Jo Van Damme

University of Leuven, Louvain, Flemish, Belgium

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Publications (536)2222.48 Total impact

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    ABSTRACT: Post-translational modification of chemokines is an essential regulatory mechanism to enhance or dampen the inflammatory response. CD26/dipeptidylpeptidase IV, ubiquitously expressed in tissues and blood, removes NH2-terminal dipeptides from proteins with a penultimate Pro or Ala. A large number of human chemokines, including CXCL2, CXCL6, CXCL9, CXCL10, CXCL11, CXCL12, CCL3L1, CCL4, CCL5, CCL11, CCL14, and CCL22, are cleaved by CD26; however, the efficiency is clearly influenced by the amino acids surrounding the cleavage site and although not yet proven, potentially affected by the chemokine concentration and interactions with third molecules. NH2-terminal cleavage of chemokines by CD26 has prominent effects on their receptor binding, signaling, and hence, in vitro and in vivo biologic activities. However, rather than having a similar result, the outcome of NH2-terminal truncation is highly diverse. Either no difference in activity or drastic alterations in receptor recognition/specificity and hence, chemotactic activity are observed. Analogously, chemokine-dependent inhibition of HIV infection is enhanced (for CCL3L1 and CCL5) or decreased (for CXCL12) by CD26 cleavage. The occurrence of CD26-processed chemokine isoforms in plasma underscores the importance of the in vitro-observed CD26 cleavages. Through modulation of chemokine activity, CD26 regulates leukocyte/tumor cell migration and progenitor cell release from the bone marrow, as shown by use of mice treated with CD26 inhibitors or CD26 knockout mice. As chemokine processing by CD26 has a significant impact on physiologic and pathologic processes, application of CD26 inhibitors to affect chemokine function is currently explored, e.g., as add-on therapy in viral infection and cancer.
    No preview · Article · Jan 2016 · Journal of Leukocyte Biology
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    ABSTRACT: Levels of serum amyloid A (SAA), a major acute phase protein in humans, are increased up to 1000-fold upon infection, trauma, cancer or other inflammatory events. However, the exact role of SAA in host defense is yet not fully understood. Several pro- and anti-inflammatory properties have been ascribed to SAA. Here, the regulated production of SAA by cytokines and glucocorticoids is discussed first. Secondly, the cytokine and chemokine inducing capacity of SAA and its receptor usage are reviewed. Thirdly, the direct (via FPR2) and indirect (via TLR2) chemotactic effects of SAA and its synergy with chemokines are unraveled. Altogether, a complex cytokine–SAA–chemokine network is established, in which SAA plays a key role in regulating the inflammatory response.
    No preview · Article · Dec 2015 · Cytokine & growth factor reviews
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    ABSTRACT: Chemokines attract leukocytes to sites of infection in a G protein-coupled receptor (GPCR) and glycosaminoglycan (GAG) dependent manner. Therefore, chemokines are crucial molecules for proper functioning of our antimicrobial defense mechanisms. In addition, some chemokines have GPCR-independent defensin-like antimicrobial activities against bacteria and fungi. Recently, high affinity for GAGs has been reported for the positively charged COOH-terminal region of the chemokine CXCL9. In addition to CXCL9, also CXCL12γ has such a positively charged COOH-terminal region with about 50 % positively charged amino acids. In this report, we compared the affinity of COOH-terminal peptides of CXCL9 and CXCL12γ for GAGs and KD values in the low nM range were detected. Several enveloped viruses such as herpesviruses, hepatitis viruses, human immunodeficiency virus (HIV), dengue virus (DENV), etc. are known to bind to GAGs such as the negatively charged heparan sulfate (HS). In this way GAGs are important for the initial contacts between viruses and host cells and for the infection of the cell. Thus, inhibiting the virus-cell interactions, by blocking GAG-binding sites on the host cell, might be a way to target multiple virus families and resistant strains. This article reports that the COOH-terminal peptides of CXCL9 and CXCL12γ have antiviral activity against DENV serotype 2, clinical and laboratory strains of herpes simplex virus (HSV)-1 and respiratory syncytial virus (RSV). Moreover, we show that CXCL9(74-103) competes with DENV envelope protein domain III for binding to heparin. These short chemokine-derived peptides may be lead molecules for the development of novel antiviral agents.
