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GDNF is a homodimeric neurotrophic factor connected by disulfide bonds, sharing structural similarities with Artemin, Neurturin, and Persephin. These proteins are part of the cysteine-knot superfamily of growth factors, known for their stable dimeric structures. GDNF transmits signals through a complex receptor system involving RET and one of four GFRα receptors (α1-α4). Its specific actions include enhancing dopamine uptake and promoting the survival and morphological development of midbrain neurons.
In a mouse model of Parkinson’s disease, GDNF has demonstrated efficacy in improving symptoms such as bradykinesia, rigidity, and postural instability. The functional form of Human GDNF is a disulfide-linked homodimer composed of two 15 kDa polypeptide chains referred to as monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, essential for inter-chain disulfide bridging, and others that contribute to the cysteine-knot configuration, forming an intramolecular ring. The molecular weight of Recombinant Human GDNF is calculated to be 30.4 kDa.
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