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Distribution of arrestin-like protein and beta-subunit of GTP-binding proteins in quail choroid plexuses.

Authors
  • Oliver, J1
  • Mirshahi, M
  • Herbute, S
  • Peraldi-Roux, S
  • Trebuchon, L
  • Brisson, P
  • Collin, J P
  • Faure, J P
  • Gabrion, J
  • 1 Laboratoire de Neurobiologie Endocrinologique, URA CNRS 1197, Université de Montpellier II, France. , (France)
Type
Published Article
Journal
Cellular Signalling
Publisher
Elsevier
Publication Date
Jan 01, 1991
Volume
3
Issue
5
Pages
461–472
Identifiers
PMID: 1760255
Source
Medline
License
Unknown

Abstract

Monoclonal antibodies (Mabs) directed against retinal arrestin (S-antigen) were used to detect and characterize this protein in choroid plexus (CP) of quails maintained during eight days, either under long-day photoperiods or in constant darkness. Immunocytochemistry and Western blotting confirmed the presence and the distribution of an arrestin-like protein in quail CP. Arrestin-like immunoreactivities in CP were compared with those obtained with Mabs to beta 36-subunit of G proteins (G beta), alpha-subunit of transducin and rhodopsin. Rhodopsin-like and transducin-like proteins could not be detected in choroidal cells, whereas intense positive reactions were observed with anti-G beta and anti-arrestin Mabs. The strongest immunoreactivities were found in choroidal ependymocytes of the lateral and IIIrd ventricles. In CP epithelial cells lining the IVth ventricle, very weak or no immunoreactivity could be detected with Mabs to arrestin, while Mab against G beta subunit always provided a positive reaction. In quails maintained in constant darkness, arrestin- and G beta-immunoreactivities of CP epithelial cells displayed changes in cellular distribution and intensity (decrease or disappearance of the immunoreactions). The strong arrestin-like immunoreaction located in the apical region of ependymocytes suggests the preferential association of the protein with choroidal microvilli and a possible role in cerebrospinal fluid production assumed by CP cells.

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