Selection and characterization of monoclonal antibodies to the idiotype-like structure of an interleukin-2-producing human leukemia t-cell line

1985 ◽  
Vol 36 (2) ◽  
pp. 253-259 ◽  
Author(s):  
Alessandro Moretta ◽  
Giuseppe Pantaleo ◽  
Miguel Lopez-Botet ◽  
Lorenzo Moretta
1980 ◽  
Vol 152 (6) ◽  
pp. 1709-1719 ◽  
Author(s):  
S Gillis ◽  
J Watson

To isolate a stable tumor cell line capable of producing human interleukin 2 (IL-2; formerly referred to as T cell growth factor), 16 human T and B leukemia cell lines were screened for constitutive and mitogen-stimulated IL-2 production. We found that the T cell leukemia line designated Jurkat-FHCRC produced > 200 U/ml of IL-2 activity after a 24-h stimulation with T cell mitogens. Peak mitogen-induced IL-2 activity was found in supernates harvested from 24-h Jurkat-FHCRC cell cultures stimulated with either 1% phytohemagglutinin or 20 microgram/ml concanavalin A. Addition of the fatty acid derivative phorbol myristate acetate to mitogen-stimulated cultures increased Jurkat-FHCRC IL-2 production to concentrations > 400 U/ml. IL-2 activity observed in such cases represented between 100--300 times that produced in conventional cultures of mitogen- or alloantigen-stimulated normal human peripheral blood or splenic lymphocytes. Jurkat-FHCRC-derived conditioned medium demonstrated equal capacity to promote the sustained in vitro proliferation of either murine or human activated T cell lines confirming the ability of Jurkat-FHCRC cells to produce human IL-2. These studies identify a new source of human IL-2 and establish a valuable reagent for the isolation and further molecular characterization of this immunoregulatory molecule.


1992 ◽  
Vol 144 (2) ◽  
pp. 367-381 ◽  
Author(s):  
Richard G. Cook ◽  
Barbara Leone ◽  
Joseph W. Leone ◽  
Suzanne M. Widacki ◽  
Peter J. Zavell
Keyword(s):  

1992 ◽  
Vol 7 (1-2) ◽  
pp. 157-164 ◽  
Author(s):  
Toshio Kakihara ◽  
Toshiyuki Yamada ◽  
Takeaki Fukuda ◽  
Yoshihisa Ohnishi ◽  
Kenji Kishi ◽  
...  

1989 ◽  
Vol 489 (1) ◽  
pp. 120-128 ◽  
Author(s):  
Hans-Peter Hartung ◽  
Ba¨rbel Scha¨fer ◽  
Tibor Diamanststein ◽  
Walter Fierz ◽  
Kurt Heininger ◽  
...  

1999 ◽  
Vol 112 (4) ◽  
pp. 491-502
Author(s):  
M. Mirabet ◽  
C. Herrera ◽  
O.J. Cordero ◽  
J. Mallol ◽  
C. Lluis ◽  
...  

Extracellular adenosine has a key role in the development and function of the cells of the immune system. Many of the adenosine actions seem to be mediated by specific surface receptors positively coupled to adenylate cyclase: A2A and A2B. Despite the fact that A2A receptors (A2ARs) can be easily studied due to the availability of the specific agonist CGS21680, a pharmacological and physiological characterization of adenosine A2B receptors (A2BRs) in lymphocytes has not been possible due to the lack of suitable reagents. Here we report the generation and characterization of a polyclonal antipeptide antibody raised against the third extracellular loop of the A2BR human clone which is useful for immunocytochemical studies. This antibody has permitted the detection of A2BR+ cells in lymphocyte samples isolated from human peripheral blood. The pharmacology of cAMP-producing compounds is consistent with the presence of functional A2BRs but not of A2A receptors in these human cells. The percentage of A2BR-expressing cells was similar in the CD4(+) or CD8(+) T cell subpopulations. Interestingly activation signals delivered by either phytohemagglutinin or anti-T cell receptor/CD3 complex antibodies led to a significant increase in both the percentage of cells expressing the receptor and the intensity of the labeling. These receptors are functional since interleukin-2 production in these cells is reduced by NECA but not by R-PIA or CGS21680. These results show that A2BR expression is regulated in T cell activation and suggest that the role of adenosine in lymphocyte deactivation is mediated by A2BRs.


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