon, L., Lider, O. (2000). Fibronectin-bound TNF-{alpha} stimulates monocyte matrix metalloproteinase-9 expression and regulates chemotaxis. J. Leukoc. Biol. 68: 737-747 [Abstract] [Full Text]  
• Lathey, J. L., Brambilla, D., Goodenow, M. M., Nokta, M., Rasheed, S., Siwak, E. B., Bremer, J. W., Huang, D. D., Yi, Y., Reichelderfer, P. S., Collman, R. G. (2000). Co-receptor usage was more predictive than NSI/SI phenotype for HIV replication in macrophages: is NSI/SI phenotyping sufficient?. J. Leukoc. Biol. 68: 324-330 [Abstract] [Full Text]  
• Smith, P. D., Meng, G., Sellers, M. T., Rogers, T. S., Shaw, G. M. (2000). Biological parameters of HIV-1 infection in primary intestinal lymphocytes and macrophages. J. Leukoc. Biol. 68: 360-365 [Abstract] [Full Text]  
• Franitza, S., Hershkoviz, R., Kam, N.'a., Lichtenstein, N., Vaday, G. G., Alon, R., Lider, O. (2000). TNF-{alpha} Associated with Extracellular Matrix Fibronectin Provides a Stop Signal for Chemotactically Migrating T Cells. J. Immunol. 165: 2738-2747 [Abstract] [Full Text]  
• Jinquan, T., Quan, S., Jacobi, H. H., Jing, C., Millner, A., Jensen, B., Madsen, H. O., Ryder, L. P., Svejgaard, A., Malling, H.-J., Skov, P. S., Poulsen, L. K. (2000). CXC chemokine receptor 3 expression on CD34+ hematopoietic progenitors from human cord blood induced by granulocyte-macrophage colony-stimulating factor: chemotaxis and adhesion induced by its ligands, interferon gamma -inducible protein 10 and monokine induced by interferon gamma. Blood 96: 1230-1238 [Abstract] [Full Text]  
• Hornung, F., Scala, G., Lenardo, M. J. (2000). TNF-{alpha}-Induced Secretion of C-C Chemokines Modulates C-C Chemokine Receptor 5 Expression on Peripheral Blood Lymphocytes. J. Immunol. 164: 6180-6187 [Abstract] [Full Text]  
• Andres, P. G., Beck, P. L., Mizoguchi, E., Mizoguchi, A., Bhan, A. K., Dawson, T., Kuziel, W. A., Maeda, N., MacDermott, R. P., Podolsky, D. K., Reinecker, H.-C. (2000). Mice with a Selective Deletion of the CC Chemokine Receptors 5 or 2 Are Protected from Dextran Sodium Sulfate-Mediated Colitis: Lack of CC Chemokine Receptor 5 Expression Results in a NK1.1+ Lymphocyte-Associated Th2-Type Immune Response in the Intestine. J. Immunol. 164: 6303-6312 [Abstract] [Full Text]  
• Murdoch, C., Finn, A. (2000). Chemokine receptors and their role in inflammation and infectious diseases. Blood 95: 3032-3043 [Abstract] [Full Text]  
• ZEIDLER, R., CSANADY, M., GIRES, O., LANG, S., SCHMITT, B., WOLLENBERG, B. (2000). Tumor cell-derived prostaglandin E2 inhibits monocyte function by interfering with CCR5 and Mac-1. FASEB J. 14: 661-668 [Abstract] [Full Text]  
• Bonecchi, R., Facchetti, F., Dusi, S., Luini, W., Lissandrini, D., Simmelink, M., Locati, M., Bernasconi, S., Allavena, P., Brandt, E., Rossi, F., Mantovani, A., Sozzani, S. (2000). Induction of Functional IL-8 Receptors by IL-4 and IL-13 in Human Monocytes. J. Immunol. 164: 3862-3869 [Abstract] [Full Text]  
• Saccani, A., Saccani, S., Orlando, S., Sironi, M., Bernasconi, S., Ghezzi, P., Mantovani, A., Sica, A. (2000). Redox regulation of chemokine receptor expression. Proc. Natl. Acad. Sci. USA 97: 2761-2766 [Abstract] [Full Text]  
