0000000000548388

AUTHOR

Pierre Van Der Bruggen

showing 4 related works from this author

Consensus nomenclature for CD8(+) T cell phenotypes in cancer

2015

International audience; Whereas preclinical investigations and clinical studies have established that CD8+ T cells can profoundly affect cancer progression, the underlying mechanisms are still elusive. Challenging the prevalent view that the beneficial effect of CD8+ T cells in cancer is solely attributable to their cytotoxic activity, several reports have indicated that the ability of CD8+ T cells to promote tumor regression is dependent on their cytokine secretion profile and their ability to self-renew. Evidence has also shown that the tumor microenvironment can disarm CD8+ T cell immunity, leading to the emergence of dysfunctional CD8+ T cells. The existence of different types of CD8+ T…

senescenceT cellOncology and CarcinogenesisImmunology[SDV.CAN]Life Sciences [q-bio]/CancerBiologyCD8+ T cellsIFN gammaanergy03 medical and health sciencesstemness0302 clinical medicineImmune system[SDV.CAN] Life Sciences [q-bio]/Cancerexhaustionmedicine2.1 Biological and endogenous factorsImmunology and AllergyCytotoxic T cellAetiologyPoint of ViewCancer030304 developmental biologyCD8+ T cells; IFNγ; anergy; anticancer immunity; cytotoxicity; effector; exhaustion; senescence; stemness0303 health sciencesTumor microenvironmentCD8(+) T cellsCancermedicine.diseasePhenotype3. Good healthanticancer immunitymedicine.anatomical_structureeffectorOncologyImmunologycytotoxicityCytokine secretionCD8030215 immunologyIFNγ
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Monitoring of anti-vaccine CD4 T cell frequencies in melanoma patients vaccinated with a MAGE-3 protein.

2005

Abstract Quantitative evaluation of T cell responses of patients receiving antitumoral vaccination with a protein is difficult because of the large number of possible HLA-peptide combinations that could be targeted by the response. To evaluate the responses of patients vaccinated with protein MAGE-3, we have developed an approach that involves overnight stimulation of blood T cells with autologous dendritic cells loaded with the protein, sorting by flow cytometry of the T cells that produce IFN-γ, cloning of these cells, and evaluation of the number of T cell clones that secrete IFN-γ upon stimulation with the Ag. An important criterion is that T cell clones must recognize not only stimulat…

CD4-Positive T-Lymphocytesmedicine.medical_treatmentT cellImmunologyAntigen presentationMolecular Sequence DataCD4 T cellsCell SeparationBiologyLymphocyte ActivationCancer VaccinesFlow cytometryInterleukin 21Interferon-gammaAntigenSDG 3 - Good Health and Well-beingAntigens NeoplasmMonitoring ImmunologicmedicineTumor Cells CulturedImmunology and AllergyHumansAmino Acid SequenceLymphocyte CountMelanomaCell Line TransformedAntigen Presentationmedicine.diagnostic_testT-cell receptorCoculture TechniquesGrowth InhibitorsClone CellsNeoplasm Proteinsmedicine.anatomical_structureCell cultureImmunologyAdjuvantVaccineMAGE-3 proteinJournal of immunology (Baltimore, Md. : 1950)
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A tyrosinase peptide presented by HLA-B35 is recognized on a human melanoma by autologous cytotoxic T lymphocytes

1999

We previously described different cytotoxic T lymphocyte (CTL) clones isolated from the blood lymphocytes of a melanoma patient after in vitro stimulation with autologous tumor cells. These CTL clones recognized at least 2 distinct antigens on the melanoma cells. Here, we show that one of them consists of a peptide derived from tyrosinase and presented by HLA-B35. The peptide is 9 amino acids long and has the sequence LPSSADVEF. It can be presented by the 2 major B35 allelic subtypes, B*3501 and B*3503. As HLA-B35 is one of the most frequent HLA-B specificities, being present in about 20% of Caucasian individuals, it may be a useful target for peptide-based immunotherapy of melanoma.

Cytotoxicity ImmunologicHerpesvirus 4 HumanCancer Researchmedicine.medical_treatmentAntigen presentationTyrosinase PeptideBiologyTransfectionAntigenTumor Cells CulturedmedicineAnimalsHumansCytotoxic T cellAmino Acid SequenceMelanomaPeptide sequenceAllelesCell Line TransformedB-LymphocytesMonophenol MonooxygenaseMelanomaImmunotherapymedicine.diseasePeptide FragmentsRecombinant ProteinsCTL*OncologyCOS CellsImmunologyCancer researchHLA-B35 AntigenT-Lymphocytes CytotoxicInternational Journal of Cancer
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Propeptide glycosylation and galectin‐3 binding decrease proteolytic activation of human proMMP‐9/progelatinase B

2019

Matrix metalloproteinases (MMPs) are secreted as proenzymes, containing propeptides that interact with the catalytic zinc, thereby controlling MMP activation. The MMP‐9 propeptide is unique in the MMP family because of its post‐translational modification with an N‐linked oligosaccharide. ProMMP‐9 activation by MMP‐3 occurs stepwise by cleavage of the propeptide in an aminoterminal (pro‐AT) and carboxyterminal (pro‐CT) peptide. We chemically synthesized aglycosyl pro‐AT and pro‐CT and purified recombinant glycosylated pro‐ATS f−9. First, we report new cleavage sites in the MMP‐9 propeptide by MMP‐3 and neutrophil elastase. Additionally, we demonstrated with the use of western blot analysis a…

0301 basic medicinePNGase FN-linked glycosylationGlycosylationGlycosylationmatrix metalloproteinase‐9Galectin 3GalectinsProteolysisgalectin‐3Biochemistry03 medical and health scienceschemistry.chemical_compoundCongenital Disorders of Glycosylation0302 clinical medicineN-linked glycosylationmatrix metalloproteinase-9galectin-3medicineHumansZymographyAmino Acid SequenceProtein precursorMolecular BiologyN‐linked glycosylationEnzyme Precursorspropeptidemedicine.diagnostic_testbiologyBlood ProteinsOriginal ArticlesCell BiologyTrypsinEnzyme Activation030104 developmental biologyMatrix Metalloproteinase 9chemistryBiochemistryGelatinasesCase-Control Studiesproteolytic activation030220 oncology & carcinogenesisNeutrophil elastaseProteolysisbiology.proteinMatrix Metalloproteinase 3Original ArticleLeukocyte Elastasemedicine.drug
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