Characteristics of partially purified nerve growth factor receptor

R. W. Stach, C. R. Lyons, J. R. Perez-Polo

    Research output: Contribution to journalArticle

    9 Citations (Scopus)

    Abstract

    Receptors for the nerve growth factor protein (NGF) have been isolated from three cell types [embryonic chicken sensory neurons (dorsal root sensory ganglia; DRG), rat pheochromocytoma (PC12) and human neuroblastoma (LAN-1) cells] and have been shown to be similar with respect to equilibrium dissociation constant. The present results demonstrate that there are multiple molecular weight species for NGF receptors from DRG neurons and PC12 cells. NGF receptors can be isolated from DRG as four different molecular species of 228, 187, 125, and 112 kilodaltons, and PC12 cells as three molecular species of 203, 118, and 107 kilodaltons. The NGF receptors isolated from DRG show different pH-binding profiles for high- and low-affinity binding. High-affinity binding displays a bell-shaped pH profile with maximum binding between pH 7.0 and 7.9, whereas low-affinity binding is constant between pH 5.0 and 9.1, with a twofold greater binding at pH 3.6. At 22°C, the association rate constant was found to be 9.5 ± 1.0 x 106 M-1 s-1. Two dissociation rate constants were observed. The fast dissociating receptor has a dissociation rate constant of 3.0 ± 1.5 x 10-2s-1, whereas the slow dissociating receptor constant was 2.4 ± 1.0 x 10-4 s-1. The slow equilibrium dissociation constants calculated from the ratio of dissociation to association rate constants are 2.5 x 10-11 M for the high-affinity receptor (type I) and 3.2 x 10-9 M for the low-affinity receptor (type II). These values are the same as those determined by equilibrium experiments on the isolated receptors. The data are consistent with the hypothesis that there are at least two different receptors for NGF.

    Original languageEnglish (US)
    Pages (from-to)1280-1285
    Number of pages6
    JournalJournal of Neurochemistry
    Volume49
    Issue number4
    StatePublished - 1987

    Fingerprint

    Nerve Growth Factor Receptors
    Nerve Growth Factor Receptor
    Diagnosis-Related Groups
    Rate constants
    Nerve Growth Factor
    PC12 Cells
    Proteins
    Neurons
    Local Area Networks
    Association reactions
    Sensory Ganglia
    Spinal Ganglia
    Pheochromocytoma
    Sensory Receptor Cells
    Neuroblastoma
    Local area networks
    Rats
    Chickens
    Molecular Weight
    Molecular weight

    ASJC Scopus subject areas

    • Biochemistry
    • Cellular and Molecular Neuroscience

    Cite this

    Stach, R. W., Lyons, C. R., & Perez-Polo, J. R. (1987). Characteristics of partially purified nerve growth factor receptor. Journal of Neurochemistry, 49(4), 1280-1285.

    Characteristics of partially purified nerve growth factor receptor. / Stach, R. W.; Lyons, C. R.; Perez-Polo, J. R.

    In: Journal of Neurochemistry, Vol. 49, No. 4, 1987, p. 1280-1285.

    Research output: Contribution to journalArticle

    Stach, RW, Lyons, CR & Perez-Polo, JR 1987, 'Characteristics of partially purified nerve growth factor receptor', Journal of Neurochemistry, vol. 49, no. 4, pp. 1280-1285.
    Stach, R. W. ; Lyons, C. R. ; Perez-Polo, J. R. / Characteristics of partially purified nerve growth factor receptor. In: Journal of Neurochemistry. 1987 ; Vol. 49, No. 4. pp. 1280-1285.
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