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Related Experiment Videos

Cytosolic glycosidases: do they exist?

J F Haeuw1, J C Michalski, G Strecker

  • 1Université des Sciences et Techniques de Lille Flandres-Artois, Laboratoire de Chimie Biologique (Unité Mixte de Recherche no. 111 du CNRS), Villeneuve d'Ascq, France.

Glycobiology
|November 1, 1991
PubMed
Summary

Rat liver cytosol contains specific alpha-D-mannosidases distinct from lysosomal enzymes. These enzymes play a role in controlling N-glycosylprotein biosynthesis by degrading unfinished glycans.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Alpha-D-mannosidases are crucial enzymes involved in glycoprotein metabolism.
  • Understanding their substrate specificity and localization is key to elucidating cellular pathways.

Purpose of the Study:

  • To investigate the substrate specificity of alpha-D-mannosidases in rat liver lysosomes and cytosol.
  • To differentiate the roles and origins of these mannosidases in glycoprotein processing.

Main Methods:

  • Utilized oligomannosidic oligosaccharides as substrates.
  • Characterized hydrolysis products using 400 MHz 1H-NMR spectroscopy.

Main Results:

  • Lysosomal alpha-D-mannosidase activity is a two-step process involving Zn(2+)-independent and dependent enzymes, yielding Man(beta 1-4)GlcNAc.

Related Experiment Videos

  • Cytosolic pathway produces a unique hexasaccharide (Man5GlcNAc) in one step, mirroring N-glycosylprotein biosynthesis intermediates.
  • Enzymatic parameters of lysosomal, endoplasmic reticulum, and cytosolic alpha-D-mannosidases differ significantly.

    • Conclusions:

    • Rat liver cytosol possesses unique alpha-D-mannosidases not derived from lysosomes or endoplasmic reticulum.
    • Cytosolic endo-N-acetyl-beta-D-glucosaminidase activity suggests a role in controlling N-glycosylprotein biosynthesis by degrading incomplete glycans.