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Permanent link (DOI): https://doi.org/10.7939/R3ZG6GJ13

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Substrates of the Human Neuraminidase and Sialic Acid Esterase Enzymes Open Access

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Other title
Subject/Keyword
Human Neuraminidase
Sialic Acid Esterase
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Khanna, Neha
Supervisor and department
Cairo, Christopher (Chemistry)
Examining committee member and department
Lowary, Todd (Chemistry)
Campbell, Robert (Chemistry)
Department
Department of Chemistry
Specialization

Date accepted
2014-09-25T11:59:56Z
Graduation date
2014-11
Degree
Master of Science
Degree level
Master's
Abstract
Neuraminidase enzymes (NEU) catalyze the cleavage of sialic acid residues from sialylated oligosaccharides, glycoproteins, and glycolipids. The human neuraminidase enzymes (hNEU) are a family of four isoenzymes (NEU1, NEU2, NEU3, and NEU4), which cleave terminal sialic acid groups (exo-sialidase). Members of the hNEU family are proposed play important roles in health and disease by controlling the composition of cellular sialosides. The membrane-associated enzyme, NEU3, is responsible for cleaving glycolipid substrates and plays critical roles in cell signaling. Although gangliosides, such as GM3, are known as substrates for NEU3, there are several uncommon natural analogs of this substrate found in human cells, including Neu5Gc and 9-O-Ac-Neu5Ac derivatives. This thesis presents the synthesis and characterization of a series of GM3 analogs {Neu5Acα(2→3)Galβ(1→4)Glcβ(1→1)cer} with an octyl aglycone and containing either Neu5Ac, Neu5Gc, or 9-O-Ac-Neu5Ac terminal residues. Furthermore, we generated each of these compounds with either an α(2→3)- or α(2→6)-glycosidic linkage. Additionally, to examine the role of the sialic acid esterase (SIAE) enzyme, which is responsible for degredation of 9-O-Ac-Neu5Ac residues, we developed a synthesis of a chloro-acetate analog of the esterase substrate, which will be studied as an inhibitor or label of the SIAE.
Language
English
DOI
doi:10.7939/R3ZG6GJ13
Rights
This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for the purpose of private, scholarly or scientific research. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.
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