Glycosaminoglycanomics: where we are

• Published in: Glycoconjugate journal Vol. 34; no. 3; pp. 339 - 349
• Main Authors: Ricard-Blum, Sylvie, Lisacek, Frédérique
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.06.2017; Springer Nature B.V
• Subjects: Angiogenesis; Animals; Biochemistry; Biomedical and Life Sciences; Cancer; Cell adhesion; Cell adhesion & migration; Cell Communication; Cell surface; Chromatography - instrumentation; Chromatography - methods; Computational Biology - methods; Data processing; Databases, Chemical; Eukaryotic Cells - chemistry; Eukaryotic Cells - metabolism; Extracellular matrix; Extracellular Matrix - chemistry; Extracellular Matrix - metabolism; Glycomics - instrumentation; Glycomics - methods; Glycomics - trends; Glycosaminoglycans; Growth factors; Heparan sulfate; Heparitin Sulfate - chemistry; Heparitin Sulfate - metabolism; Host-Pathogen Interactions; Humans; Innate immunity; Intercellular Signaling Peptides and Proteins - chemistry; Intercellular Signaling Peptides and Proteins - metabolism; Life Sciences; Magnetic Resonance Spectroscopy - instrumentation; Mass Spectrometry - instrumentation; Mass Spectrometry - methods; Neurodegenerative diseases; Pathogens; Pathology; Protein Binding; Review; Reviews; Sulfates; Interaction networks; Databases; Glycosaminoglycomics; Heparanome; Bioinformatics; Glycosaminoglycan-protein interaction
• ISSN: 0282-0080; 1573-4986; 1573-4986
• DOI: 10.1007/s10719-016-9747-2

Glycosaminoglycans regulate numerous physiopathological processes such as development, angiogenesis, innate immunity, cancer and neurodegenerative diseases. Cell surface GAGs are involved in cell-cell and cell-matrix interactions, cell adhesion and signaling, and host-pathogen interactions. GAGs contribute to the assembly of the extracellular matrix and heparan sulfate chains are able to sequester growth factors in the ECM. Their biological activities are regulated by their interactions with proteins. The structural heterogeneity of GAGs, mostly due to chemical modifications occurring during and after their synthesis, makes the development of analytical techniques for their profiling in cells, tissues, and biological fluids, and of computational tools for mining GAG-protein interaction data very challenging. We give here an overview of the experimental approaches used in glycosaminoglycomics, of the major GAG-protein interactomes characterized so far, and of the computational tools and databases available to analyze and store GAG structures and interactions.