Searching for specific binding sites of the secretory glycoproteins of the subcommissural organ.
The molecular organization of Reissner's fiber (RF), the structure of its proteins, and the permanent turnover of these proteins are all facts supporting the possibility that RF may perform multiple functions. There is evidence that CSF-soluble RF-glycoproteins may occur under physiological conditions. The present investigation was designed to investigate the probable existence within the CNS of specific binding sites for RF-glycoproteins. Three experimental protocols were used: (1) immunocytochemistry of the CNS of bovine fetuses using anti-idiotypic antibodies, raised against monoclonal antibodies developed against bovine RF-glycoproteins; (2) in vivo binding of the RF glycoproteins, perfusing into the rat CSF 125I-labeled RF-glycoproteins, or grafting SCO into a lateral ventricle of the rat; (3) in vitro binding of unlabeled RF-glycoproteins to rat and bovine choroid plexuses maintained in culture. One of the anti-idiotypic antibody generated by a Mab raised against RF-glycoproteins binds to choroidal cells. Furthermore, binding of RF-glycoproteins to the rat choroid plexus was obtained when: (1) the choroid plexus was cultured in the presence of unlabeled RF-glycoproteins; (2) the concentration of soluble RF-glycoproteins in the CSF was increased by isografting SCOs into a lateral ventricle; (3) radiolabeled glycoproteins were perfused into the ventricular CSF. This evidence suggests that the apical plasma membrane of the ependymal cells of the choroid plexus has specific binding sites for RF-glycoproteins, of unknown functional significance. The radiolabeled RF-glycoproteins perfused into the rat CSF also bound to the paraventricular thalamic nucleus, the floor of the Sylvian aqueduct and of the rostral half of the fourth ventricle, and the meninges of the brain and spinal cord. The labeling of the paraventricular thalamic nucleus points to a functional relationship between this nucleus and the SCO. The possibility that the SCO may be a component of the circadian timing system is discussed.
Miranda
E
E
Departamento de Biología Animal, Facultad de Ciencias, Universidad de Málaga, 29071 Málaga, Spain.
Almonacid
J A
JA
Rodriguez
S
S
Perez
J
J
Hein
S
S
Cifuentes
M
M
Fernández-Llebrez
P
P
Rodríguez
E M
EM
D000818:Animals; D000888:Antibodies, Anti-Idiotypic / Q000032:analysis; D000911:Antibodies, Monoclonal / Q000276:immunology; D001345:Autoradiography; D001665:Binding Sites / Q000502:physiology*; D002417:Cattle; D015816:Cell Adhesion Molecules, Neuronal / Q000276:immunology / Q000378:metabolism*; D002552:Cerebral Ventricles / Q000502:physiology; D002555:Cerebrospinal Fluid / Q000502:physiology; D002831:Choroid Plexus / Q000502:physiology*; D046508:Culture Techniques / Q000379:methods; D004797:Enzyme-Linked Immunosorbent Assay; D008297:Male; D051379:Mice; D020644:Midline Thalamic Nuclei / Q000502:physiology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013351:Subcommissural Organ / Q000378:metabolism* / Q000637:transplantation
D000888:Antibodies, Anti-Idiotypic; D000911:Antibodies, Monoclonal; D015816:Cell Adhesion Molecules, Neuronal; C108402:SCO-spondin