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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

7.4K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Proteoglycans01:05

Proteoglycans

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Glycosaminoglycans01:23

Glycosaminoglycans

5.2K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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Glycan Node Analysis: A Bottom-up Approach to Glycomics
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Decoding glycans: deciphering the sugary secrets to be coherent on the implication.

Shreya Sharma1, Shashank Shekhar1, Bhasha Sharma1

  • 1Department of Chemistry, Netaji Subhas University of Technology Dwarka Sec-2 Delhi India sharmabhasha@gmail.com.

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Advances in glycobiology and glycochemistry enable new biomedical discoveries. This study highlights complex glycan therapeutic potentials and diagnostic strategies for diseases, addressing current knowledge gaps.

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Area of Science:

  • Glycobiology and Glycochemistry
  • Biomedical Sciences

Background:

  • Glycans, sugar-based polymers, are crucial in biological processes like immune response and cell-cell interactions.
  • Unlike proteins or DNA, complex glycans present challenges in laboratory synthesis and structural analysis due to isomerism and lack of a defined alphabet.
  • Despite their importance, glycan-based therapeutics and glycomimetics remain underexploited.

Purpose of the Study:

  • To review significant contributions enhancing the therapeutic utilization of complex glycans.
  • To discuss diagnostic strategies for recurrent diseases related to glycan alterations.
  • To address existing challenges in glycan research and application.

Main Methods:

  • Review of neoteric techniques and methodological advances in glycobiology and glycochemistry.
  • Analysis of current understanding of glycan structures and functions.
  • Discussion of therapeutic potentials and diagnostic strategies.

Main Results:

  • Methodological advances are paving the way for new discoveries in biomedical sciences.
  • Glycans play vital roles in cellular functions and disease processes.
  • Significant potential exists for glycan-based therapeutics and glycomimetics.

Conclusions:

  • Further research and exploitation of glycan-based therapeutics are needed.
  • Improved diagnostic strategies for glycan-related diseases are essential.
  • Addressing the complexities of glycan synthesis and analysis is key to unlocking their full potential.