Changes in glycoprotein fucosylation in a concanavalin A-resistant variant of a human leukemia cell line (K562).

Abstract:

:Previous studies from this and other laboratories have shown that variants of tumor cell lines can be selected for resistance to the lytic action of natural killer (NK) cells. One of these (K562-Clone I), when made resistant to the toxic effects of Concanavalin A (Con A-R1), regained its sensitivity to NK. Comparing the plasma membranes of Clone I and Con A-R1, we observed 1) a very similar electrophoretic pattern of membrane glycoproteins identified by binding to the lectins Con A, WGA, PNA, and SBA; 2) an increase in binding of Ulex europaeus lectin to a group of glycoproteins from Con A-R1 that were sensitive to treatment with fucosidase and N-glycanase and that had a diffuse mobility ranging in apparent molecular weight from 30 to 200 kDa; and 3) a marked decrease in binding of an antibody reactive with the lactoneofucopentaose III antigen (Lewis x). This constellation of changes is an unusual pattern to follow Con A resistance and may point to a pathway of glycosylation that a leukemic cell might use to modify its recognition by the NK mechanism.

journal_name

J Cell Biochem

authors

Bernier LG,Sullivan AK

doi

10.1002/jcb.240370207

subject

Has Abstract

pub_date

1988-06-01 00:00:00

pages

203-12

issue

2

eissn

0730-2312

issn

1097-4644

journal_volume

37

pub_type

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