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Lectin‐Induced Inhibition of Nerve Growth Factor Binding by Receptors of Sympathetic Ganglia
Author(s) -
Costrini Nicholas V.,
Kogan Melanie
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb01715.x
Subject(s) - wheat germ agglutinin , receptor , nerve growth factor , lectin , concanavalin a , binding site , superior cervical ganglion , cell surface receptor , cervical ganglia , biology , endocrinology , biochemistry , medicine , chemistry , in vitro
Nerve growth factor (NGF) initiates a pleiotypic response in numerous tissues derived from the neural crest by binding to specific plasma membrane receptors. In sympathetic ganglia this receptor has been characterized as a highly asymmetric, minimally hydrophobic, intrinsic membrane protein with a molecular weight of 135,000 (Costrini et al., 1979b). To further characterize this moiety we assessed the effects of lectins on 125 I‐NGF specific binding to preparations of particulate and nonionic detergent‐extracted micro‐somal receptors of rabbit superior cervical ganglia (SCG). Concanavalin A (Con A) and wheat germ agglutinin (WGA), but not soybean agglutinin or Ulex europaeus I, induced a concentration‐related, carbohydrate‐specific decrease in 125 T‐NGF binding. Following Con A exposure, 125 I‐NGF specific binding to particulate SCG receptors was maximally reduced to 23% of control values. WGA similarly reduced NGF binding to particulate microsomal receptors to 37% of control values. Scatchard analysis of growth factor binding following Con A exposure indicated that this lectin effect was principally due to a sixfold reduction in maximum receptor affinity. Lectin‐associated impairment of NGF binding was also demonstrated by using a Triton X‐100 solubilized receptor preparation. These results provide evidence that the high‐affinity‐state NGF receptor of SCG is a glycoprotein containing N ‐acetylglucosamine and α‐D‐mannopyranoside residues. These residues are probably located in close proximity to the growth factor binding region of the NGF receptor.