Disulfide Bond Formation Between Nerve Growth Factor and the Nerve Growth Factor Receptor from Embryonic Sensory Neurons

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Abstract
Recent studies with sympathetic neurons using radiolabeled nerve growth factor have indicated that a high-molecular-weight covalent complex is formed. This complex is between the nerve growth factor and the high-affinity (Type I) receptor and occurs through the formation of a disulfide bond. Studies presented in the present article demonstrate a similar complex is formed on chicken embryonic sensory neurons. The formation of this complex is inhibited by the addition of unlabeled nerve growth factor, metabolic energy inhibitors (dinitrophenol and NaF), and of sulfhydryl reagents. On the other hand, formation of this complex is not inhibited by temperature, or by the addition of insulin or epidermal growth factor. The receptor involved in the covalent complex formation is the high-affinity (type I) receptor. The molecular weight of this complex is approximately 232,000 daltons. Evidence indicates that this covalent complex may be required for the biological activity of the nerve factor.