K. Fukushima et al., ELEVATION OF ALPHA-2-]6 SIALYLTRANSFERASE AND ALPHA-1-]2 FUCOSYL-TRANSFERASE ACTIVITIES IN HUMAN CHORIOCARCINOMA, Cancer research, 58(19), 1998, pp. 4301-4306
Structures of N-linked sugar chains are species and tissue specific an
d change in the course of tumorigenesis. Sialyl linkages of human plac
ental glycoproteins are exclusively Neu5Ac alpha 2-->3Gal, whereas Fuc
alpha 1-->2Gal and Neu5Ac alpha 2-->6Gal residues are expressed in hu
man chorionic gonadotropin and alkaline phosphatase, which are produce
d in human choriocarcinoma JEG-3 and BeWo cells. In the present study,
to elucidate the enzymological and molecular biological basis of the
structural changes that occur in the course of tumorigenesis, (alpha 1
-->2 fucosyltransferase, alpha 2-->3 and alpha 2-->6 sialyltransferase
activities, and the expression levels of the corresponding mRNAs were
measured. The alpha 2-->3 sialyltransferase activity did not change a
s a result of tumorigenesis; however, the alpha 2-->6 sialyltransferas
e activity and alpha 1-->2 fucosyltransferase activity in JEG-3 and Be
Wo cells increased to levels several times higher than those in placen
ta. Competitive PCR analysis showed that the expression levels of mRNA
encoding alpha 1-->2fucosyltransferase and mRNA encoding alpha 2-->6s
ialyltransferase increased significantly as a result of tumorigenesis,
indicating that such structural changes are regulated at the level of
transcription of these glycosyltransferase genes.