CELL-SURFACE AND INTRACELLULAR FUNCTIONS FOR GALACTOSE BINDING IN RICIN CYTOTOXICITY
CELL-SURFACE AND INTRACELLULAR FUNCTIONS FOR GALACTOSE BINDING IN RICIN CYTOTOXICITY
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DOI:
10.1042/bst0200734
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发表时间:
1992-11-01
影响因子:
3.9
通讯作者:
ROBERTS, LM
中科院分区:
文献类型:
--
作者:
LORD, JM;WALES, R;ROBERTS, LM
Ricin is a heterodimeric plant protein which is potently cytotoxic to mammalian cells. Both polypeptide subunits of ricin have distinct roles in the intoxication process [11. The A subunit (RTA) is a ribosomal RNA N-glycosidase which, having entered the target cell cytosol, specifically removes an adenine residue from 28s rRNA (A4324 in the case of rat liver 28s rRNA)[2, 31. This particular adenine residue, which is present in a highly conserved, surface-exposed loop in 28s rRNA, has a crucial role in the binding of elongation factors during translation. Ribosomes containing depurinated 28s RNA are no longer capable of protein synthesis. The ricin B subunit (RTB) is a lectin which has two galactose binding sites. Interaction between these sites and galactosides present on plasma membrane glycoproteins or glycolipids bind the holotoxin to the surface of target cells [11. After endocytic uptake of surface-bound toxin, the B subunit is believed to have a further function in