Overview
- Peptide CEEIPGRWITRSTPPE corresponding to amino acid residues 188-203 of human p75NTR (Accession P08138). Extracellular, stalk domain.
- Rat DRG sections.
- Rat pheochromocytoma PC12 cells (1:20).
- Cell surface detection of p75NTR in live intact rat pheochromocytoma (PC12) cells:___ Unstained cells.
___ Cells + Anti-p75 NGF Receptor (extracellular)-ATTO Fluor-488 Antibody (#ANT-007-AG), (1:20).
- Human A875 melanoma cells (1:50).
- Expression of p75NTR in human A875 melanoma cellsCell surface detection of p75NTR in live intact human A875 melanoma cells. A. Cells were stained with Anti-p75 NGF Receptor (extracellular)-ATTO Fluor-488 Antibody (#ANT-007-AG), (1:50), (green). B. Live image of the cells. C. Merge of the two images.
The p75 neurotrophin receptor (p75NTR) is a member of the tumor necrosis factor (TNF) receptor superfamily. Like all members of this superfamily, p75NTR is a type I transmembrane protein with tandem cysteine-rich domains in its extracellular portion, as well as an intracellular death domain. p75NTR binds to its ligands as a homodimer but can also form heterodimers with other receptors such as TrkA, TrkB, TrkC, Nogo receptor, and sortilin. The precise multimeric receptor complex formed between p75NTR and the other receptors determine the ligand being recognized (see below) and the biological response to its binding1-3.
As its name implies, p75NTR binds to all the neurotrophins (NTR) (NGF, BDNF, NT-3, and NT-4) with similar nanomolar affinities. Co-expression of p75NTR with the Trk receptors enhances its ability to bind and respond to the specific neurotrophin and induces cell survival. On the other hand, it has recently been demonstrated that p75NTR binds with high affinity to the unprocessed form of NGF (proNGF), probably as a complex with sortilin, leading to cell death by apoptosis1-3. Finally, a multimeric complex of p75NTR and Nogo receptor binds to myelin proteins such as Nogo-66, MAG, and OmgP, resulting in inhibition of axonal growth4.