Nerve Growth Factor Signaling Pathway

1. Nerve Growth Factor Signaling Pathway Nerve growth factor (NGF) is one of the most important biologically active molecules in the nervous system. It plays an important role and has clinical significance in regulating the growth, development, differentiation, survival of nerve cells and the regeneration and repair of injured nerves. Current basic research indicates that NGF can be applied to neurotoxicity, peripheral nerve injury, diabetic peripheral neuropathy, senile dementia, Parkinson's disease, facial neuritis, and nerve damage (including spinal cord injury, high paraplegia, finger replantation, and neurological diseases). Brain damage and other peripheral nervous system damages are the only neurological protein factors currently available for clinical use. NGF has been in the historical process of early discovery to medical applications for more than half a century. Human nerve growth factor (hNGF) is a biologically active factor found in the human body that has a trophic effect on normal nerve cells and regulates the function of damaged nerve repair. It can maintain the survival of sympathetic and sensory nerves and promote nerve cells. The differentiation determines the direction of axon stretching and plays a decisive role in promoting brain development, nervous system growth, damage nerve regeneration and functional recovery. Nerve growth factor family NGF is synthesized as precursor in vivo, including signal peptides, leader peptides, and mature peptides. The signal peptide contributes to protein secretion. Two conserved regions in the leader peptide are required for NGF expression, enzymatic hydrolysis to form biologically active proteins, and secretion of mature NGF. It has now been found that leader peptides also contribute to the correct folding of proteins, and such leader peptides are known as molecular chaperones (IMCs). Therefore, it is considered that the leader peptide may play an intramolecular molecular chaperone role in the folding process of NGF. ProNGF contains a potential N-glycosylation site, and studies by Seidah et al. have shown that the propeptide portion of the NGF precursor can be N-glycosylated, and the glycosylation of proNGF helps to secrete the endoplasmic reticulum. ProNGF undergoes post-translational modifications at the N-terminus and C-terminus to form biologically active mature NGF. https://www.creative-diagnostics.com/nerve-growth-factor-signaling-pathway.htm