About: Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures

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About: Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures
Creator	Kuja-Panula, Juha Nykänen, Niko-Petteri Rauvala, Heikki Rouhiainen, Ari Vanttola, Päivi Huttunen, Henri
Source	PMC
abstract	Background: Heparin and heparin-related sulphated carbohydrates inhibit ligand binding of the receptor for advanced glycation end products (RAGE). Here, we have studied the ability of heparin to inhibit homophilic interactions of RAGE in living cells and studied how heparin related structures interfere with RAGE–ligand interactions. Methods: Homophilic interactions of RAGE were studied with bead aggregation and living cell protein-fragment complementation assays. Ligand binding was analyzed with microwell binding and chromatographic assays. Cell surface advanced glycation end product binding to RAGE was studied using PC3 cell adhesion assay. Results: Homophilic binding of RAGE was mediated by V(1)- and modulated by C(2)-domain in bead aggregation assay. Dimerisation of RAGE on the living cell surface was inhibited by heparin. Sulphated K5 carbohydrate fragments inhibited RAGE binding to amyloid β-peptide and HMGB1. The inhibition was dependent on the level of sulfation and the length of the carbohydrate backbone. α-d-Glucopyranosiduronic acid (glycyrrhizin) inhibited RAGE binding to advanced glycation end products in PC3 cell adhesion and protein binding assays. Further, glycyrrhizin inhibited HMGB1 and HMGB1 A-box binding to heparin. Conclusions: Our results show that K5 polysaccharides and glycyrrhizin are promising candidates for RAGE targeting drug development.
has issue date	2018-07-30(xsd:dateTime)
bibo:doi	10.3390/medicines5030079
bibo:pmid	30061484
has license	cc-by
sha1sum (hex)	16874a8b95e04383b0ee7049220a36354ffab2ea
schema:url	https://doi.org/10.3390/medicines5030079
resource representing a document's title	Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures
has PubMed Central identifier	PMC6165534
has PubMed identifier	30061484
schema:publication	Medicines (Basel)
resource representing a document's body	covid:16874a8b95e04383b0ee7049220a36354ffab2ea#body_text
is schema:about of	named entity 'INTERFERE' named entity 'USING' named entity 'RELATED' named entity 'BACKGROUND' named entity 'DEPENDENT' named entity 'CELL ADHESION' named entity 'RAGE' named entity 'LIVING CELL' named entity 'HOW' named entity 'INHIBITION' named entity 'MODULATED' named entity 'HMGB1' named entity 'POLYSACCHARIDES' named entity 'CARBOHYDRATES' named entity 'CELLS' named entity 'ANALYZED' named entity 'ADVANCED GLYCATION END PRODUCTS' named entity 'FRAGMENTS' named entity 'MEDIATED' named entity 'PROTEIN' named entity 'AMYLOID' named entity 'HEPARIN' named entity 'ABILITY' named entity 'TARGETING' named entity 'RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS' named entity 'CELL SURFACE' named entity 'DOMAIN' named entity 'HOMOPHILIC' named entity 'receptor' named entity 'Results' named entity 'bead' named entity 'glycation' named entity 'domain' named entity 'INHIBITION' named entity 'CARBOHYDRATE' named entity 'LIVING' named entity 'ADVANCED GLYCATION END PRODUCT' named entity 'SULFATION' named entity 'FRAGMENT' named entity 'C 2' named entity 'LENGTH' named entity 'HAVE' named entity 'OUR' named entity 'ACID' named entity 'LIGAND BINDING' named entity 'BINDING ASSAYS' named entity 'BEAD AGGREGATION' named entity 'RECEPTOR FOR ADVANCED GLYCATION END PRODUCTS' named entity 'MEDICINES' named entity 'RELATED' covid:arg/16874a8b95e04383b0ee7049220a36354ffab2ea named entity 'HEPARIN' named entity 'STRUCTURES' named entity 'INTERACTIONS' named entity 'BINDING' named entity 'PROTEIN BINDING' named entity 'INHIBITED' named entity 'DRUG DEVELOPMENT' named entity 'HERE' named entity 'GLYCYRRHIZIN' named entity 'METHODS' named entity 'COMPLEMENTATION' named entity 'HOMOPHILIC' named entity 'PC3 CELL' named entity 'LIGAND BINDING' named entity 'PEPTIDE' named entity 'MICROWELL' named entity 'STRUCTURES' named entity 'TO INHIBIT' named entity 'CELL ADHESION ASSAY' named entity 'LIGAND' named entity 'A-BOX' named entity 'LEVEL' named entity 'RESULTS' named entity 'CARBOHYDRATE' named entity 'SULPHATED'

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