Premium
α2, 6 sialylation of N ‐acetyllactosaminic sequences in human colorectal cancer cell lines. Relationship with non‐adherent growth
Author(s) -
Dall'olio Fabio,
Malagolini Nadia,
Stefano Giuseppina Di,
Ciambella Manuela,
SerafiniCessi Franca
Publication year - 1991
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910470220
Subject(s) - sialyltransferase , lectin , colorectal cancer , cell culture , glycolipid , glycoprotein , sambucus nigra , biology , sialic acid , agglutinin , microbiology and biotechnology , biochemistry , concanavalin a , cancer , in vitro , genetics
In a previous work we found that human colorectal cancer tissues express increased levels of an α2,6 sialyltransferase (α2,6 ST) acting on N ‐acetyllactosaminic sequences (E.C. 2.4.99.1). In this study we have taken advantage of the known specificity of elderberry bark lectin (Sambucus nigra agglutinin, SNA) for NeuAcα2, 6Gal/GalNAc structures to investigate the relationship between expression of α2,6 sialyltransferase activity and occurrence of α2,6‐sialylated oligosaccharide sequences in human colorectal cancer cell lines. Three cell lines with opposite adhesion properties were used in this study: SW 948 cells grow adherent to the culture flask surface and express very low levels of enzyme activity; COLO 205 cells grow in non‐adherent form and express the highest levels of α2,6 ST activity; A non‐adherent subline of SW 948 cells (SW 948 FL) was isolated and found to express high levels of α2,6 ST activity. By using SNA‐Sepharose chromatography we found that expression of α2,6 ST activity correlates with the extent of α2,6‐sialylation of N ‐linked chains of glycoproteins but not with the presence of α2,6‐sialylated glycolipids.