    Full-text · Article · Nov 2015 · Biochemical pharmacology

  • No preview · Article · Oct 2015
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    ABSTRACT: Cell migration depends on the ability of leukocytes to sense an external gradient of chemotactic proteins produced during inflammation. These proteins include chemokines, complement factors, and some acute phase proteins, such as serum amyloid A. Serum amyloid A chemoattracts neutrophils, monocytes, and T lymphocytes via its G protein-coupled receptor formyl peptide receptor 2. We demonstrate that serum amyloid A1α more potently chemoattracts neutrophils in vivo than in vitro. In contrast to CD14(+) monocytes, no rapid (within 2 h) induction of interleukin-8/CXC chemokine ligand 8 or macrophage-inflammatory protein-1α/CC chemokine ligand 3 was observed in purified human neutrophils after stimulation of the cells with serum amyloid A1α or lipopolysaccharide. Moreover, interleukin-8/CXC chemokine ligand 8 induction in monocytes by serum amyloid A1α was mediated by toll-like receptor 2 and was inhibited by association of serum amyloid A1α with high density lipoprotein. This indicates that the potent chemotactic response of neutrophils toward intraperitoneally injected serum amyloid A1α is indirectly enhanced by rapid induction of chemokines in peritoneal cells, synergizing in a paracrine manner with serum amyloid A1α. We observed direct synergy between IL-8/CXC chemokine ligand 8 and serum amyloid A1α, but not lipopolysaccharide, in chemotaxis and shape change assays with neutrophils. Furthermore, the selective CXC chemokine receptor 2 and formyl peptide receptor 2 antagonists, SB225002 and WRW4, respectively, blocked the synergy between IL-8/CXC chemokine ligand 8 and serum amyloid A1α in neutrophil chemotaxis in vitro, indicating that for synergy their corresponding G protein-coupled receptors are required. Additionally, SB225002 significantly inhibited serum amyloid A1α-mediated peritoneal neutrophil influx. Taken together, endogenous (e.g., IL-1β) and exogenous (e.g., lipopolysaccharide) inflammatory mediators induce primary chemoattractants such as serum amyloid A that synergize in an autocrine (monocyte) or a paracrine (neutrophil) fashion with secondary chemokines induced in stromal cells. © Society for Leukocyte Biology.
    No preview · Article · Aug 2015 · Journal of leukocyte biology
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    ABSTRACT: The ELR-CXC chemokine CXCL9 is characterized by a long, highly positively charged COOH-terminal region, absent in most other chemokines. Several natural leukocyte- and fibroblast-derived COOH-terminally truncated CXCL9 forms missing up to 30 amino acids were identified. To investigate the role of the COOH-terminal region of CXCL9, several COOH-terminal peptides were chemically synthesized. These peptides display high affinity for glycosaminoglycans (GAG) and compete with functional intact chemokines for GAG binding, the longest peptide, i.e. CXCL9(74-103), being the most potent. The COOH-terminal peptide CXCL9(74-103) does not signal through or act as an antagonist for CXCR3, the G protein coupled CXCL9 receptor, and does not influence neutrophil chemotactic activity of CXCL8 in vitro. Based on the GAG binding data, an anti inflammatory role for CXCL9(74-103) was further evidenced in vivo. Simultaneous intravenous injection of CXCL9(74-103) with CXCL8 injection in the joint diminished CXCL8-induced neutrophil extravasation. Analogously, monosodium urate crystal-induced neutrophil migration to the tibiofemural articulation, a murine model of gout, is highly reduced by i.v. injection of CXCL9(74-103). These data show that chemokine-derived peptides with high affinity for GAGs may be used as anti-inflammatory peptides: by competing with active chemokines for binding and immobilization on GAGs, these peptides may lower chemokine presentation on the endothelium and disrupt the generation of a chemokine gradient, thereby preventing a chemokine from properly performing its chemotactic function. The CXCL9 peptide may serve as a lead molecule for further development of inhibitors of inflammation based on interference with chemokine-GAG-interactions. Copyright © 2015, The American Society for Biochemistry and Molecular Biology.
