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Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

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Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
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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.
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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.
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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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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.
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Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
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Polysialic acid: biosynthesis, novel functions and applications.

Karen J Colley1, Ken Kitajima, Chihiro Sato

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Summary

Polysialic acid (polySia) is vital for nervous system development and cancer progression. Its unique binding properties and bacterial enzyme applications show significant therapeutic potential for tissue repair and drug delivery.

Keywords:
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Area of Science:

  • Biochemistry
  • Glycobiology
  • Neuroscience

Background:

  • Polysialic acid (polySia) plays crucial roles in the nervous system, cancer, and tissue repair.
  • It modifies glycoproteins like NCAM, influencing cell adhesion and signaling.
  • Bacterial polySia aids immune evasion, while mammalian polySia has specific protein targets.

Purpose of the Study:

  • To review the biosynthesis and functions of mammalian polySia.
  • To explore the therapeutic applications of polySia.
  • To highlight the importance of polySia's quality and quantity in its functions.

Main Methods:

  • Literature review focusing on polysialic acid biosynthesis, function, and therapeutic uses.
  • Analysis of studies on mammalian and bacterial polysialyltransferases.
  • Examination of polySia's interaction with biomolecules and its role in disease and therapy.

Main Results:

  • Mammalian polysialyltransferases exhibit specific protein recognition for polySia addition.
  • PolySia's functions extend beyond anti-adhesion to include binding of signaling molecules, dependent on chain length.
  • Bacterial polySia offers a 'stealth' characteristic beneficial for therapeutic protein modification.

Conclusions:

  • PolySia's role is nuanced, depending on its quality and quantity, not just presence.
  • Bacterial polysialyltransferases present significant therapeutic potential, particularly for neural regeneration and tissue repair.
  • PolySia is a promising alternative to polyethylene glycol for developing immunogenic therapeutic proteins with extended half-lives.