JBC, Vol. 250, Issue 7, 2447-2451, Apr, 1975
Surface carbohydrates of hamster fibroblasts. II. Interaction of hamster NIL cell surfaces with Ricinus communis lectin and concanavalin A as revealed by surface galactosyl label
C. G. Gahmberg and S. Hakomori
When hamster fibroblasts (NIL) were treated with galactose oxidase followed
by reduction with tritiated borohydride (GAHMBERG, C. G. AND HAKOMORI, S.
(1973) J. Biol. Chem. 248, 4311; STECK, T. L., AND DAWSON, G. (1974) J.
Biol. Chem. 249, 2135), two major galactoprotein labels were detected on
the cell surface: "galactoprotein a" (apparent molecular weight 200,000)
and "galactoprotein b" (apparent molecular weight 130,000). The labeling in
galactoprotein a of NIL cells was greatly suppressed by pretreating cells
with a high concentration of Ricinus communis lectin or concanavalin A,
whereas the label in it was greatly enhanced with a low concentration of
the lectins. The label in galactoprotein b of NIL cells was less affected
by pretreatment with lectins. In NILpy cells the label in galactoprotein a
was absent and the lable in galactoprotein b was enhanced by pretreating
cells with lectins at low concentrations, but it was suppressed at high
concentrations. The results indicate that NIL cells mainly interact with
the lectins through galactoprotein a, whereas NILpy cells interact with the
lectins through galacto-protein b. After treatment with lectins, the
glycolipids of normal NIL cells, but not NILpy cells, became exposed as
evidenced by enhanced labeling, possibly because of "clustering" of
glyco-proteins. These results support the view that specific, well defined
glycoproteins are the binding sites for lectins, and that these interacting
glycoproteins are qualitatively different in normal and transformed cells.
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