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Related Concept Videos

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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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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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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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Chemistry of Carbohydrates03:25

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Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...
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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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Related Experiment Video

Updated: May 9, 2025

Single-Animal, Single-Tube RNA Extraction for Comparison of Relative Transcript Levels via qRT-PCR in the Tardigrade Hypsibius exemplaris
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Uncommon N-Glycan Structures in Anhydrobiotic Tardigrades.

Hirokazu Yagi1, Taiki Saito1, Shih-Yun Guu2

  • 1Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan; Department of Creative Research, Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan.

Molecular & Cellular Proteomics : MCP
|April 30, 2025
PubMed
Summary
This summary is machine-generated.

Tardigrades possess unique N-glycosylation patterns, including abundant paucimannose glycans and a novel fucosylation signature, crucial for their extreme stress tolerance.

Keywords:
N-Glycanfucosylationglycomicsglycoproteomicstardigrade

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Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
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Area of Science:

  • Glycobiology
  • Tardigrade Biology
  • Extremophile Research

Background:

  • N-glycosylation plays vital roles in protein function and stability.
  • Tardigrades exhibit remarkable resilience to extreme environmental conditions, but the underlying molecular mechanisms are not fully understood.
  • Glycosylation patterns can be critical for stress adaptation in various organisms.

Purpose of the Study:

  • To characterize the N-glycosylation profiles of anhydrobiotic tardigrades, Ramazzottius varieornatus and Hypsibius exemplaris.
  • To identify unique glycosylation signatures and their potential roles in tardigrade stress tolerance.
  • To investigate the enzymatic machinery potentially responsible for observed glycosylation patterns.

Main Methods:

  • Mass spectrometry-based glycomic analysis of N-glycans from tardigrade species.
  • Identification and quantification of different N-glycan structures, including fucosylation patterns.
  • Comparative analysis of tardigrade glycosylation with other species.
  • Genomic analysis to identify potential fucosyltransferase genes.

Main Results:

  • Tardigrades exhibit high-mannose, paucimannose, and complex-type N-glycans; hybrid-type glycans were absent.
  • Paucimannose glycans were abundant (39% in R. varieornatus, 17% in H. exemplaris), with significant core fucosylation.
  • A unique glycosylation signature with non-reducing terminal α1,3-fucosylated N-acetylglucosamine (GlcNAc) was identified, particularly in H. exemplaris, and induced during anhydrobiosis.
  • Key proteins like Cu/Zn-superoxide dismutase were modified with this unique glycan structure.
  • Tardigrade fucosylation patterns differ from mammalian and other invertebrate structures, suggesting unique fucosyltransferase specificities.

Conclusions:

  • Tardigrades possess distinct N-glycosylation profiles characterized by abundant paucimannose and unique fucosylation patterns.
  • The identified α1,3-fucosylated GlcNAc motif may contribute to tardigrade stress tolerance mechanisms.
  • Homologs of FUT9 and FucTC suggest potential enzymes responsible for this unique glycosylation.
  • Further research into tardigrade glycosylation can illuminate mechanisms of extremotolerance.