    Full-text · Article · Jul 2015 · Journal of Biological Chemistry
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    ABSTRACT: Purpose:To investigate the expression of platelet factor-4 variant (PF-4var) in epiretinal membranes from patients with proliferative diabetic retinopathy (PDR) and the role of PF-4var in the regulation of blood-retinal barrier (BRB) breakdown in diabetic rat retinas and human retinal microvascular endothelial cells (HRMEC). Methods:Rats were treated intravitreally with PF-4var or the anti-vascular endothelial growth factor (VEGF) agent bevacizumab on the first day after diabetes induction. BRB breakdown was assessed in vivo with fluorescein isothiocyanate (FITC)-conjugated dextran and in vitro in HRMEC by transendothelial electrical resistance and FITC-conjugated dextran cell permeability assay. Occludin, vascular endothelial (VE)-cadherin, hypoxia-inducible factor (HIF)-1α, VEGF, tumor necrosis factor (TNF)-α, receptor for advanced glycation end products (RAGE), caspase-3 levels and generation of reactive oxygen species (ROS) were assessed by Western blot, enzyme-linked immunosorbent assays or spectrophotometry. Results:In epiretinal membranes, vascular endothelial cells and stromal cells expressed PF-4var. In vitro, HRMEC produced PF-4var after stimulation with a combination of interleukin (IL)-1β and TNF-α and PF-4var inhibited VEGF-mediated hyperpermeability in HRMEC. In rats PF-4var was as potent as bevacizumab in attenuating diabetes-induced BRB breakdown. This effect was associated with upregulation of occludin and VE-cadherin and downregulation of HIF-1α, VEGF, TNF-α, RAGE and caspase-3, whereas ROS generation was not altered. Conclusions:Our findings suggest that increasing intraocular PF-4var levels early after the onset of diabetes protects against diabetes-induced BRB breakdown. Copyright © 2015 by Association for Research in Vision and Ophthalmology.
    No preview · Article · Feb 2015 · Investigative ophthalmology & visual science
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    ABSTRACT: Myofibroblasts expressing α-smooth muscle actin (α-SMA) are the key cellular mediator of fibrosis. Fibrovascular epiretinal membranes from patients with proliferative diabetic retinopathy (PDR) are characterized by the accumulation of a large number of myofibroblasts. We explored the hypothesis that proliferating endothelial cells via endothelial-to-mesenchymal transition (EndoMT) and/or bone marrow-derived circulating fibrocytes contribute to the myofibroblast population present in PDR epiretinal membranes. Epiretinal membranes from 14 patients with PDR were studied by immunohistochemistry. All membranes contained neovessels expressing the endothelial cell marker CD31. CD31+ endothelial cells co-expressed the fibroblast/myofibroblast markers fibroblast-specific protein-1 (FSP-1) and α-SMA, indicative for the occurrence of endoMT. In the stroma, cells expressing FSP-1, α-SMA, the leukocyte common antigen CD45, and the myelomonocytic marker CD11b were detected. Double labeling showed co-localization of CD45 with FSP-1 and α-SMA and co-localization of CD11b with α-SMA and matrix metalloproteinase-9, demonstrating the presence of infiltrating fibrocytes. In addition, we investigated the phenotypic changes that take place in human retinal microvascular endothelial cells following exposure to transforming growth factor-β1 (TGF-β1), connective tissue growth factor (CTGF) and the proinflammatory cytokines interleukin-1β (IL-1β) and tumor necrosis factor-α (TNF-α). Retinal microvascular endothelial cells changed morphology upon cytokine exposure, lost the expression of endothelial cell markers (endothelial nitric oxide synthase and vascular endothelial-cadherin) and started to express mesenchymal markers (calponin, snail, transgelin and FSP-1). These results suggest that endothelial cells as well as circulating fibrocytes may differentiate into myofibroblasts in the diabetic eye and contribute to pathologic fibrosis in PDR.
