Efficient processing and expression of human nerve growth factor receptors in Xenopus laevis oocytes: effects on...

The nerve growth factor (NGF) receptor is an integral membrane protein that is phosphorylated and heavily glycosylated. Determination of the amino acid sequence by molecular cloning indicates that the receptor is a cysteine-rich protein which contains a signal peptide sequence and spans the lipid bilayer with a single transmembrane sequence. A single mRNA of 3.8 kilobases was observed for the receptor, of which 1.5 kilobases is coding sequence. We have used microinjection of receptor RNA in Xenopus laevis oocytes to obtain cell surface expression of the receptor. The presence of NGF receptors in oocytes was verified by radioimmunoassay, specific binding of [125I]NGF, and metabolic labeling followed by immunoprecipitation. The NGF receptor protein was rapidly processed in oocytes and displayed extensive glycosylation. Furthermore, the presence of NGF receptors in oocytes potentiates the ability of progesterone to induce maturation.