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pubmed:abstractText |
Evidence is presented suggesting the presence of galactosyl transferases and galactosyl acceptors on the outer surfaces of intact Balb/c 3T3 cells. In addition, the data indicate that these transferases may only be capable of transferring galactose from uridine diphosphate galactose to galactosyl acceptors on adjacent cells after intercellular contact is made (trans-glycosylation). Intact Balb/c 3T12 cells, by contrast, show no requirement for intercellular contact in order to carry out this reaction suggesting that these cells, which do not exhibit contact inhibition of growth, may be able to transfer galactose to acceptors situated on the same cell as the enzyme (cis-glycosylation). Electrophoretic and radioautographic assays were used to detect surface transferase activities in these two cell lines. Results of experiments on cells from sparse and dense cultures, and under conditions where intercellular contact was regulated, are consistent with the above hypothesis.
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