• Nasreen, N., Mohammed, K. A., Galffy, G., Ward, M. J., Antony, V. B. (2000). MCP-1 in pleural injury: CCR2 mediates haptotaxis of pleural mesothelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 278: L591-L598 [Abstract] [Full Text]  
• Franchin, G., Zybarth, G., Dai, W. W., Dubrovsky, L., Reiling, N., Schmidtmayerova, H., Bukrinsky, M., Sherry, B. (2000). Lipopolysaccharide Inhibits HIV-1 Infection of Monocyte- Derived Macrophages Through Direct and Sustained Down-Regulation of CC Chemokine Receptor 5. J. Immunol. 164: 2592-2601 [Abstract] [Full Text]  
• Rajan, A. J., Asensio, V. C., Campbell, I. L., Brosnan, C. F. (2000). Experimental Autoimmune Encephalomyelitis on the SJL Mouse: Effect of {gamma}{delta} T Cell Depletion on Chemokine and Chemokine Receptor Expression in the Central Nervous System. J. Immunol. 164: 2120-2130 [Abstract] [Full Text]  
• Sica, A., Saccani, A., Bottazzi, B., Bernasconi, S., Allavena, P., Gaetano, B., Fei, F., LaRosa, G., Scotton, C., Balkwill, F., Mantovani, A. (2000). Defective Expression of the Monocyte Chemotactic Protein-1 Receptor CCR2 in Macrophages Associated with Human Ovarian Carcinoma. J. Immunol. 164: 733-738 [Abstract] [Full Text]  
• Sica, A., Saccani, A., Bottazzi, B., Polentarutti, N., Vecchi, A., Damme, J. V., Mantovani, A. (2000). Autocrine Production of IL-10 Mediates Defective IL-12 Production and NF-{kappa}B Activation in Tumor-Associated Macrophages. J. Immunol. 164: 762-767 [Abstract] [Full Text]  
• Penton-Rol, G., Cota, M., Polentarutti, N., Luini, W., Bernasconi, S., Borsatti, A., Sica, A., LaRosa, G. J., Sozzani, S., Poli, G., Mantovani, A. (1999). Up-Regulation of CCR2 Chemokine Receptor Expression and Increased Susceptibility to the Multitropic HIV Strain 89.6 in Monocytes Exposed to Glucocorticoid Hormones. J. Immunol. 163: 3524-3529 [Abstract] [Full Text]  
• Weber, K. S. C., Nelson, P. J., Grone, H.-J., Weber, C. (1999). Expression of CCR2 by Endothelial Cells : Implications for MCP-1 Mediated Wound Injury Repair and In Vivo Inflammatory Activation of Endothelium. Arterioscler. Thromb. Vasc. Bio. 19: 2085-2093 [Abstract] [Full Text]  
• Zhu, L., Bisgaier, C. L., Aviram, M., Newton, R. S. (1999). 9-cis Retinoic Acid Induces Monocyte Chemoattractant Protein-1 Secretion in Human Monocytic THP-1 Cells. Arterioscler. Thromb. Vasc. Bio. 19: 2105-2111 [Abstract] [Full Text]  
• Hogaboam, C. M., Bone-Larson, C. L., Lipinski, S., Lukacs, N. W., Chensue, S. W., Strieter, R. M., Kunkel, S. L. (1999). Differential Monocyte Chemoattractant Protein-1 and Chemokine Receptor 2 Expression by Murine Lung Fibroblasts Derived from Th1- and Th2-Type Pulmonary Granuloma Models. J. Immunol. 163: 2193-2201 [Abstract] [Full Text]  
• Singh, A., Besson, G., Mobasher, A., Collman, R. G. (1999). Patterns of Chemokine Receptor Fusion Cofactor Utilization by Human Immunodeficiency Virus Type 1 Variants from the Lungs and Blood. J. Virol. 73: 6680-6690 [Abstract] [Full Text]  
• Fantuzzi, L., Borghi, P., Ciolli, V., Pavlakis, G., Belardelli, F., Gessani, S. (1999). Loss of CCR2 Expression and Functional Response to Monocyte Chemotactic Protein (MCP-1) During the Differentiation of Human Monocytes: Role of Secreted MCP-1 in the Regulation of the Chemotactic Response. Blood 94: 875-883 [Abstract] [Full Text]  
