Be a part of Webinar on Glycomics

Glycans and complementary glycan-binding proteins are essential components in the language of cell-cell interactions in immunity. The study of glycan function is the purview of glycobiology, which has often been presented as an unusually complex discipline. In fact, the human glycome, composed of all of its glycans, is built primarily from only 9 building blocks that are combined by enzymes (writers) with specific and limited biosynthetic capabilities into a tractable and increasingly accessible number of potential glycan patterns that are functionally read by several dozen human glycan-binding proteins (readers). Nowhere is the importance of glycan recognition better understood than in infection and immunity, and knowledge in this area has already led to glycan mimetic anti-infective and anti-inflammatory drugs.

Glycoconjugates belong without doubt to the most complex and diverse molecules found in nature. They are crucial for both prokaryotic and eukaryotic life despite the fact that the glycosylation pathways and building blocks do diverge tremendously between the different phylogenetic kingdoms Glycomics is the comprehensive study of glycomes (the entire complement of sugars, whether free or present in more complex molecules of an organism), including genetic, physiologic, pathologic, and other aspects.

 

Glycans function in many different ways in the body. When sugars bind to proteins, glycation occurs, which prematurely ages the body by decreasing the flexibility of proteins, leading to cataracts as well as decreased nerve and renal functioning and myocardial contractility? The process of glycation is damaging to the body, but glycans function positively on the cell surface to act as antennae, allowing efficient communication. Sugars are essential to human life, and their decrease with aging provides an interesting target for aging prevention. Glycans on the cell surface can be tagged to fluorescent substances and analyzed for changes in their distribution following cosmeceutical application, which provides a way of studying topical glycan modulation and improving appearance of aged skin.

 

Proteins essential to normal cell physiology are usually glycosylated and variation in their glycosylation patterns often leads to changes in their function. Changes in glycosylation pattern can also be associated with disease. It is now becoming increasingly clear how important it is to understand these changes, to gain insight into their involvement in disease mechanisms and the potential for novel therapeutic interventions.

 

There are several different ways to classify the biological roles of glycans, based on the glycan types in question, on the glycan-binding protein involved, etc. Divides glycan functions into four somewhat distinct categories. The first is structural and modulatory roles (including nutrient sequestration). The second category involves extrinsic (interspecies) recognition. The third is intrinsic (interspecies) recognition. Finally, there is molecular mimicry of host glycans. All of these categories can involve glycan-binding proteins.

 

Glycans can mediate a wide variety of biological roles by virtue of their mass, shape, charge, or other physical properties. However, many of their more specific biological roles are mediated via recognition by GBPs. Nature appears to have taken full advantage of the vast diversity of glycans expressed in organisms by evolving protein modules to recognize discrete glycans that mediate specific physiological or pathological processes. Indeed, there are no living organisms in which GBPs have not been found.

 

Initially believed to be inactive molecules, glycans are now considered essential for life, both under normal and pathological conditions. This volume of the series “Biology of Extracellular Matrix” reviews the most recent findings on the role of glycans in the development of diseases and the possible therapeutic use of this class of molecules. It shows how the interaction of glycans with growth factors, growth factor binding proteins, extracellular proteases, protease inhibitors, chemokines, morphogens, and adhesive proteins regulates inflammation.

 

Glycans are saccharides that can be involved to a widespread variation of biological molecules through an enzymatic course called glycosylation to augment their purpose. Of the four essential building blocks of life, proteins, carbohydrates (glycans), lipids and nucleic acids, glycans have expected the smallest consideration from scientists. Glyco-epitope diversity enriches the role of glycans in the group of debilitating and life-shortening disorders known as congenital muscular dystrophy, or CMD. Numerous Glycoepitomics forms of CMD are well-known to result after dysfunctional O-glycosylation of membrane and ECM proteins; however, one-third of CMDs arise from an unknown genetic etiology O-Glycans, , Shared Outer Chains of Glycans, N-Glycans, Glycosphingolipids, Sialic Acids.

The term ‘glycomics’ describes the scientific attempt to identify and study all the glycan molecules the glycome synthesised by an organism. The aim is to create a cell-by-cell catalogue of glycosyltransferase expression and detected glycan structures. The current status of databases and bioinformatics tools, which are still in their infancy, is reviewed. The structures of glycans as secondary gene products cannot be easily predicted from the DNA sequence. The lack of generally accepted ways to normalise glycan structures and exchange glycan formats hampers an efficient cross-linking and the automatic exchange of distributed data. The upcoming glycomics should accept that unrestricted dissemination of scientific data accelerates scientific findings and initiates a number of new initiatives to explore the data.