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

scholarly journals The isolation and characterization of temperature-dependent ricin A chain molecules inSaccharomyces cerevisiae

FEBS Journal ◽  
2007 ◽  
Vol 274 (21) ◽  
pp. 5586-5599 ◽  
Author(s):  
Stuart C. H. Allen ◽  
Katherine A. H. Moore ◽  
Catherine J. Marsden ◽  
Vilmos Fülöp ◽  
Kevin G. Moffat ◽  
...  
Keyword(s):  
Temperature Dependent ◽  
Ricin A Chain ◽  
Chain Molecules ◽  
Isolation And Characterization ◽  
A Chain ◽  
Ricin A

scholarly journals Optimal elimination of leukemic T cells from human bone marrow with T101-ricin A-chain immunotoxin

Blood ◽  
1985 ◽  
Vol 65 (2) ◽  
pp. 289-297 ◽  
Author(s):  
P Casellas ◽  
X Canat ◽  
AA Fauser ◽  
O Gros ◽  
G Laurent ◽  
...  
Keyword(s):  
Bone Marrow ◽  
T Cells ◽  
T Cell ◽  
Autologous Transplantation ◽  
Leukemic Cells ◽  
Ricin A Chain ◽  
Hematopoietic Stem ◽  
Human T Cell ◽  
A Chain ◽  
Ricin A

Abstract In view of bone marrow purging before autologous transplantation in T cell malignancies, an anti-human T cell immunotoxin (IT) has been prepared by coupling ricin A-chain to the monoclonal antibody T101 that binds the T1 differentiation antigen expressed by T lymphocytes as well as by T cell-derived hematologic malignancies. Using a sensitive and reliable clonogenic assay, optimal conditions were defined for the elimination of clonogenic human T leukemic cells among bone marrow cells. Maximal cytoreduction was obtained with IT at a dose of 2 micrograms/mL in the presence of 10 mmol/L NH4Cl. This treatment led to the reduction of more than six orders of magnitude of T101-positive clonogenic leukemic cells, with no harm to T101-negative cells. Moreover, we observed no toxicity of IT to human hematopoietic stem cells (CFU-GEMMT) derived from bone marrow of healthy volunteers. Thus, pretreatment of bone marrow samples with IT plus NH4Cl offers a safe, simple, reliable, and highly efficient means to eliminate undesirable leukemic T cells from the graft.

RATIONALE FOR THE SELECTION OF RICIN A-CHAIN ANTI-T IMMUNOTOXINS FOR MATURE T CELL DEPLETION

1987 ◽  
Vol 44 (6) ◽  
pp. 763-769 ◽  
Author(s):  
JEAN-MARIE DEROCQ ◽  
GUY LAURENT ◽  
PIERRE CASELLAS ◽  
HUBERT VIDAL ◽  
P. PONCELET ◽  
...  
Keyword(s):  
T Cell ◽  
Cell Depletion ◽  
Ricin A Chain ◽  
T Cell Depletion ◽  
A Chain ◽  
Ricin A ◽  
Selection Of

scholarly journals Identification of ricin A-chain HLA class II-restricted epitopes by human T-cell clones

2001 ◽  
Vol 125 (3) ◽  
pp. 391-400 ◽  
Author(s):  
M. Tommasi ◽  
D. Castelletti ◽  
M. Pasti ◽  
G. Fracasso ◽  
I. Lorenzetti ◽  
...  
Keyword(s):  
T Cell ◽  
Class Ii ◽  
Hla Class Ii ◽  
Ricin A Chain ◽  
T Cell Clones ◽  
Human T Cell ◽  
Cell Clones ◽  
A Chain ◽  
Ricin A

scholarly journals Adult T cell leukemia: a potential target for ricin A chain immunotoxins

Blood ◽  
1985 ◽  
Vol 65 (6) ◽  
pp. 1416-1421 ◽  
Author(s):  
M Kronke ◽  
JM Depper ◽  
WJ Leonard ◽  
ES Vitetta ◽  
TA Waldmann ◽  
...  
Keyword(s):  
T Cells ◽  
Protein Synthesis ◽  
T Cell ◽  
T Cell Leukemia ◽  
Cell Leukemia ◽  
Maximal Inhibition ◽  
Ricin A Chain ◽  
Adult T Cell Leukemia ◽  
A Chain ◽  
Ricin A

Abstract Adult T cell leukemia (ATL) is an almost uniformly fatal malignancy of mature T cells associated with human T cell leukemia/lymphoma virus type 1 (HTLV-1) infection. Cells from this leukemia are characterized by the expression of large numbers of receptors for interleukin 2 (IL- 2). In an attempt to prepare an immunotoxin with selective cytotoxicity for ATL cells, we conjugated anti-Tac, a monoclonal anti-IL-2 receptor antibody, to purified ricin A chains. Although unmodified anti-Tac had no effect on the protein synthesis of these cells, anti-Tac-ricin A chain conjugates produced half-maximal inhibition of protein synthesis in HTLV-1-infected leukemic T cell lines at concentrations of 2 to 6 X 10(-10) mol/L (ID50). An essentially identical ID50 was obtained with leukemic peripheral blood T lymphocytes isolated from two patients with ATL. In contrast, half-maximal inhibition of protein synthesis in HTLV- uninfected, IL-2 receptor-negative T and B cell lines required 200- to 1,000-fold higher concentrations of anti-Tac-ricin A chain conjugates. Both unconjugated anti-Tac and immunoaffinity-purified IL-2 completely inhibited the toxic effects of anti-Tac-ricin A, confirming the specificity of the conjugate-IL-2 receptor interaction. Clonogenic assays demonstrated that anti-Tac-ricin A chain was able to eliminate greater than 99.9% of an HTLV-1-infected T cell population at concentrations only marginally affecting IL-2 receptor-negative cells. The data presented demonstrate that anti-Tac-ricin A is selectively cytotoxic for HTLV-1-infected leukemic T cells in vitro and raises the future possibility of specific therapeutic intervention with immunotoxins in this disease.

Application of Sodium Dodecyl Sulfate-Capillary Gel Electrophoresis to the Characterization of Ricin A-Chain Immunotoxins

2012 ◽  
Vol 75 (11-12) ◽  
pp. 679-683 ◽  
Author(s):  
Dong Hee Na ◽  
Eun Ji Park ◽  
Myung Sun Kim ◽  
Hye Suk Lee ◽  
Kang Choon Lee
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Ricin A Chain ◽  
Capillary Gel Electrophoresis ◽  
Dodecyl Sulfate ◽  
A Chain ◽  
Ricin A
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