• Worgall, S., Connor, R., Kaner, R. J., Fenamore, E., Sheridan, K., Singh, R., Crystal, R. G. (1999). Expression and Use of Human Immunodeficiency Virus Type 1 Coreceptors by Human Alveolar Macrophages. J. Virol. 73: 5865-5874 [Abstract] [Full Text]  
• Han, K. H., Han, K. O., Green, S. R., Quehenberger, O. (1999). Expression of the monocyte chemoattractant protein-1 receptor CCR2 is increased in hypercholesterolemia: differential effects of plasma lipoproteins on monocyte function. J. Lipid Res. 40: 1053-1063 [Abstract] [Full Text]  
• Foti, M., Granucci, F., Aggujaro, D., Liboi, E., Luini, W., Minardi, S., Mantovani, A., Sozzani, S., Ricciardi-Castagnoli, P. (1999). Upon dendritic cell (DC) activation chemokines and chemokine receptor expression are rapidly regulated for recruitment and maintenance of DC at the inflammatory site. Int Immunol 11: 979-986 [Abstract] [Full Text]  
• Draude, G., von Hundelshausen, P., Frankenberger, M., Ziegler-Heitbrock, H. W. L., Weber, C. (1999). Distinct scavenger receptor expression and function in the human CD14+/CD16+ monocyte subset. Am. J. Physiol. Heart Circ. Physiol. 276: H1144-H1149 [Abstract] [Full Text]  
• Rahimpour, R., Mitchell, G., Khandaker, M. H., Kong, C., Singh, B., Xu, L., Ochi, A., Feldman, R. D., Pickering, J. G., Gill, B. M., Kelvin, D. J. (1999). Bacterial Superantigens Induce Down-Modulation of CC Chemokine Responsiveness in Human Monocytes Via an Alternative Chemokine Ligand-Independent Mechanism. J. Immunol. 162: 2299-2307 [Abstract] [Full Text]  
• Hariharan, D., Douglas, S. D., Lee, B., Lai, J.-P., Campbell, D. E., Ho, W.-Z. (1999). Interferon-gamma Upregulates CCR5 Expression in Cord and Adult Blood Mononuclear Phagocytes. Blood 93: 1137-1144 [Abstract] [Full Text]  
• Zybarth, G., Reiling, N., Schmidtmayerova, H., Sherry, B., Bukrinsky, M. (1999). Activation-Induced Resistance of Human Macrophages to HIV-1 Infection In Vitro. J. Immunol. 162: 400-406 [Abstract] [Full Text]  
• Bonecchi, R., Polentarutti, N., Luini, W., Borsatti, A., Bernasconi, S., Locati, M., Power, C., Proudfoot, A., Wells, T. N. C., Mackay, C., Mantovani, A., Sozzani, S. (1999). Up-Regulation of CCR1 and CCR3 and Induction of Chemotaxis to CC Chemokines by IFN-{gamma} in Human Neutrophils. J. Immunol. 162: 474-479 [Abstract] [Full Text]  
• Han, K. H., Tangirala, R. K., Green, S. R., Quehenberger, O. (1998). Chemokine Receptor CCR2 Expression and Monocyte Chemoattractant Protein-1–Mediated Chemotaxis in Human Monocytes : A Regulatory Role for Plasma LDL. Arterioscler. Thromb. Vasc. Bio. 18: 1983-1991 [Abstract] [Full Text]  
• Huang, L., Bosch, I., Hofmann, W., Sodroski, J., Pardee, A. B. (1998). Tat Protein Induces Human Immunodeficiency Virus Type 1 (HIV-1) Coreceptors and Promotes Infection with both Macrophage-Tropic and T-Lymphotropic HIV-1 Strains. J. Virol. 72: 8952-8960 [Abstract] [Full Text]  
• Wahl, S. M., Greenwell-Wild, T., Peng, G., Hale-Donze, H., Doherty, T. M., Mizel, D., Orenstein, J. M. (1998). Mycobacterium avium complex augments macrophage HIV-1 production and increases CCR5 expression. Proc. Natl. Acad. Sci. USA 95: 12574-12579 [Abstract] [Full Text]  
