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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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The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
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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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Ganglioside Extraction, Purification and Profiling
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Ganglioside biochemistry.

Thomas Kolter1

  • 1Program Unit Membrane Biology & Lipid Biochemistry, LiMES, University of Bonn, Gerhard-Domagk Straße 1, 53121 Bonn, Germany.

ISRN Biochemistry
|May 14, 2015
PubMed
Summary

This paper overviews gangliosides, which are sialic acid-containing glycosphingolipids. It summarizes their structures, occurrence, metabolism, and key functional, biochemical, and pathobiochemical aspects.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Gangliosides are complex glycosphingolipids characterized by the presence of sialic acid.
  • They are prominently expressed on neuronal cell surfaces, forming intricate patterns.
  • Gangliosides are also found in various other cell types throughout the body.

Purpose of the Study:

  • To provide a comprehensive overview of ganglioside structures.
  • To detail the occurrence and distribution of gangliosides in different cell types.
  • To summarize the metabolism, function, and pathobiochemistry of gangliosides.

Main Methods:

  • Literature review and synthesis of existing research.
  • Comparative analysis of ganglioside structures and functions.

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  • Summary of metabolic pathways and biochemical properties.

    • Main Results:

    • Detailed descriptions of diverse ganglioside structures.
    • Elucidation of their specific localization, particularly in neuronal tissues.
    • Summary of key metabolic enzymes and pathways involved in ganglioside synthesis and degradation.
    • Highlighting critical roles in cellular function and disease.

    Conclusions:

    • Gangliosides are crucial molecules with diverse structures and functions.
    • Their complex expression patterns, especially in neurons, underscore their importance.
    • Understanding ganglioside metabolism and biochemistry is vital for} elucidating their roles in health and disease.