Glycodelin and amniotic fluid transferrin as inhibitors of E-selectin-mediated cell adhesion

• Published in: Histochemistry and cell biology Vol. 119; no. 5; pp. 345 - 354
• Main Authors: Jeschke, Udo, Wang, Xiaoyu, Briese, Volker, Friese, Klaus, Stahn, Renate
• Format: Journal Article
• Language: English
• Published: Germany Springer Nature B.V 01.05.2003
• Subjects: Adult; Amniotic Fluid - chemistry; Cell Adhesion - drug effects; Cells, Cultured; Dose-Response Relationship, Drug; Drug Combinations; E-Selectin - metabolism; E-Selectin - pharmacology; Endothelium, Vascular - cytology; Endothelium, Vascular - drug effects; Endothelium, Vascular - metabolism; Female; Glycodelin; Glycoproteins - isolation & purification; Glycoproteins - metabolism; Glycoproteins - pharmacology; Hepatocytes - cytology; Hepatocytes - drug effects; Hepatocytes - metabolism; Humans; Inhibitory Concentration 50; Lewis X Antigen - metabolism; Pregnancy - blood; Pregnancy Proteins - isolation & purification; Pregnancy Proteins - metabolism; Pregnancy Proteins - pharmacology; Transferrin - isolation & purification; Transferrin - metabolism; Transferrin - pharmacology
• ISSN: 0948-6143; 1432-119X
• DOI: 10.1007/s00418-003-0529-0

Human amniotic fluid contains a variety of glycoproteins. Several of these substances have been shown to exert immunomodulatory effects. Glycodelin, previously known as placental protein 14, is one of these glycoproteins. It has a unique carbohydrate configuration, consistent with fucosylated LacdiNAc structures that are very unusual for mammals. Oligosaccharides with fucosylated LacdiNAc antennae have previously been shown to block selectin-mediated cell adhesion. Another glycoprotein, human transferrin, is also present in amniotic fluid in relatively high concentrations. This transferrin shows a different glycosylation compared with serum transferrin. Amniotic fluid transferrin carries sialylated Lewis X antigens. Glycodelin and transferrin were isolated from amniotic fluid and for comparison from serum of pregnant women by chromatographic methods. The purified proteins were used as ligands to block E-selectin-mediated HepG2 cell adhesion. Two types of binding assays with distinct receptor accommodations (immobilised E-selectin and activated HUVECs) were used to quantify inhibition efficiencies of the different proteins. We found that glycodelin is a strong inhibitor with a 10(3)-fold potency compared to the monovalent tetrasaccharide sialyl Lewis X whereas the potency of transferrin is rather low.