1. Identification of rabbit and mouse β-glucuronidases in human fibroblasts following direct interaction with lymphocytes
- Author
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M. F. Dean, I. Olsen, and H. Muir
- Subjects
Cell signaling ,Hot Temperature ,Cell ,Mice, Inbred Strains ,Cell Communication ,Biology ,Mice ,Species Specificity ,Cell–cell interaction ,medicine ,Animals ,Humans ,Lymphocytes ,Fibroblast ,Molecular Biology ,Cells, Cultured ,Glucuronidase ,chemistry.chemical_classification ,Cell Biology ,Receptor-mediated endocytosis ,Fibroblasts ,Donor Lymphocytes ,Molecular biology ,Enzyme assay ,Enzyme ,medicine.anatomical_structure ,chemistry ,biology.protein ,Rabbits - Abstract
Human fibroblasts totally deficient in beta-glucuronidase acquired high levels of enzyme activity when co-cultured with mouse or rabbit lymphocytes. Direct cell-to-cell contact was obligatory for this process. The enzyme acquired by the fibroblasts was shown to be identical to beta-glucuronidase from donor lymphocytes by its position of elution from DEAE-cellulose, thermal stability, mobility on polyacrylamide gels and by its antigenic determinants. The enzyme extracted from deficient fibroblasts after co-culture with lymphocytes showed no evidence of any hybridisation between human and mouse or rabbit sub-units. It is concluded that during direct cell interaction, enzymically active beta-glucuronidase is transferred directly from donor lymphocytes to deficient fibroblasts by a mechanism, previously shown not to involve normal receptor mediated endocytosis.
- Published
- 1982
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