Analysis of the trk NGF receptor tyrosine kinase using recombinant fusion proteins

C. M. Horvath*, A. Wolven, D. Machadeo, J. Huber, L. Boter, M. Benedetti, B. Hempstead, M. V. Chao

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Nerve growth factor (NGF) represents a family of structurally related trophic factors, including brain-derived neurotrophin factor (BDNF), neurotrophin-3 (NT-3), NT-4, and NT-5. These neurotrophin factors interact with two classes of receptors, the trk receptor tyrosine kinase family, and the low affinity p75 neurotrophin receptor. To study potential ligand-receptor interactions, recombinant trk fusion proteins have been constructed, and pan-trk polyclonal antisera directed against the cytoplasmic tyrosine kinase domain have been generated. The recombinant proteins were assessed for in vitro kinase activity and for the ability of K-252a to inhibit phosphorylation. Antibodies made against the fusion protein recognize all trk family members, and are effective in immunoprecipitation of affinity-crosslinked receptors. Comparative crosslinking indicates that NGF can recognize all trk receptor members, illustrating the large number of potential ligand-receptor interactions between neurotrophins and their receptors.

Original languageEnglish (US)
Pages (from-to)223-228
Number of pages6
JournalJournal of cell science
Volume106
Issue numberSUPPL. 17
DOIs
StatePublished - 1993

Keywords

  • NGF
  • Recombinant fusion protein
  • Tyrosine kinase
  • trk receptor

ASJC Scopus subject areas

  • Cell Biology

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