In:
BMC Cancer, Springer Science and Business Media LLC, Vol. 11, No. 1 ( 2011-12)
Kurzfassung:
Emmprin, a glycoprotein containing two Ig domains, is enriched on tumor cell surfaces and stimulates matrix metalloproteinase (MMP) production by adjacent stromal cells. Its first Ig domain (ECI) contains the biologically active site. The dependence of emmprin activity on N-glycosylation is controversial. We investigated whether synthetic ECI with the shortest sugar is functionally active. Methods The whole ECI peptides carrying sugar chains, a chitobiose unit or N-linked core pentasaccharide, were synthesized by the thioester method and added to fibroblasts to examine whether they stimulate MMP-2 production. Results ECI carrying a chitobiose unit, ECI-(GlcNAc) 2 , but not ECI without a chitobiose unit or the chitobiose unit alone, dose-dependently stimulated MMP-2 production by fibroblasts. ECI with longer chitobiose units, ECI-[(Man) 3 (GlcNAc) 2 ], also stimulated MMP-2 production, but the extent of its stimulation was lower than that of ECI-(GlcNAc) 2 . Conclusions Our results indicate that ECI can mimic emmprin activity when substituted with chitobiose, the disaccharide with which N-glycosylation starts.
Materialart:
Online-Ressource
ISSN:
1471-2407
DOI:
10.1186/1471-2407-11-300
Sprache:
Englisch
Verlag:
Springer Science and Business Media LLC
Publikationsdatum:
2011
ZDB Id:
2041352-X