    No preview · Article · Jan 2015 · Experimental Eye Research
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    ABSTRACT: Serum amyloid A (SAA) is an acute phase protein which is up-regulated in inflammatory diseases and chemoattracts monocytes, lymphocytes and granulocytes via its G protein-coupled receptor FPRL1/FPR2. Here, we demonstrated that the SAA1α isoform also chemoattracts monocyte-derived immature dendritic cells (DCs) in the Boyden and μ-slide chemotaxis assay and that its chemotactic activity for monocytes and DCs was indirectly mediated via rapid chemokine induction. Indeed, SAA1 induced significant amounts (≥5 ng/ml) of MIP-1α/CCL3 and IL-8/CXCL8 in monocytes and DCs in a dose-dependent manner within 3 h. However, SAA1 also directly activated monocytes and DCs for signaling and chemotaxis without chemokine interference. SAA1-induced monocyte migration was nevertheless significantly prevented (60 to 80% inhibition) in the constant presence of desensitizing exogenous MIP-1α/CCL3, neutralizing anti-MIP-1α/CCL3 antibody or a combination of CCR1 and CCR5 antagonists, indicating that this endogenously produced CC chemokine was indirectly contributing to SAA1-mediated chemotaxis. Further, anti-IL-8/CXCL8 antibody neutralized SAA1-induced monocyte migration, suggesting that endogenous IL-8/CXCL8 acted in concert with MIP-1α/CCL3. This explained why SAA1 failed to synergize with exogenously added MIP-1α/CCL3 or SDF-1α/CXCL12 in monocyte and DC chemotaxis. In addition to direct leukocyte activation, SAA1 induces a chemotactic cascade mediated by expression of cooperating chemokines to prolong leukocyte recruitment to the inflammatory site.This article is protected by copyright. All rights reserved
    No preview · Article · Jan 2015 · European Journal of Immunology
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    ABSTRACT: Chemokines, binding their various G protein-coupled receptors, lead the way for leukocytes in health and inflammation. Yet chemokine receptor expression is not limited to leukocytes. Accordingly, chemokines are remarkably pleiotropic molecules involved in a range of physiological as well as pathological processes. For example, the CXCR3 chemokine receptor is expressed on activated T lymphocytes, dendritic cells and natural killer cells, but also fibroblasts and smooth muscle, epithelial and endothelial cells. In men, these cells express either CXCR3A, its splice variant CXCR3B or a balanced combination of both. The CXCR3 ligands, activating both receptor variants, include CXCL4, CXCL4L1, CXCL9, CXCL10 and CXCL11. Upon CXCR3A activation these ELR-negative CXC chemokines mediate chemotactic and proliferative responses, for example in leukocytes. In contrast, CXCR3B induces anti-proliferative and anti-migratory effects, as exemplified by angiostatic effects on endothelial cells. Taken together, the unusual and versatile characteristics of CXCR3 and its ligands form the basis for their pertinent involvement in a myriad of diseases. In this review, we discuss the presence and function of all CXCR3 ligands in various malignant, angiogenic, infectious, inflammatory and other disorders. By extension, we have also elaborated on the potential therapeutic applicability of CXCR3 ligand administration or blockade, as well as their additional value as predictive or prognostic biomarkers. This review illustrates the multifunctional, intriguing character of the various CXCR3-binding chemokines. Copyright © 2014. Published by Elsevier Ltd.
    No preview · Article · Nov 2014 · Cytokine & Growth Factor Reviews
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    ABSTRACT: The blood-brain barrier (BBB) is a specific structure that is composed of two basement membranes (BMs) and that contributes to the control of neuroinflammation. As long as the BBB is intact, extravasated leukocytes may accumulate between two BMs, generating vascular cuffs. Specific matrix metalloproteinases, MMP-2 and MMP-9, have been shown to cleave BBB beta-dystroglycan and to disintegrate thereby the parenchymal BM, resulting in encephalomyelitis. This knowledge has been added to the molecular basis of the REGA model to understand the pathogenesis of multiple sclerosis, and it gives further ground for the use of MMP inhibitors for the treatment of acute neuroinflammation. MMP-9 is associated with central nervous system inflammation and occurs in various forms: monomers and multimers. None of the various neurological and neuropathologic functions of MMP-9 have been associated with either molecular structure or molecular form, and therefore, in-depth structure-function studies are needed before medical intervention with MMP-9-specific inhibitors is initiated.
