Nucleic Acids Research, Vol 24, Issue 20 4003-4008, Copyright © 1996 by Oxford University Press
A Stoddart, Y Zhang and CJ Paige
We describe the isolation of a cDNA encoding a murine sialic acid- specific
9-O-acetylesterase as well as its expression pattern in cells of both
hematopoietic and non-hematopoietic origin. This enzyme catalyzes the
removal of O-acetyl ester groups from position 9 of the parent sialic acid
N-acetylneuraminic acid. The cDNA is 2105 nt in length and encodes a
protein of 541 amino acids with a predicted molecular weight of 61 kDa, not
including oligosaccharides linked to eight potential N-glycosylation sites.
The cDNA encoding the acetylesterase displays a widespread distribution in
various cell lines and tissues. Expression studies of B lineage cell lines
and primary fetal liver cells revealed a developmentally regulated
expression pattern in cells of hematopoietic origin. Given the importance
of 9-O- acetylation of sialic acids, the cloning of the cDNA encoding a
sialic acid-specific 9-O-acetylesterase will be helpful in understanding
further the regulation of this post-translational modification and the
biological consequences thereof.
ARTICLES
Molecular cloning of the cDNA encoding a murine sialic acid-specific 9- O-acetylesterase and RNA expression in cells of hematopoietic and non- hematopoietic origin
The Wellesley Hospital Research Institute, University of Toronto, Ontario, Canada.
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H. Takematsu, S. Diaz, A. Stoddart, Y. Zhang, and A. Varki Lysosomal and Cytosolic Sialic Acid 9-O-Acetylesterase Activities Can Be Encoded by One Gene via Differential Usage of a Signal Peptide-encoding Exon at the N Terminus J. Biol. Chem., September 3, 1999; 274(36): 25623 - 25631. [Abstract] [Full Text] [PDF] |
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