Search PubMed⌕ Search

Biomedical subjects

L Sachs

Publications and source records attributed to L Sachs.

At least 325 records · Page 18Linked to original sources

Mobility of carbohydrate-containing structures on the surface membrane and the normal differentiation of myeloid leukemic cells to macrophages and granulocytes.

Clones (D(+)) of a cultured line of myeloid leukemic cells can be induced to undergo normal differentiation to mature macrophages and granulocytes. There are also clones derived from the same cell line (D(-)) that could not be induced to differentiate. The carbohydrate-binding protein concanavalin A was used as a probe to study the mobility of carbohydrate-containing sites on the surface membrane of these cells. Changes in the distribution of concanavalin A binding sites on the surface membrane can be induced by concanavalin A. With the appropriate site mobility, this induction of a new distribution resulted in a concentration of concanavalin A-membrane site complexes on one pole of the cell to form a cap. D(+) and D(-) clones showed 50 and 5% of cells with caps, respectively, although both types of cells bound a similar number of concanavalin A molecules. Treatment of cells with trypsin increased cap formation from 5 to 40% in D(-) cells, but did not change the percentage of cells with caps in D(+) cells. The results show a difference in the mobility of concanavalin A binding sites in these two types of cells and suggest a difference in the fluid state of these carbohydrate-containing structures on the surface membrane. It is suggested that a gain of the ability of myeloid leukemic cells to undergo normal differentiation is associated with an increase in the fluidity of structures on the surface membrane where the concanavalin A sites are located. Differences in fluidity of specific membrane sites may also explain differences in the response of cells to other differentiation-inducing stimuli.

Agglutination↗

Differences in the binding of fluorescent concanavalin A to the surface membrane of normal and transformed cells.

The binding of fluorescein-conjugated Concanavalin A to the cell surface has been studied in normal and transformed cells in interphase and mitosis. Binding to the cell surface was in the form of an incomplete ring of fluorescence, and the binding was inhibited by alpha-methyl-D-mannopyranoside. All the cells were fluorescent when treated with 25-250 mug/ml of fluorescent Concanavalin A. With 10 mug, the cells were all fluorescent after 30 min of binding, but after 0.5-5 min with 10 mug or 30 min with 1 or 2.5 mug, transformed interphase cells showed a higher percentage of cells with surface fluorescence than did normal interphase cells. Trypsinized normal and transformed interphase cells showed the same fluorescence. Binding with 2.5 mug at 4 degrees instead of at 24 degrees , gave a higher percentage of fluorescent cells with trypsinized than with untrypsinized transformed cells. Mitotic normal cells were similar to transformed interphase cells, whereas mitotic transformed cells were intermediate between normal and transformed interphase cells. The results indicate that the use of low concentrations of fluorescent Concanavalin A can show differences in surface fluorescence between normal and transformed, interphase and mitotic, and trypsinized and untrypsinized cells. It is suggested that the observed differences in fluorescence can be explained by differences in affinity of the lectin binding sites and/or differences in the clustering of sites.

Animals↗