Philippe Delannoy

ORCID: 0000-0001-6467-7553
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About
Contact & Profiles
Research Areas
  • Glycosylation and Glycoproteins Research
  • Carbohydrate Chemistry and Synthesis
  • Galectins and Cancer Biology
  • Monoclonal and Polyclonal Antibodies Research
  • Proteoglycans and glycosaminoglycans research
  • Cancer Research and Treatments
  • Peptidase Inhibition and Analysis
  • Caveolin-1 and cellular processes
  • Cancer, Hypoxia, and Metabolism
  • Cell Adhesion Molecules Research
  • Neuroblastoma Research and Treatments
  • Infant Nutrition and Health
  • ATP Synthase and ATPases Research
  • Genomics and Phylogenetic Studies
  • Craniofacial Disorders and Treatments
  • Enzyme Production and Characterization
  • RNA and protein synthesis mechanisms
  • Bone and Dental Protein Studies
  • Immunotherapy and Immune Responses
  • RNA Interference and Gene Delivery
  • Connective tissue disorders research
  • Ubiquitin and proteasome pathways
  • RNA modifications and cancer
  • Wnt/β-catenin signaling in development and cancer
  • Immune Response and Inflammation

Centre National de la Recherche Scientifique
2013-2024

Unité de Glycobiologie Structurale et Fonctionnelle
2014-2024

Université de Lille
2012-2024

Institut pour la Recherche sur le Cancer de Lille
2020

Université Lille Nord de France
2003-2017

Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement
2015

Laboratoire d'Informatique Fondamentale de Lille
2015

University of the Sciences
2008-2012

Milbank Memorial Fund
2012

Institut polytechnique de Grenoble
2010

The animal sialyltransferases are Golgi type II transmembrane glycosyltransferases. Twenty distinct have been identified in both human and murine genomes. These enzymes catalyze transfer of sialic acid from CMP-Neu5Ac to the glycan moiety glycoconjugates. Despite low overall identities, they share four conserved peptide motifs [L (large), S (small), motif III, VS (very small)] that hallmarks for sialyltransferase identification. We 155 new putative genes 25 species, we exploited two lines...

10.1093/glycob/cwi063 article EN Glycobiology 2005-04-20

To determine the role of physicochemical characteristics surface dense ceramics on osteoconduction, we studied proliferation and differentiation human trabecular (HT) osteoblastic cells, extracellular collagenous matrix production, biologic apatite formation stoichiometric hydroxyapatite (HA) type A carbonate (CA). The (composition, roughness) HA CA carefully were determined by Fourier-transformed infrared, X-ray photoelectron, Raman spectroscopies, FTIR microscopy, before after cell...

10.1002/(sici)1097-4636(20000605)50:3<353::aid-jbm9>3.0.co;2-c article EN Journal of Biomedical Materials Research 2000-06-05

Sialyl-Tn is a carbohydrate antigen overexpressed in several epithelial cancers, including breast cancer, and usually associated with poor prognosis. synthesized by CMP-Neu5Ac:GalNAcα2,6-sialyltransferase: CMP-Neu5Ac: R-GalNAcα1-O-Ser/Thr α2,6-sialyltransferase (EC 2.4.99.3) (ST6GalNAc I), which transfers sialic acid residue α2,6-linkage to the GalNAcα1-O-Ser/Thr structure. However, established cancer cell lines express neither ST6GalNAc I nor sialyl-Tn. We have previously shown that stable...

10.1093/glycob/cwj033 article EN Glycobiology 2005-08-31

Quantum dots (QD) are inorganic nanocrystals with outstanding optical properties, specially suited for biological imaging applications. Their attachment to biomolecules in mild aqueous conditions the design of bioconjugates is therefore highly desirable. 1,3-dipolar [3 + 2] cycloaddition between azides and terminal alkynes ("click chemistry") could represent an attractive QD functionalization method. Unfortunately, use popular Cu(I)-catalyzed version this reaction not applicable achieving...

10.1021/bc900564w article EN Bioconjugate Chemistry 2010-03-11

Sialyl-Tn antigen (STn) is a short O-glycan containing sialic acid residue a2,6-linked to GalNAca-O-Ser/Thr. The biosynthesis of STn mediated by specific sialyltransferase termed ST6GalNAc I, which competes with O-glycans elongating glycosyltransferases and prevents cancer cells from exhibiting longer O-glycans. While weakly expressed fetal normal adult tissues, more than 80% human carcinomas in all cases, detection associated adverse outcome decreased overall survival for the patients....

10.3390/biom2040435 article EN cc-by Biomolecules 2012-10-11

Abstract Background The rat hybridoma cell line YB2/0 appears a good candidate for the large-scale production of low fucose recombinant mAbs due to its lower expression fut8 gene than other commonly used rodent lines. However, important variations content are observed in culture conditions. To improve our knowledge on fucosylation capacity, we have cloned and characterized gene. Results cDNAs encoding α1,6-fucosyltransferase (FucT VIII) were from cells by polymerase chain reaction-based 5'...

10.1186/1472-6750-11-1 article EN cc-by BMC Biotechnology 2011-01-05

Gangliosides, the glycosphingolipids carrying one or several sialic acid residues, are located on outer leaflet of plasma membrane in glycolipid-enriched microdomains, where they interact with molecules signal transduction pathways including receptors tyrosine kinases (RTKs). The role gangliosides regulation has been reported many cases and a large number cell types. In this review, we summarize current knowledge biosynthesis mechanism by which regulate RTKs signaling.

10.3390/cells2040751 article EN cc-by Cells 2013-12-06

We have recently established and characterized cellular clones deriving from MDA-MB-231 breast cancer cells that express the human GD3 synthase (GD3S), enzyme controls biosynthesis of b- c-series gangliosides. The GD3S positive show a proliferative phenotype in absence serum or growth factors an increased tumor severe immunodeficient mice. This results constitutive activation receptor tyrosine kinase c-Met spite ligand subsequent mitogen-activated protein kinase/extracellular...

10.1093/glycob/cws049 article EN Glycobiology 2012-02-01

All eukaryotic sialyltransferases have in common the presence their catalytic domain of several conserved peptide regions (sialylmotifs L, S, and VS). Functional analysis sialylmotifs L S previously demonstrated involvement binding donor acceptor substrates. The region comprised between VS contains a stretch four highly residues, with following consensus sequence (H/y)Y(Y/F/W/h)(E/D/q/g). (Capital letters lowercase indicate strong or low occurrence amino acid, respectively.) functional...

10.1074/jbc.m311764200 article EN cc-by Journal of Biological Chemistry 2004-03-26

Bronchial mucins from patients suffering CF (cystic fibrosis) exhibit glycosylation alterations, especially increased amounts of the sialyl-Lewis(x) (NeuAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc-R) and 6-sulfo-sialyl-Lewis(x) (NeuAcalpha2-3Galbeta1-4[Fucalpha1-3][SO(3)H-6]GlcNAc-R) terminal structures. These epitopes are preferential receptors for Pseudomonas aeruginosa, bacteria responsible chronicity airway infection involved in morbidity early death patients. However, these changes cannot...

10.1042/bj20070958 article EN Biochemical Journal 2008-01-29
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