• Wang, J., Roderiquez, G., Oravecz, T., Norcross, M. A. (1998). Cytokine Regulation of Human Immunodeficiency Virus Type 1 Entry and Replication in Human Monocytes/Macrophages through Modulation of CCR5 Expression. J. Virol. 72: 7642-7647 [Abstract] [Full Text]  
• Khandaker, M. H., Xu, L., Rahimpour, R., Mitchell, G., DeVries, M. E., Pickering, J. G., Singhal, S. K., Feldman, R. D., Kelvin, D. J. (1998). CXCR1 and CXCR2 Are Rapidly Down-Modulated by Bacterial Endotoxin Through a Unique Agonist-Independent, Tyrosine Kinase-Dependent Mechanism. J. Immunol. 161: 1930-1938 [Abstract] [Full Text]  
• Sozzani, S., Allavena, P., D'Amico, G., Luini, W., Bianchi, G., Kataura, M., Imai, T., Yoshie, O., Bonecchi, R., Mantovani, A. (1998). Cutting Edge: Differential Regulation of Chemokine Receptors During Dendritic Cell Maturation: A Model for Their Trafficking Properties. J. Immunol. 161: 1083-1086 [Abstract] [Full Text]  
• Thivierge, M., Le Gouill, C., Tremblay, M. J., Stankova, J., Rola-Pleszczynski, M. (1998). Prostaglandin E2 Induces Resistance to Human Immunodeficiency Virus-1 Infection in Monocyte-Derived Macrophages: Downregulation of CCR5 Expression by Cyclic Adenosine Monophosphate. Blood 92: 40-45 [Abstract] [Full Text]  
• Penton-Rol, G., Polentarutti, N., Luini, W., Borsatti, A., Mancinelli, R., Sica, A., Sozzani, S., Mantovani, A. (1998). Selective Inhibition of Expression of the Chemokine Receptor CCR2 in Human Monocytes by IFN-{gamma}. J. Immunol. 160: 3869-3873 [Abstract] [Full Text]  
• Ghorpade, A., Xia, M. Q., Hyman, B. T., Persidsky, Y., Nukuna, A., Bock, P., Che, M., Limoges, J., Gendelman, H. E., Mackay, C. R. (1998). Role of the beta -Chemokine Receptors CCR3 and CCR5 in Human Immunodeficiency Virus Type 1 Infection of Monocytes and Microglia. J. Virol. 72: 3351-3361 [Abstract] [Full Text]  
• Gupta, S. K., Lysko, P. G., Pillarisetti, K., Ohlstein, E., Stadel, J. M. (1998). Chemokine Receptors in Human Endothelial Cells. FUNCTIONAL EXPRESSION OF CXCR4 AND ITS TRANSCRIPTIONAL REGULATION BY INFLAMMATORY CYTOKINES. J. Biol. Chem. 273: 4282-4287 [Abstract] [Full Text]  
• Luster, A. D. (1998). Chemokines -- Chemotactic Cytokines That Mediate Inflammation. NEJM 338: 436-445 [Full Text]  
• Yi, Y., Rana, S., Turner, J. D., Gaddis, N., Collman, R. G. (1998). CXCR-4 Is Expressed by Primary Macrophages and Supports CCR5-Independent Infection by Dual-Tropic but Not T-Tropic Isolates of Human Immunodeficiency Virus Type 1. J. Virol. 72: 772-777 [Abstract] [Full Text]  
• Kuziel, W. A., Morgan, S. J., Dawson, T. C., Griffin, S., Smithies, O., Ley, K., Maeda, N. (1997). Severe reduction in leukocyte adhesion and monocyte extravasation in mice deficient in CC chemokine receptor 2. Proc. Natl. Acad. Sci. USA 94: 12053-12058 [Abstract] [Full Text]  
• Wang, J., Guan, E., Roderiquez, G., Calvert, V., Alvarez, R., Norcross, M. A. (2001). Role of Tyrosine Phosphorylation in Ligand-independent Sequestration of CXCR4 in Human Primary Monocytes-Macrophages. J. Biol. Chem. 276: 49236-49243 [Abstract] [Full Text]  

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