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Biomedical subjects

L Sachs

Publications and source records attributed to L Sachs.

At least 343 records · Page 19Linked to original sources
PubMed1972

Virus deoxyribonucleic acid sequences in subdiploid and subtetraploid revertants of polyoma-transformed cells.

Polyoma-transformed cells can revert in the properties characteristic of transformation, although they maintain the polyoma-specific T antigen. Transformed cells contain the same number of copies of polyoma virus deoxyribonucleic acid (DNA) per cell (eight) as revertants with a subdiploid or a subtetraploid chromosome number. The results indicate that the duplication of chromosomes in the subtetraploid revertants did not include the chromosomes that carry the viral genome. The virus DNA in both transformed and revertant cells was associated with high-molecular-weight cell DNA. Reversion of the properties of transformed cells was, therefore, not associated either with a decrease in number of virus DNA copies per cell or with a lack of association of the virus DNA with cell DNA.

Animals↗
PubMed1971

Characterization of the inducer required for the development of macrophage and granulocyte colonies.

A substance produced by various types of cells can induce from single hematopoietic cells the formation of colonies of normal macrophages and granulocytes. This inducer has been purified 600-fold from serum-free conditioned medium from a tissue culture line of mouse cells. It is shown that the inducer is a protein, with a molecular weight of 65-70,000, whose inducing activity was about 1 ng per colony. Acrylamide gel electrophoresis of this material gave four bands, only one of which contained inducing activity. The purified protein was inactive. Activity was regained by the addition of a low molecular weight cofactor that is present in conditioned medium. Under certain conditions, activity was also regained by the addition of adenosine 3':5'-cyclic monophosphate (cyclic AMP).

Animals↗
PubMed1971

A specific metabolic activity on the surface membrane in malignant cell-transformation.

The carbohydrate-binding protein, Concanavalin A (Con A), binds to glucose- or mannose-like sites on the cell-surface membrane. Unless the cells are treated with trypsin, this protein agglutinates malignantly transformed cells, but not normal cells. The transformed cells were agglutinated at 24 degrees C but not at 4 degrees C. Transformed and normal cells treated with trypsin were agglutinated at both 24 degrees C and 4 degrees C with high concentrations of Con A (500 mug/ml), but only at 24 degrees C with low concentrations (5 mug/ml). The same number of Con A molecules were bound to normal and transformed cells at both temperatures. The results indicate that the site for Con A on the surface membrane contains two activities, a component that binds Con A molecules (B) and a component that determines agglutination (A). B is not temperature sensitive and is active in normal and transformed cells, whereas A, which is temperature sensitive, is in an active form only in transformed cells. A can be activated by trypsin, and the increased activity per cell allows agglutination at 4 degrees C with a high, but not with a low, concentration of Con A. Agglutination of transformed cells by wheat-germ agglutinin, which binds to N-acetyl-D-glucosamine-like sites, and by soybean agglutinin, which binds to N-acetyl-D-galactosamine-like sites, was not temperature sensitive. Thus, the temperature-sensitive component A is specific for Con A, and malignant transformation of normal cells, which results in agglutinability by Con A, is associated with the activation of a specific temperature-sensitive activity on the surface membrane.

Agglutination Tests↗
PubMed1970

Specific aggregation of SV40-transformed cells by ornithine, leucine copolymers.

A basic copolymer of ornithine and leucine (1:1) was shown to rapidly agglutinate, in the absence of serum, normal cells and cells transformed by viral and nonviral carcinogens. This agglutination was inhibited by addition of serum. In presence of serum, the same copolymer and those of ornithine and valine (1:1) and arginine and leucine (1:1), produced a specific aggregation of simian virus 40 (SV40)-transformed cells cultured for about 24 hr after addition of the peptide. The rapid agglutination and SV40-specific aggregation could not be inhibited by a variety of individual amino acids or carbohydrates. The specific aggregation could be detected in mixtures of SV40-transformed and other cells, and it was not prevented by x-irradiating the cells with 4000 R. Aggregation of the SV40-transformed cells was inhibited by acidic polyamino acids provided these were added not later than about 5 hr after addition of the basic copolymer. The results indicate that the basic copolymer, in the presence of serum, produces a change in SV40-transformed cells, presumably in the surface membrane, that causes the cells to aggregate. In addition to the aggregation of cells transformed by SV40, cells transformed by adenovirus 12, which did not contain detectable SV40-specific nuclear tumor (T) antigen, were also aggregated by the basic copolymer in the presence of serum. This indicates that the ornithine, leucine copolymer is able to detect an SV40-like change in the surface membrane of cells transformed by adenovirus 12.

Adenoviridae↗