    No preview · Article · Nov 2014 · Progress in brain research
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    Preview · Article · Nov 2014 · Oncotarget
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    ABSTRACT: Gelatinase B/ matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) cleaves many substrates and is produced by most cell types as a zymogen, proMMP-9, in complex with the tissue inhibitor of metalloproteinases-1 (TIMP-1). Natural proMMP-9 occurs as monomers, homomultimers, and heterocomplexes, but our knowledge about the overall structure of proMMP-9 monomers and multimers is limited. We investigated biochemical, biophysical, and functional characteristics of zymogen and activated forms of MMP-9 monomers and multimers. In contrast to a conventional notion of a dimeric nature of MMP-9 homomultimers, we demonstrate that these are reduction-sensitive trimers. Based on the information from electrophoresis, atomic force microscopy (AFM) and transmission electron microscopy (TEM), we generated a 3D structure model of the proMMP-9 trimer. Remarkably, the proMMP-9 trimers possessed a 50-fold higher affinity for TIMP-1 than the monomers. In vivo, this finding was reflected in a higher extent of TIMP-1 inhibition of angiogenesis induced by trimers versus monomers. Our results show that proMMP-9 trimers constitute a novel structural and functional entity that is differentially regulated by TIMP-1.
    Full-text · Article · Oct 2014 · Biochemical Journal
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    ABSTRACT: CXCL4 and CXCL4L1, platelet-derived CXC chemokines, and their carboxy-terminal peptides CXCL447-70 and CXCL4L147-70 previously displayed angiostatic and anti-tumoral activity in a melanoma model. Here, we found CXCL447-70 and CXCL4L147-70 to inhibit lymphatic endothelial cell proliferation in vitro. Furthermore, the angiostatic potential of CXCL447-70 and CXCL4L147-70 was tested against different angiogenic stimuli (FGF1, FGF2, FGF8, EGF and VEGF). Besides reducing FGF2-induced vascular endothelial cell growth, CXCL447-70 and CXCL4L147-70 efficiently counteracted EGF. Consequently, we considered their anti-tumoral potential in EGF-dependent MDA-MB-231 breast tumors. In tumor-bearing mice, CXCL447-70 reduced tumor growth better than CXCL4L147-70. In CXCL447-70-treated tumors significantly more intratumoral monocytes/macrophages and dendritic cells were present and higher expression levels of CCL5 and IFN- γ were detected by qPCR on tumor lysates. Because neither peptide was able to specifically bind CXCR3A or CXCR3B, differential glycosaminoglycan binding and direct interaction with cytokines (EGF and CCL5) might explain any differences in anti-tumoral effects. Notably, CCL5-induced monocyte chemotaxis in vitro was increased by addition of CXCL447-70 or CXCL4L147-70. Finally, CXCL447-70 and CXCL4L147-70 inhibited proliferation of MDA-MB-231 cells. Our results suggest a tumor type-dependent responsiveness to either CXCL447-70 or CXCL4L147-70 treatment, defined by anti-proliferative, angiostatic and inflammatory actions, and substantiate their therapeutic potential.
    Full-text · Article · Oct 2014 · Oncotarget
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    ABSTRACT: In vivo leukocyte recruitment is not fully understood and may result from interactions of chemokines with glycosaminoglycans/GAGs. We previously showed that chlorite-oxidized oxyamylose/COAM binds the neutrophil chemokine GCP-2/CXCL6. Here, mouse chemokine binding by COAM was studied systematically and binding affinities of chemokines to COAM versus GAGs were compared. COAM and heparan sulphate bound the mouse CXC chemokines KC/CXCL1, MIP-2/CXCL2, IP-10/CXCL10 and I-TAC/CXCL11 and the CC chemokine RANTES/CCL5 with affinities in the nanomolar range, whereas no binding interactions were observed for mouse MCP-1/CCL2, MIP-1α/CCL3 and MIP-1β/CCL4. The affinities of COAM-interacting chemokines were similar to or higher than those observed for heparan sulphate. Although COAM did not display chemotactic activity by itself, its co-administration with mouse GCP-2/CXCL6 and MIP-2/CXCL2 or its binding of endogenous chemokines resulted in fast and cooperative peritoneal neutrophil recruitment and in extravasation into the cremaster muscle in vivo. These local GAG mimetic features by COAM within tissues superseded systemic effects and were sufficient and applicable to reduce LPS-induced liver-specific neutrophil recruitment and activation. COAM mimics glycosaminoglycans and is a nontoxic probe for the study of leukocyte recruitment and inflammation in vivo.
