Specific sides to multifaceted glycosaminoglycans are observed in embryonic development

Ubiquitously found in the extracellular matrix and attached to the surface of most cells, glycosaminoglycans (GAGs) mediate many intercellular interactions. Originally described in 1889 as the primary carbohydrate in cartilage and then in 1916 as a coagulation inhibitor from liver, various GAGs have...

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Published inSeminars in cell & developmental biology Vol. 21; no. 6; pp. 631 - 637
Main Author Kramer, Kenneth L.
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.08.2010
Subjects
Animals
Carbohydrate Conformation
Carbohydrate Sequence
Chondroitin sulfate
Embryonic Development
Extracellular Matrix - chemistry
Glycosaminoglycan
Glycosaminoglycans - chemistry
Glycosaminoglycans - metabolism
Heparan sulfate
Homeostasis
Hyaluronan
Keratan sulfate
Molecular Sequence Data
Morphogenesis
Heparan sulfate
Hyaluronan
Glycosaminoglycan
Chondroitin sulfate
Keratan sulfate
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Summary:Ubiquitously found in the extracellular matrix and attached to the surface of most cells, glycosaminoglycans (GAGs) mediate many intercellular interactions. Originally described in 1889 as the primary carbohydrate in cartilage and then in 1916 as a coagulation inhibitor from liver, various GAGs have since been identified as key regulators of normal physiology. GAGs are critical mediators of differentiation, migration, tissue morphogenesis, and organogenesis during embryonic development. While GAGs are simple polysaccharide chains, many GAGs acquire a considerable degree of complexity by extensive modifications involving sulfation and epimerization. Embryos that lack specific GAG modifying enzymes have distinct developmental defects, illuminating the importance of GAG complexity. Revealing how these complex molecules specifically function in the embryo has often required additional approaches, the results of which suggest that GAG modifications might instructively mediate embryonic development.
Bibliography:ObjectType-Article-2
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ISSN:1084-9521
1096-3634
DOI:10.1016/j.semcdb.2010.06.002