Biomaterials, Biodegradables and Biomimetics Research Group

Invited Lecture

Sulfated glycosaminoglycans: biosynthesis, bioactivities and associated diseases 


Authors: Pashkuleva I.
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Abstract

Glycosylation is the most common of all known protein post-translational modifications. Virtually all animal cells produce proteoglycans and secrete them into the extracellular matrix (ECM), insert them into the plasma membrane, or store them in secretory granules. Thus, the glycans and particularly glycosaminoglycans (GAGs) are key element of the closest cellular environment where they can either determine the physical characteristics of tissues or modulate the biological functions of cells.

The biological activity of GAGs depends on several properties such as molecular weight, monosaccharide constituents, bonds between the disaccharides repeating units. Among those the negative charge, intrinsic to all GAGs, is of prime importance. This charge is generally associated with the presence of sulfate groups. Sulfation is a dynamic posttranslational modification process: different sulfation patterns have been identified for the same organs and cells during their development. In contrast to phosphorylation that is involved in the intracellular signal transduction, sulfation modulates extracellular signals such as cell-cell and cell-matrix interactions. Alternations in the degree of sulfation of GAGs are also associated with different disorders in humans.

This talk will make a brief overview of the role of GAG sulfation in different biological processes at cellular, tissue and organism level. The connection between the sulfation patterns of GAGs and several physiological processes will be addressed. Misregulation of GAG sulfation and its involvement in several genetic and metabolic disorders in human will be also discussed. Finally, the therapeutic potential of GAGs and their synthetic mimics in the biomedical field will be presented briefly.

Journal
CHEM2NATURE First School
Keywords
Glycosaminoglycans, Sulfation
Rights
Open Access
Peer Reviewed
Yes
Status
published
Project
CHEM2NATURE
Year of Publication
2016
Date Published
2016-11-21
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