PMID: 8958964Oct 31, 1996Paper

Evidence for multiple sites of interaction between IL-12 and its receptor

Annals of the New York Academy of Sciences
D H PreskyM K Gately

Abstract

We have previously described the identification of a protein, now designated IL-12R beta 1, that binds 125I-huIL-12 with a Kd of about 10 nM, corresponding to the low affinity 125I-huIL-12 binding sites seen on PHA-activated human lymphoblasts. Using expression cloning techniques, we have recently identified an additional IL-12-binding protein subunit, IL-12R beta 2, which binds 125I-huIL-12 with a Kd of about 5 nM when expressed alone in COS-7 cells. Coexpression of IL-12R beta 1 and IL-12R beta 2 in COS-7 cells results in formation of two classes of 125 I-huIL-12-binding sites with Kds of about 50 pM and 5 nM. Mouse IL-12 p40 subunit homodimer (mo(p40)2) blocked 125I-huIL-12 binding to human IL-12R beta 1, but did not inhibit binding to human IL-12R beta 2. In contrast, anti-huIL-12 monoclonal antibody 20C2, which does not block 125I-huIL-12 binding to human IL-12R beta 1, completely blocked binding to human IL-12R beta 2. These results demonstrate that two classes of IL-12 inhibitors, one that primarily blocks IL-12/IL-12R beta 1 interaction (e.g., mo(p40)2), and one that primarily blocks IL-12/IL-12R beta 2 interaction (e.g., 20C2), can be identified.

References

Jan 1, 1995·European Journal of Immunology·S GillessenM K Gately
Sep 1, 1993·European Journal of Immunology·F MattnerT Germann

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Citations

Jan 5, 2002·Veterinary Immunology and Immunopathology·Ann Marie WhiteCynthia L Baldwin
Apr 17, 2003·Trends in Immunology·Frank BrombacherGottfried Alber
Jan 11, 2002·Science's STKE : Signal Transduction Knowledge Environment·David M Frucht
Aug 30, 2001·International Immunology·I ShiratoriT Seya
Oct 23, 2008·The Journal of Immunology : Official Journal of the American Association of Immunologists·Ce TangYasunobu Yoshikai

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