RESUMEN
Recent investigations have shown that the neuroendocrine and immune systems profoundly affect each other. In part, these interactions occur via common chemical messengers and receptors. One possible shared chemical messenger is the opioid precursor preproenkephalin, for which high concentrations of messenger RNA are present in brain, adrenal, and activated T helper cells. Because the biologic action of most peptide messengers depends on the posttranslational processing of the precursor, we have examined T helper cell lines for the production of proenkephalin-derived peptides. These peptides were characterized by multiple radioimmunoassays, gel filtration chromatography, and opiate radioreceptor assays. We found that activated T helper cells secrete significant concentrations of high-molecular-weight, opiate-inactive peptides, which are distinct from the proenkephalin-derived peptides of the neuroendocrine system. These studies clearly indicate cell-specific processing of proenkephalin, and suggest that the T helper cell-secreted products may have nonopiate receptor-mediated actions.
Asunto(s)
Encefalinas/metabolismo , Péptidos/metabolismo , Linfocitos T Colaboradores-Inductores/metabolismo , Glándulas Suprarrenales/metabolismo , Animales , Encéfalo/metabolismo , Bovinos , Cromatografía en Gel , Endorfinas/metabolismo , Ratones , Ratones Endogámicos CBA , Naloxona/metabolismo , Radioinmunoensayo , RatasRESUMEN
Using a radioimmunoassay specific for the carboxyl terminus of beta-endorphin-(1-9) large amounts of beta-endorphin-(1-9)-immunoreactive material was detected in the human pituitary. The major peak of immunoreactivity was purified and characterized by fast atom bombardment-mass spectrometry and Edman degradation sequencing as authentic beta-endorphin-(1-9). In the rat pituitary the highest concentration of beta-endorphin-(1-9) immunoreactivity was in the posterior neurointermediate lobe. This material was identified as N-acetyl beta-endorphin-(1-9) by multiple radioimmunoassays, gel chromatography, and reversed-phase high-performance liquid chromatography. Control experiments determined that beta-endorphin-(1-9) was not formed postmortem or during the extraction procedure. These studies suggest that single lysine residues, similar to single arginine residues, are potential sites of posttranslational processing.