Related Experiment Video
Updated: Aug 11, 2026

Protocol for Culturing Sympathetic Neurons from Rat Superior Cervical Ganglia (SCG)
Published on: January 30, 2009
Protein tyrosine phosphatase activation during nerve growth factor-induced neuronal differentiation of PC12 cells
L F Aparicio1, I Ocrant, J M Boylan
1Division of Pediatric Endocrinology and Metabolism, Rhode Island Hospital, Providence 02903.
Abstract:
We have studied the role of protein tyrosine phosphatases (PTPases) during neuronal differentiation of PC12 cells. Nerve growth factor (NGF), a well-characterized differentiating agent for these cells, led to a decrease in DNA synthesis within 24 h. This was accompanied by a 2- to 3-fold increase in the activity of PTPases, measured as the dephosphorylation of polyacidic or polybasic substrates phosphorylated on tyrosine. PTPase activation was independent of cell density and proportional to NGF concentration, with a half-maximal effect occurring at 0.35 nM. High-performance liquid chromatography size exclusion chromatography revealed that PTPases with molecular masses of 550, 300, and 60 kilodaltons were activated in response to NGF. Additional studies showed that the presence of NGF made PC12 cells refractory to the mitogenic effect of epidermal growth factor. Our data indicate that NGF-induced neuronal differentiation and growth arrest in PC12 cells are associated with activation of several PTPases. We speculate that PTPase activation in response to NGF may inhibit the mitogenic actions of other growth factors.
Related Concept Videos
Enzyme-linked Receptors
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Amplifying Signals via Enzymatic Cascade
Receptor Tyrosine Kinases
PI3K/mTOR/AKT Signaling Pathway
TGF - β Signaling Pathway
Activation and Inactivation of G Proteins