    Full-text · Article · Aug 2014 · PLoS ONE
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    Full-text · Article · Jul 2014

  • No preview · Article · Jun 2014
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    ABSTRACT: Outgrowth of Porphyromonas gingivalis within the inflammatory subgingival plaque is associated with periodontitis characterized by periodontal tissue destruction, loss of alveolar bone, periodontal pocket formation and eventually tooth loss. Potential virulence factors of P. gingivalis are peptidylarginine deiminase (PPAD), an enzyme modifying free or peptide-bound arginine to citrulline, and the bacterial proteases referred to as gingipains (Rgp and Kgp). Chemokines attract leukocytes during inflammation. However, posttranslational modification (PTM) of chemokines by proteases or human peptidylarginine deiminases may alter their biological activities. Since chemokine processing may be important in microbial defense mechanisms, we investigated whether PTM of chemokines occurs by P. gingivalis enzymes. Upon incubation of interleukin-8 (IL-8/CXCL8) with PPAD, only minor enzymatic citrullination was detected. In contrast, Rgp rapidly cleaved CXCL8 in vitro. Subsequently, different P. gingivalis strains were incubated with the chemokines CXCL8 or CXCL10 and their PTM were investigated. No significant CXCL8 citrullination was detected for the tested strains. Interestingly, although considerable differences in efficiency of CXCL8 degradation were observed with full cultures of various strains, similar rates of chemokine proteolysis were exerted by cell-free culture supernatants. Sequencing of CXCL8 incubated with supernatant or bacteria showed that CXCL8 is processed into its more potent 6-77 and 9-77 forms. In contrast, CXCL10 was entirely and rapidly degraded by P. gingivalis with no transient chemokine forms being observed. In conclusion, this study demonstrates PTM of CXCL8 and CXCL10 by gingipains of P. gingivalis and that strain differences may particularly affect the activity of these bacterial membrane-associated proteases.
    Full-text · Article · Mar 2014 · Infection and immunity
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    ABSTRACT: CXC chemokines influence a variety of biological processes, such as angiogenesis, both in a physiological and pathological context. Platelet factor-4 (PF-4)/CXCL4 and its variant PF-4var/CXCL4L1 are known to favor angiostasis by inhibiting endothelial cell proliferation and chemotaxis. CXCL4L1 in particular is a potent inhibitor of angiogenesis with anti-tumoral characteristics, both through regulation of neovascularization and through attraction of activated lymphocytes. However, its underlying signaling pathways remain to be elucidated. Here, we have identified various intracellular pathways activated by CXCL4L1 in comparison with other CXCR3 ligands, including CXCL4 and interferon-γ-induced protein 10/CXCL10. Signaling experiments show involvement of the mitogen-activated protein kinase (MAPK) family in CXCR3A-transfected cells, activated lymphocytes and human microvascular endothelial cells (HMVEC). In CXCR3A transfectants, CXCL4 and CXCL4L1 activated p38 MAPK, as well as Src kinase within 30 and 5 min, respectively. Extracellular signal-regulated kinase (ERK) phosphorylation occured in activated lymphocytes, yet was inhibited in microvascular and lymphatic endothelial cells. CXCL4L1 and CXCL4 counterbalanced the angiogenic chemokine stromal cell-derived factor-1/CXCL12 in both endothelial cell types. Notably, inhibition of ERK signaling by CXCL4L1 and CXCL4 in lymphatic endothelial cells implies that these chemokines might also regulate lymphangiogenesis. Furthermore, CXCL4, CXCL4L1 and CXCL10 slightly enhanced forskolin-stimulated cAMP production in HMVEC. Finally, CXCL4, but not CXCL4L1, induced activation of p70S6 kinase within 5 min in HMVEC. Our findings confirm that the angiostatic chemokines CXCL4L1 and CXCL4 activate both CXCR3A and CXCR3B and bring new insights into the complexity of their signaling cascades.
