Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 131, Issue 31, Pages 11041-11048Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja903038d
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Funding
- Div Of Information & Intelligent Systems
- Direct For Computer & Info Scie & Enginr [1019160] Funding Source: National Science Foundation
- NCRR NIH HHS [R41 RR023764-02, RR023764, R41 RR023764] Funding Source: Medline
- NHLBI NIH HHS [R01 HL094463, R01 HL062244, R01 HL096972-01, R01 HL096972, HL094463, R01 HL062244-08, HL62244] Funding Source: Medline
- NIGMS NIH HHS [R01 GM038060, R01 GM038060-20, GM38060, R01 GM090257] Funding Source: Medline
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Using digital microfluidics, recombinant enzyme technology, and magnetic nanoparticles, we have created a functional prototype of an artificial Golgi organelle. Analogous to the natural Golgi, which is responsible for the enzymatic modification of glycosaminoglycans immobilized on proteins, this artificial Golgi enzymatically modifies glycosaminoglycans, specifically heparan sulfate (HS) chains immobilized onto magnetic nanoparticles. Sulfo groups were transferred from adenosine X-phosphate 5'-phosphosulfate to the 3-hydroxyl group of the D-glucosamine residue in an immobilized HS chain using D-glucosaminyl 3-O-sulfotransferase. After modification, the nanoparticles with immobilized HS exhibited increased affinity for fluorescently labeled antithrombin III as detected by confocal microscopy. Since the biosynthesis of HS involves an array of specialized glycosyl transferases, epimerase, and sulfotransferases, this approach should mimic the synthesis of HS in vivo. Furthermore, our method demonstrates the feasibility of investigating the effects of multienzyme systems on the structure of final glycan products for HS-based glycomic studies.
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