PE-11, a peptide derived from chromogranin B, in the human brain.

This study was performed to investigate the distribution of chromogranin B in the human central nervous system. We used an antiserum raised against a synthetic peptide (PE-11) present in the chromogranin B molecule. PE-11-like immunoreactivity was characterized by molecular size exclusion and reversed-phase high-performance liquid chromatography. Its localization was studied using immunocytochemistry. Only the free peptide and an N-terminally elongated peptide were detected by molecular size exclusion high-performance liquid chromatography, indicating that proteolytic processing of chromogranin B is quite extensive. PE-11-like immunoreactivity was present in differently shaped fibers, varicosities and neurons, but not in glial cells. Its density varied throughout the brain. An especially high density was observed in the bed nucleus of the stria terminalis, the central and cortical nuclei of the amygdala, the hypothalamus, the hippocampus, the raphe complex, the nucleus interpeduncularis, the nucleus of the solitary tract, and laminae I and II of the spinal cord. This study demonstrates a significant processing of chromogranin B and indicates that chromogranin B constitutes a precursor for smaller peptides which are derived by endoproteolytic processing. It provides the neuroanatomical basis to investigate the chromogranin B molecule as a widespread component of large dense-core vesicles in the human central nervous system.