Overview
- Bouzas-Rodriguez, J. et al. (2010) J. Clin. Invest. 120, 850.
- Palazzo, E. et al. (2012) J. Cell. Physiol. 227, 1017.
- Ramos, B. et al. (2009) Mol. Cell. Neurosci. 42, 152.
Alomone Labs Human TrkC-Fc Chimera inhibits NT-3-induced ERK1/2 MAPK phosphorylation in TrkB stably expressed in HEK293 cells.TrkB-stably transfected HEK293 cells were serum deprived for 2 hr and then stimulated for 10 min with 30 ng/ml Recombinant human Neurotrophin (NT-3) protein (#N-260) (lane 2) or 0.5 µg/ml Human TrkC-Fc Chimera (#RPC-004) preincubated with 30 ng/ml Recombinant human Neurotrophin (NT-30 protein for 90 min (lane 3). Control cells incubated without human NT-3 are shown in lane 1. Cell proteins were resolved by SDS-PAGE and detected with anti-phospho-ERK1/2.
TrkC-Fc chimera is a recombinant protein, a soluble fusion of the TrKC receptor which comprises the extracellular domains of the human TrkC fused to the IgG heavy chain. TrkC-Fc has the binding specificity and affinity of TrkC receptor that can block the biological activity of neurotrophin-31.
The neurotrophin family includes four members- nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4). These are encoded by NGF, BDNF, NTF3, and NTF4 human genes, respectively2.
Neurotrophins activate in part Trk family receptor protein-Tropomyosin related kinases. The Trk family includes three members: TrkA, TrkB, and TrkC, encoded by NTRK1, NTRK2, and NTRK3 human genes, respectively. TrkC has the highest affinity for NT-32.
The Trk structure includes a cytoplasmic domain containing several sites of tyrosine phosphorylation which are responsible for activating intracellular signaling cascades. The extracellular domain consists of a cysteine-rich cluster followed by three leucine-rich repeats, another cysteine-rich cluster and two immunoglobulin-like domains3,4.
