Abstract
The high-affinity nerve growth factor receptor corresponds to the tyrosine protein kinase encoded by the proto-oncogene trkA. Different findings suggest that nerve growth factor (NGF) can be operative in the growth modulation of tumor cell lines possessing high-affinity binding sites for this molecule. Using as immunizing material the SKNBE neuroblastoma cell line transfected with proto-trkA we produced a monoclonal antibody (MAb) able to recognize the high-affinity nerve growth factor receptor. The selected MAb, designated MGR12, is directed against an epitope present on the extracellular domain of the receptor since it showed reactivity on living trkA-expressing cells and was able to immunoprecipitate the proto-trkA molecule. The MGR12 MAb is directed against a non-functional epitope since it neither inhibited NGF binding nor induced receptor internalization. This new reagent appears to be an appropriate tool for analyzing the expression of high-affinity nerve growth factor receptor in tumors of different origin and for elucidating its involvement in tumor progression.
Original language | English |
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Pages (from-to) | 68-72 |
Number of pages | 5 |
Journal | International Journal of Biological Markers |
Volume | 14 |
Issue number | 2 |
Publication status | Published - Apr 1999 |
Keywords
- High-affinity nerve growth factor receptor
- Monoclonal antibody
- Somatic fusion
ASJC Scopus subject areas
- Immunology
- Biochemistry