Nerve growth factor signal transduction in mature pig oligodendrocytes

Autor: Hempel R, Tyede Schmidt-Schultz, Kruska L, Rolf Heumann, Engel J, Sabine Klöppner, H. H. Althaus
Rok vydání: 1998
Předmět:
animal structures
Swine
Carbazoles
Protein Tyrosine Phosphatase
Non-Receptor Type 11
Receptors
Nerve Growth Factor
Biology
Tropomyosin receptor kinase A
Receptor
Nerve Growth Factor
Indole Alkaloids
Cellular and Molecular Neuroscience
Glycogen Synthase Kinase 3
Proto-Oncogene Proteins
Low-affinity nerve growth factor receptor
Animals
Nerve Growth Factors
Phosphorylation
Receptor
trkA
Cells
Cultured
Protein Kinase C
Protein Tyrosine Phosphatase
Non-Receptor Type 6
Autophosphorylation
Intracellular Signaling Peptides and Proteins
Signal transducing adaptor protein
Brain
Receptor Protein-Tyrosine Kinases
Protein-Tyrosine Kinases
Cell biology
Up-Regulation
Isoenzymes
Oligodendroglia
Nerve growth factor
nervous system
Biochemistry
Calcium-Calmodulin-Dependent Protein Kinases
biology.protein
Calcium
Signal transduction
Protein Tyrosine Phosphatases
Tyrosine kinase
Proto-Oncogene Proteins c-fos
Neurotrophin
Signal Transduction
Zdroj: Journal of neuroscience research. 50(5)
ISSN: 0360-4012
Popis: It has previously been shown that nerve growth factor (NGF) is of functional significance for mature pig oligodendrocytes (OLs) in culture. The present data give evidence for the expression of TrkA, the so-called high-affinity NGF receptor, and of p75NTR, the so-called low-affinity NGF receptor. TrkA is upregulated during culturing, in contrast to the p75 receptor. Exposure of OLs to NGF induces an autophosphorylation of TrkA via its intrinsic tyrosine kinase. K-252a inhibits the TrkA autophosphorylation, which reduces the OL process formation to control levels. To the tyrosine-phosphorylated sites of TrkA several proteins, such as phospholipase C-gamma1, the adaptor protein SHC, the phosphotyrosine phosphatase SH-PTP2 (SYP) associate via their SH2 phosphotase SH-PTP2 domain. The association of SHC to TrkA is shown by co-immunoprecipitation. Indirect evidence for a possible activation of PLC-gamma1 is given by an NGF-induced increase of oligodendroglial [Ca2+]i. Downstream from TrkA, a mitogen-activated protein kinase cascade, which includes Erk1 and Erk2, is operating. An in-gel myelin basic protein kinase assay revealed that NGF activates predominantly Erk1. Finally, it is shown that NGF stimulates expression of c-fos.
Databáze: OpenAIRE
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