Publication Date:
2001-10-13
Description:
Poly-alpha2,8-sialic acid (PSA) has been implicated in numerous normal and pathological processes, including development, neuronal plasticity, and tumor metastasis. We report that cell surface PSA expression can be reversibly inhibited by a small molecule, N-butanoylmannosamine (ManBut). Inhibition occurs through a metabolic mechanism in which ManBut is converted to unnatural sialic acid derivatives that effectively act as chain terminators during cellular PSA biosynthesis. N-Propanoylmannosamine (ManProp), which differs from ManBut by a single methylene group, did not inhibit PSA biosynthesis. Modulation of PSA expression by chemical means has a role complementary to genetic and biochemical approaches in the study of complex PSA-mediated events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahal, L K -- Charter, N W -- Angata, K -- Fukuda, M -- Koshland, D E Jr -- Bertozzi, C R -- CA33895/CA/NCI NIH HHS/ -- DK09765/DK/NIDDK NIH HHS/ -- GM58867-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Oct 12;294(5541):380-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11598302" target="_blank"〉PubMed〈/a〉
Keywords:
Carbohydrate Conformation
;
Cell Membrane/*metabolism
;
HeLa Cells
;
Hexosamines/metabolism/*pharmacology
;
Humans
;
Microscopy, Fluorescence
;
Neural Cell Adhesion Molecules/genetics/metabolism
;
Neurons/*metabolism
;
Recombinant Fusion Proteins/metabolism
;
Sialic Acids/*biosynthesis/chemistry
;
Sialyltransferases/genetics/metabolism
;
Transfection
;
Tumor Cells, Cultured
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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