Membrane glycopeptides from subcellular fractions of control and virus-transformed cells.
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Biomedical subjects
Publications and source records attributed to L Warren.
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In this brief review the hypothesis that altered membrane proteins and glycoproteins may be critical mediators of malignant expression is discussed. Examples of alterations of membrane proteins in malignancy are presented. Data is summarized showing changes in the carbohydrate components of glycoproteins of surface and internal membranes of malignant cells in culture as compared to their normal counterparts.
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The pattern of elution from a column of Sephadex G-50 of a fucose-labeled carbohydrate component derived from the surface glycoproteins of transformed cells can be altered to resemble that from untransformed cells by enzymatic removal of the sialic acid. These results indicate that the consistent differences found between control and virus-transformed cells may depend upon a relatively specific sialyl transferase that is found in greater amounts (2.5- to 11-times) in transformed cells than in control cells, and in dividing cells as compared to nondividing cells.
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Glycopeptides were removed by trypsin digestion from the surface of control cells and cells transformed by Rous sarcoma virus, murine sarcoma virus, or polyoma virus. After digestion with pronase, the glycopeptides were analyzed by gel filtration. The elution profiles suggest that there are differences in the glycopeptides from the surface of control cells and those from transformed cells.
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