Document Detail

Hypoxic regulation of glycosylation via the N-acetylglucosamine cycle.
MedLine Citation:
PMID:  21297907     Owner:  NLM     Status:  PubMed-not-MEDLINE    
Glucose is an energy substrate, as well as the primary source of nucleotide sugars, which are utilized as donor substrates in protein glycosylation. Appropriate glycosylation is necessary to maintain the stability of protein, and is also important in the localization and trafficking of proteins. The dysregulation of glycosylation results in the development of a variety of disorders, such as cancer, diabetes mellitus and emphysema. Glycosylation is kinetically regulated by dynamically changing the portfolio of glycosyltransferases, nucleotide sugars, and nucleotide sugar transporters, which together form a part of what is currently referred to as the "Glycan cycle". An excess or a deficiency in the expression of glycosyltransferases has been shown to alter the glycosylation pattern, which subsequently leads to the onset, progression and exacerbation of a number of diseases. Furthermore, alterations in intracellular nucleotide sugar levels can also modulate glycosylation patterns. It is observed that pathological hypoxic microenvironments frequently occur in solid cancers and inflammatory foci. Hypoxic conditions dramatically change gene expression profiles, by activating hypoxia-inducible factor-1, which mediates adaptive cellular responses. Hypoxia-induced glycosyltransferases and nucleotide sugar transporters have been shown to modulate glycosylation patterns that are part of the mechanism associated with cancer metastasis. Hypoxia-inducible factor-1 also induces the expression of glucose transporters and various types of glycolytic enzymes, leading to shifts in glucose metabolic patterns. This fact strongly suggests that hypoxic conditions are an important factor in modulating various nucleotide sugar biosynthetic pathways. This review discusses some of the current thinking of how hypoxia alters glucose metabolic fluxes that can modulate cellular glycosylation patterns and consequently modify cellular functions, particularly from the standpoint of the N-acetylglucosamine cycle, a part of the "Glycan cycle".
Ken Shirato; Kazuki Nakajima; Hiroaki Korekane; Shinji Takamatsu; Congxiao Gao; Takashi Angata; Kazuaki Ohtsubo; Naoyuki Taniguchi
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Publication Detail:
Type:  Journal Article     Date:  2010-12-29
Journal Detail:
Title:  Journal of clinical biochemistry and nutrition     Volume:  48     ISSN:  1880-5086     ISO Abbreviation:  J Clin Biochem Nutr     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-02-07     Completed Date:  2011-07-14     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  8700907     Medline TA:  J Clin Biochem Nutr     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  20-5     Citation Subset:  -    
Department of Disease Glycomics, Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka 567-0047, Japan.
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