    Full-text · Article · Jan 2014 · Angiogenesis
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    Full-text · Dataset · Jan 2014

Publication Stats

30k Citations
2,222.48 Total Impact Points

Institutions

  • 1977-2015
    • University of Leuven
      • • Department of Microbiology and Immunology
      • • Centre of Microbial and Plant Genetics (CMPG)
      • • Division of Forensic Biomedical Sciences
      • • Rega Institute for Medical Research
      Louvain, Flemish, Belgium
  • 2014
    • Jagiellonian University
      Cracovia, Lesser Poland Voivodeship, Poland
  • 2013-2014
    • Universitair Psychiatrisch Centrum KU Leuven
      Cortenberg, Flanders, Belgium
  • 2011
    • University of Lausanne
      • Department of Biochemistry
      Lausanne, Vaud, Switzerland
  • 1978-2008
    • Ghent University
      • • VIB Department of Medical Protein Research
      • • Department of Food Safety and Food Quality
      • • Department of Biochemistry (Medicine)
      • • Laboratory of Microbiology
      Gand, Flanders, Belgium
  • 2005
    • Vanderbilt University
      Nashville, Michigan, United States
  • 2003-2005
    • The Institute for Molecular Medicine
      Huntington Beach, California, United States
  • 2002
    • Université Libre de Bruxelles
      Bruxelles, Brussels Capital, Belgium
  • 1987-2002
    • Mario Negri Institute for Pharmacological Research
      • Department of Oncology
      Milano, Lombardy, Italy
    • Maastricht University
      • Algemene Heelkunde
      Maastricht, Provincie Limburg, Netherlands
  • 1989-2000
    • University of Antwerp
      • • Department of Pharmaceutical sciences
      • • Faculty of Medicine
      Antwerpen, Flanders, Belgium
    • Sapienza University of Rome
      Roma, Latium, Italy
  • 1999
    • Hospital Universitari Germans Trias i Pujol
      • Department of Clinical Pharmacology
      Badalona, Catalonia, Spain
  • 1996-1998
    • Beijing Medical University
      • Department of Immunology
      Peping, Beijing, China
    • Instytut Chemicznej Przeróbki Węgla
      Hindenburg, Silesian Voivodeship, Poland
  • 1997
    • University of Nottingham
      • School of Medicine
      Nottigham, England, United Kingdom
    • King Abdulaziz University
      • Department of Ophthalmology
      Djidda, Makkah, Saudi Arabia
  • 1987-1996
    • Leiden University Medical Centre
      • Department of Hematology
      Leyden, South Holland, Netherlands
  • 1995
    • National Cancer Institute (USA)
      • Laboratory of Molecular Immunoregulation
      베서스다, Maryland, United States
  • 1994
    • University of Texas Medical Branch at Galveston
      • Department of Internal Medicine
      Galveston, TX, United States
    • Saint Petersburg Medical Academy
      Sankt-Peterburg, St.-Petersburg, Russia
    • Christian-Albrechts-Universität zu Kiel
      • Department of Dermatology, Venereology and Allergology
      Kiel, Schleswig-Holstein, Germany
  • 1993
    • Utrecht University
      Utrecht, Utrecht, Netherlands
  • 1992
    • Texas A&M University
      • Department of Entomology
      College Station, Texas, United States
    • National Veterinary Laboratory
      فرانکلین لیکس، نیوجرسی, New Jersey, United States
  • 1990-1992
    • Universitair Ziekenhuis Leuven
      • Department of General internal medicine
      Louvain, Flanders, Belgium
    • University of Liège
      • Department of Neurology
      Liège, WAL, Belgium
  • 1988-1991
    • Catholic University of Louvain
      Лувен-ла-Нев, Walloon, Belgium
    • Austrian Academy of Sciences
      • Institut für Molekulare Biotechnologie (IMBA)
      Vienna, Vienna, Austria
    • Ludwig Institute for Cancer Research Ltd Belgium
      Bruxelles, Brussels Capital, Belgium