Nerve growth factor (NGF) influences the survival and differentiation of a variety of neuronal and nonneuronal cells. The actions of this polypeptide result from binding to specific cell surface receptors which are present as both high and low affinity sites. Although both types of receptor bind NGF only the high affinity form is capable of signal transduction. Cross-linking studies with 125I-NGF have shown that the high affinity receptor of rat PC12 cells forms an Mr 158,000 complex with NGF while the low affinity receptor forms an Mr 100,000 complex. Full length cDNA clones for both the human and rat NGF receptor genes have been produced and sequenced, revealing greater than 90% homology between the two species. Recently, it has been shown that cells which do not normally respond to NGF only express low affinity receptors from transfected NGF genes but cells which normally are NGF-responsive express high affinity receptors from the same NGF sequences. This supports the hypothesis that the high affinity receptors have a unique component in addition to the subunit common to the low affinity receptors.
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