Protein secretion by choroid plexus: isolated apical fragments synthesize protein in vitro.
Protein synthesis was studied in the isolated rat choroid plexus. When the choroid plexus was studied by transmission electron microscopy, membrane-bound structures were often observed in the ventricular space. These structures appear to bud from the apical surface of the epithelial cells. In the present study, we attempted to isolate these membrane-bound cellular fragments from the choroid plexus and to determine their ability to synthesize proteins. The apical fragments (aposomes) were isolated from the choroid plexus by allowing tissue explants to incubate in media (37 degrees C) for 1 h. The tissue was removed and the media, now containing aposomes, was incubated with [S35]methionine (100 microCi). The media was collected and analysed by SDS-PAGE followed by fluorography. Parallel [S35]methionine incubations were done with whole tissue explants. The SDS-PAGE protein derived from the aposomes was similar to the profile derived from the tissue. In addition, proteins detected in CSF had relative molecular weights comparable to the products synthesized by aposomes. These observations suggest that aposomes provide an additional route of entry for proteins into CSF.
D000818:Animals; D002831:Choroid Plexus / Q000378:metabolism* / Q000648:ultrastructure; D004247:DNA / Q000032:analysis; D066298:In Vitro Techniques; D008297:Male; D008715:Methionine / Q000378:metabolism; D008854:Microscopy, Electron; D008970:Molecular Weight; D014176:Protein Biosynthesis; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013462:Sulfur Radioisotopes
D011506:Proteins; D013462:Sulfur Radioisotopes; D004247:DNA; D008715:Methionine