The expression of soluble and cell-bound alpha 2,6 sialyltransferase in human colonic carcinoma CaCo-2 cells correlates with the degree of enterocytic differentiation.

Abstract

alpha 2,6 sialyltransferase towards the N-acetyllactosaminyl sequence (alpha 2,6 ST, E.C. 2.4.99.1) is one of the major sialyltransferases in human colonic cells; it strongly increases in human colorectal tumors and is largely expressed in fetal and neonatal rat colon. In this study we demonstrate that human colon carcinoma CaCo-2 cells, which differentiate spontaneously into enterocytes when maintained confluent for several days, exhibit a very high expression of alpha 2,6 ST both in the cell-bound and soluble form. When the CaCo-2 cells were cultured on porous membranes the soluble alpha 2,6 ST was mainly detected in the medium collected from the chamber corresponding to the basolateral face of the monolayer. The soluble alpha 2,6 ST could be concentrated and purified from the alpha 2,3 sialyltransferase by affinity chromatography on Blue Sepharose.

• Authors: F Dall'Olio, N Malagolini, F Serafini-Cessi
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 184 Issue 3 Pg. 1405-10 (May 15 1992) ISSN: 0006-291X [Print] United States
• PMID: 1590800 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Culture Media
• Sialyltransferases
• beta-D-Galactoside alpha 2-6-Sialyltransferase

Topics

• Carbohydrate Sequence
• Cell Differentiation
• Cell Line
• Cell Membrane (enzymology)
• Chromatography, Affinity
• Colonic Neoplasms
• Culture Media
• Humans
• Kinetics
• Molecular Sequence Data
• Sialyltransferases (isolation & purification, metabolism)
• Time Factors
• beta-D-Galactoside alpha 2-6-Sialyltransferase