Abstract:
:Ricin is internalized after binding at the cell surface via lectin activity of the B-chain recognizing terminal galactose residues. Ricin-A chain is then translocated to the cytosol from various endocytic structures. Cell death is the result of catalytic inactivation of protein synthesis. Using (125)I-ricin overlays, we examined the distribution of ricin binding-proteins within highly purified preparations of plasma membrane vesicles, endosomes and lysosomes from lymphocytes. All compartments of the endocytic pathway had distinct profiles; some ricin-binding proteins were present throughout the pathway; others were restricted to the plasma membrane and endosomes. The major endosomal protein recognized by (125)I-ricin, a 166 kDa glycoprotein, was endosome-specific. When endosomal proteins were solubilized before chromatography onto ricin-agarose this protein was also by far the major specifically-bound glycoprotein. This 166 kDa glycoprotein might be involved in ricin translocation from this compartment.
journal_name
Cell Biol Intjournal_title
Cell biology internationalauthors
Alami M,Taupiac MP,Beaumelle Bdoi
10.1006/cbir.1996.0120subject
Has Abstractpub_date
1997-03-01 00:00:00pages
145-50issue
3eissn
1065-6995issn
1095-8355pii
S1065-6995(96)90120-1journal_volume
21pub_type
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