Contact-dependent transfer of a lysosomal enzyme from lymphocytes to fibroblasts.
In this study we have examined the mechanism underlying the contact-mediated transfer of a lysosomal enzyme from lymphocytes to fibroblasts in culture. We found that although antibody against the mannose 6-phosphate lysosomal targetting receptor (MPR) completely inhibited fibroblast uptake of the lysosomal enzyme beta-glucuronidase (Gus) from the culture medium, it had no effect on the transfer of the enzyme from normal lymphocytes. In contrast, the presence of antibody that prevented the adhesion of the lymphocytes to the fibroblasts inhibited Gus acquisition but had no effect on endocytosis. Immunogold electron microscopy of the contact site between the two types of cell showed that the transfer of Gus involved uncoated vesicles localized near the cell surface of the fibroblast at sites of contact with the lymphocytes. The acquired lymphocyte enzyme was shown to be transported to the fibroblast lysosomes.
Bou-Gharios
G
G
Cell Enzymology Unit, Kennedy Institute of Rheumatology, London, UK.
Moss
J
J
Partridge
T
T
Abraham
D
D
Olsen
I
I
D000818:Animals; D001693:Biological Transport, Active; D002448:Cell Adhesion; D002450:Cell Communication; D002478:Cells, Cultured; D005347:Fibroblasts / Q000166:cytology / Q000201:enzymology*; D005966:Glucuronidase / Q000378:metabolism; D006801:Humans; D008214:Lymphocytes / Q000166:cytology / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D008854:Microscopy, Electron
D005966:Glucuronidase