title: Expression of neuropeptide processing enzymes and neurosecretory proteins in ependyma and choroid plexus epithelium.
abstract: Recent studies suggest that brain ependyma and choroid plexus produce neuropeptide processing enzymes. To facilitate the understanding of these cells and their ability to produce biologically active peptides, we developed cultures of defined cell type. Ependymal cells were characterized by morphological criteria, and choroid plexus epithelial cell lines were characterized by the presence of the mRNA for IGF-II and transthyretin, a thyroxine binding protein produced in liver and choroid plexus. The ependymal cells and the choroid plexus epithelial cell lines were then examined for the presence of mRNAs for various neuropeptide processing enzymes. Northern blot analysis revealed high levels of furin, carboxypeptidase E, and peptidyl glycine alpha-amidating monooxygenase mRNAs, with levels in ependymal cells comparable to those in brain or pituitary. Carboxypeptidase E activity was detected in medium from cultured ependymal cells; this activity was identified as carboxypeptidase E based on the acidic pH optimum and sensitivity to various inhibitors. The mRNAs for other neuropeptide processing enzymes, such as prohormone convertases 1 and 2, were not detected on Northern blots of RNA from ependyma or choroid plexus epithelium. Since ependyma and choroid plexus epithelium express a subset of processing enzymes, we suggest that these cells have the capacity to produce biologically active peptides. Initial screening by reverse transcriptase-polymerase chain reaction assays has demonstrated the presence of mRNA for the neurosecretory proteins chromogranin B and secretogranin II in both ependyma and choroid plexus epithelium.
authors.affiliation: Department of Developmental Biology and Cancer, Albert Einstein College of Medicine, Bronx, NY 10461.
authors.forename: P
authors.initials: P
authors.lastname: Gee
authors.forename: C H
authors.initials: CH
authors.lastname: Rhodes
authors.forename: L D
authors.initials: LD
authors.lastname: Fricker
authors.forename: R H
authors.initials: RH
authors.lastname: Angeletti
mesh_terms: D000818:Animals; D001483:Base Sequence; D043423:Carboxypeptidase H; D002268:Carboxypeptidases / Q000096:biosynthesis; D002478:Cells, Cultured; D002831:Choroid Plexus / Q000378:metabolism*; D002864:Chromogranins / Q000096:biosynthesis; D010450:Endopeptidases / Q000096:biosynthesis*; D004805:Ependyma / Q000378:metabolism*; D004848:Epithelium / Q000378:metabolism; D045683:Furin; D006899:Mixed Function Oxygenases / Q000096:biosynthesis; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes; D009419:Nerve Tissue Proteins / Q000096:biosynthesis*; D009479:Neuropeptides / Q000378:metabolism*; D009490:Neurosecretory Systems / Q000502:physiology*; D014176:Protein Biosynthesis; D011506:Proteins; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D017208:Rats, Wistar; D013381:Subtilisins / Q000096:biosynthesis
chemical_list: D002864:Chromogranins; D009097:Multienzyme Complexes; D009419:Nerve Tissue Proteins; D009479:Neuropeptides; D011506:Proteins; D012333:RNA, Messenger; D006899:Mixed Function Oxygenases; C035189:peptidylglycine monooxygenase; D002268:Carboxypeptidases; D010450:Endopeptidases; D043423:Carboxypeptidase H; D013381:Subtilisins; D045683:Furin