A trans-Golgi network retention signal YQRL fused to ricin A chain significantly enhances its cytotoxicity

2004 ◽  
Vol 313 (4) ◽  
pp. 1053-1057 ◽  
Author(s):  
Jinbiao Zhan ◽  
Liping Ge ◽  
Jiangen Shen ◽  
Keyi Wang ◽  
Shu Zheng
Keyword(s):  
Ricin A Chain ◽  
Trans Golgi Network ◽  
A Chain ◽  
Golgi Network ◽  
Retention Signal ◽  
Ricin A

scholarly journals Estimation of the amount of internalized ricin that reaches the trans-Golgi network

1988 ◽  
Vol 106 (2) ◽  
pp. 253-267 ◽  
Author(s):  
B van Deurs ◽  
K Sandvig ◽  
OW Petersen ◽  
S Olsnes ◽  
K Simons ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
G Protein ◽  
Golgi Complex ◽  
Endocytic Pathway ◽  
Membrane Glycoproteins ◽  
Double Labeling ◽  
Trans Golgi Network ◽  
A Chain ◽  
Golgi Network ◽  
Ricin A

We have used a protocol for internalization of ricin, a ligand binding to plasma membrane glycoproteins and glycolipids with terminal galactosyl residues, and infection with the vesicular stomatitis virus ts 045 mutant in BHK-21 cells to determine whether internalized plasma membrane molecules tagged by ricin reach distinct compartments of the biosynthetic-exocytic pathway. At 39.5 degrees C newly synthesized G protein of ts 045 was largely prevented from leaving the endoplasmic reticulum. At the same temperature ricin was endocytosed and reached, in addition to endosomes and lysosomes, elements of the Golgi complex. When the temperature was lowered to 19.5 degrees C, no more ricin was delivered to the Golgi complex, but now G protein accumulated in the Golgi stacks and the trans-Golgi network (TGN). Double-labeling immunogold cytochemistry on ultracryosections was used to detect G protein and ricin simultaneously. These data, combined with stereological and biochemical methods, showed that approximately 5% of the total amount of ricin within the cells, corresponding to 6-8 X 10(4) molecules per cell, colocalized with G protein in the Golgi complex after 60 min at 39.5 degrees C. Of this amount approximately 70-80% was present in the TGN. Since most of the ricin molecules remain bound to their binding sites at the low pH prevailing in compartments of the endocytic pathway, the results indicate that a fraction of the internalized plasma membrane molecules with terminal galactose are not recycled directly from endosomes or delivered to lysosomes, but are routed to the Golgi complex. Also, the results presented here, in combination with other recent studies on ricin internalization, suggest that translocation of the toxic ricin A-chain to the cytosol occurs in the TGN.

Addition of an ER retention signal to the ricin A chain increases the cytotoxicity of the holotoxin

1992 ◽  
Vol 203 (1) ◽  
pp. 1-4 ◽  
Author(s):  
R. Wales ◽  
J.A. Chaddock ◽  
L.M. Roberts ◽  
J.M. Lord
Keyword(s):  
Ricin A Chain ◽  
Er Retention ◽  
A Chain ◽  
Er Retention Signal ◽  
Retention Signal ◽  
Ricin A

scholarly journals Free Energy Determinants of Binding the rRNA Substrate and Small Ligands to Ricin A-Chain

1999 ◽  
Vol 76 (1) ◽  
pp. 28-39 ◽  
Author(s):  
Mark A. Olson ◽  
Lilee Cuff
Keyword(s):  
Free Energy ◽  
Ricin A Chain ◽  
A Chain ◽  
Ricin A ◽  
Small Ligands

scholarly journals Characterization of the increased cytotoxicity of gelonin anti-T cell immunoconjugates compared with ricin A chain immunoconjugates

2008 ◽  
Vol 97 (1) ◽  
pp. 10-18 ◽  
Author(s):  
D. M. FISHWILD ◽  
H.-M. WU ◽  
S. F. CARROLL ◽  
S. L. BERNHARD
Keyword(s):  
T Cell ◽  
Ricin A Chain ◽  
A Chain ◽  
Ricin A

Toxicity of ligand and antibody-directed ricin A-chain conjugates recognizing the epidermal growth factor receptor

1987 ◽  
Vol 131 (3) ◽  
pp. 418-425 ◽  
Author(s):  
Angelika M. Vollmar ◽  
Deborah E. Banker ◽  
John Mendelsohn ◽  
Harvey R. Herschman
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Ricin A Chain ◽  
Epidermal Growth ◽  
A Chain ◽  
Ricin A
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