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Related Experiment Video

Updated: Jun 26, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Molecular cloning and functional expression of two members of mouse NeuAcalpha2,3Galbeta1,3GalNAc

Y C Lee1, M Kaufmann, S Kitazume-Kawaguchi

  • 1Molecular Glycobiology, Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-0198, Japan.

The Journal of Biological Chemistry
|April 17, 1999
PubMed
Summary

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Diagnosis and treatment of acute central cervical cord injury.

Chinese medical journal·1999
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[Histological evaluation of collagen-hydroxyapatite composite as osseous implants in the repair of mandibular defect].

Zhongguo xiu fu chong jian wai ke za zhi = Zhongguo xiufu chongjian waike zazhi = Chinese journal of reparative and reconstructive surgery·1999
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[A new method to repair artery injuries in extremities by phleboplasty of branched vein graft].

Zhongguo xiu fu chong jian wai ke za zhi = Zhongguo xiufu chongjian waike zazhi = Chinese journal of reparative and reconstructive surgery·1999
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Evidence of an interaction between Mos and Hsp70: a role of the Mos residue serine 3 in mediating Hsp70 association.

Oncogene·1999
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[Relationship between the expression of transforming growth factor beta type I receptor (T beta R I) and prognosis of hepatocellular carcinoma (HCC)].

Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology·1999
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Captopril and platelet-activating factor (PAF) antagonist prevent cardiac allograft vasculopathy in rats: role of endogenous PAF and PAF-like compounds.

The Journal of heart and lung transplantation : the official publication of the International Society for Heart Transplantation·1999
This summary is machine-generated.

Researchers identified a new mouse sialyltransferase, ST6GalNAc IV, crucial for adding sialic acid to specific sugar structures. This enzyme shows distinct preferences for O-glycans over glycolipids, unlike its counterpart ST6GalNAc III.

Area of Science:

  • Biochemistry
  • Glycobiology
  • Enzymology

Background:

  • Sialyltransferases are key enzymes in glycosylation, synthesizing sialic acid linkages.
  • Understanding specific sialyltransferase functions is vital for elucidating biological processes and disease mechanisms.

Purpose of the Study:

  • To isolate and characterize novel sialyltransferases from mouse brain cDNA libraries.
  • To determine the substrate specificity and functional characteristics of a newly identified enzyme.

Main Methods:

  • cDNA cloning and sequencing from mouse brain libraries.
  • Expression and purification of recombinant soluble enzyme.
  • Enzymatic activity assays using various substrates (glycoproteins, glycolipids, and synthetic acceptors).
  • Sialidase sensitivity analysis of sialylated products.

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Main Results:

  • Two cDNA clones encoding GalNAcalpha2,6-sialyltransferase were isolated; one homologous to rat ST6GalNAc III, and a novel one designated mouse ST6GalNAc IV.
  • Mouse ST6GalNAc IV exhibits activity towards NeuAcalpha2,3Galbeta1,3GalNAc, fetuin, and GM1b, requiring sialic acid on Galbeta1,3GalNAc residues.
  • The expressed enzyme prefers O-glycans as substrates over glycolipids, differentiating it from ST6GalNAc III which favors glycolipids.

Conclusions:

  • Mouse ST6GalNAc IV represents a newly discovered GalNAcalpha2,6-sialyltransferase with unique substrate preferences.
  • The distinct substrate specificities of ST6GalNAc III and IV highlight their specialized roles in cellular glycosylation.
  • Further research into ST6GalNAc IV function can illuminate its role in mammalian biology and disease.