Document Detail


Chondroitin/dermatan 2-O sulfotransferase potentiates Fgf2 induced cell migration.
MedLine Citation:
PMID:  25480151     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Fibroblast growth factor-2 (Ffg2) is involved in several biological functions. Fgf2 requires glycosaminoglycans, like chondroitin/dermatan sulfate (CS/DS) as co-receptors. CS/DS are linear polysaccharides composed of repeating disaccharide units [-4GlcUAβ1-3-GalNAc-β1-] and [-4IdoUAα1-3-GalNAc-β1-], which can be sulfated. Uronyl 2-O-sulfotransferase (Ust) introduces sulfation at the C2 of IdoUA and GlcUA resulting in over-sulfated units. CHO-K1 cells over-expressing Ust contain significantly more CS/DS 2-O sulfated units, while Ust knock-down abolished CS/DS 2-O sulfation. Structural difference of CS/DS resulted in altered Fgf2 binding and increased p-ERK1/2. As functional consequence of CS/DS 2-O sulfation and altered Fgf2 binding, cell migration and paxillin activation was increased. Inhibition of sulfation, knock-down of Ust and inhibition of FgfR resulted in reduced migration. Similarly, Fgf2 treatment increased migration, which was abolished by Ust knock-down in 3T3 cells. The proteoglycan controlling the CHO migration was syndecan1. Knock-down of Sdc1 in CHO-K1/Ust abolished cell migration. We conclude that the presence of distinctly sulfated CS/DS can tune the Fgf2 effect on cell migration.
Authors:
Katerina Nikolovska; Dorothe Spillmann; Daniela G Seidler
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-12-5
Journal Detail:
Title:  Journal of cell science     Volume:  -     ISSN:  1477-9137     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2014 Dec 
Date Detail:
Created Date:  2014-12-6     Completed Date:  -     Revised Date:  2014-12-7    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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