scholarly journals The chloride channel ClC‐2 contributes to the inwardly rectifying Cl − conductance in cultured porcine choroid plexus epithelial cells

2000 ◽  
Vol 523 (2) ◽  
pp. 313-324 ◽  
Author(s):  
Hidetoshi Kajita ◽  
Koichiro Omori ◽  
Hiroko Matsuda
Keyword(s):  
Epithelial Cells ◽  
Choroid Plexus ◽  
Chloride Channel ◽  
Inwardly Rectifying ◽  
Cl Conductance ◽  
Choroid Plexus Epithelial

Cl- current activation in choroid plexus epithelial cells involves a G protein and protein kinase A

1994 ◽  
Vol 266 (2) ◽  
pp. C536-C540 ◽  
Author(s):  
T. Kotera ◽  
P. D. Brown
Keyword(s):  
Protein Kinase ◽  
Epithelial Cells ◽  
Protein Kinase A ◽  
Choroid Plexus ◽  
G Proteins ◽  
Patch Clamp Technique ◽  
Gamma S ◽  
Cl Conductance ◽  
Kinase A ◽  
Choroid Plexus Epithelial

The involvement of GTP-binding proteins (G proteins) in the regulation of the Cl- conductance in rat choroid plexus epithelial cells was investigated, using the whole cell patch-clamp technique. Intracellular application of a nonhydrolyzable GTP analogue, guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S; 0.1-0.2 mM), evoked a transient increase in the Cl- conductance. The activated Cl- current exhibited inward rectification and was independent of time at hyperpolarizing or depolarizing voltage pulses. The effect of GTP gamma S was inhibited by a nonhydrolyzable GDP analogue, guanosine 5'-O-(2-thiodiphosphate) (2 mM), and by an inhibitor of protein kinase A, H-89, but was not affected by chelation of cytosolic Ca2+ with 5 mM 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid. GTP gamma S failed to activate the current when ATP was omitted from the pipette solution. Intracellular application of adenosine 3',5'-cyclic monophosphate (cAMP; 0.25 mM) or the catalytic subunit of protein kinase A activated a similar Cl- current. These results suggest that G proteins activate Cl- channels via a cAMP-dependent pathway in rat choroid plexus.

scholarly journals Porcine Choroid Plexus Epithelial Cells Induce Streptococcus suis Bacteriostasis In Vitro

2004 ◽  
Vol 72 (5) ◽  
pp. 3084-3087 ◽  
Author(s):  
Rüdiger A. Adam ◽  
Tobias Tenenbaum ◽  
Peter Valentin-Weigand ◽  
Maurice Laryea ◽  
Bernd Schwahn ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Bacterial Meningitis ◽  
Choroid Plexus ◽  
Host Defense ◽  
Streptococcus Suis ◽  
Active Role ◽  
Necrosis Factor Alpha ◽  
Ifn Γ ◽  
Choroid Plexus Epithelial

ABSTRACT The involvement of the choroid plexus in host defense during bacterial meningitis is unclear. Aiming to elucidate possible antibacterial mechanisms, we stimulated primary porcine choroid plexus epithelial cells (pCPEC) with proinflammatory cytokines and challenged them with various Streptococcus suis strains. In the supernatant of gamma interferon (IFN-γ)-stimulated pCPEC, streptococcal growth was markedly suppressed. Costimulation with tumor necrosis factor alpha enhanced this bacteriostatic effect, while supplementation of l-tryptophan completely eliminated it. We also demonstrate that an activation of indoleamine 2,3-dioxygenase in the pCPEC seems to be responsible for the IFN-γ-induced bacteriostasis. This supports the hypothesis of an active role of the choroid plexus in host defense against bacterial meningitis.

Characterization of two splice variants of human organic anion transporting polypeptide 3A1 isolated from human brain

2007 ◽  
Vol 292 (2) ◽  
pp. C795-C806 ◽  
Author(s):  
Robert D. Huber ◽  
Bo Gao ◽  
Marguerite-Anne Sidler Pfändler ◽  
Wenting Zhang-Fu ◽  
Simone Leuthold ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Human Brain ◽  
Frontal Cortex ◽  
Choroid Plexus ◽  
Splice Variants ◽  
Organic Anion ◽  
Xenopus Laevis Oocytes ◽  
Organic Anion Transporting Polypeptide ◽  
Human Frontal Cortex ◽  
Choroid Plexus Epithelial

In the present study we isolated two splice variants of organic anion transporting polypeptide 3A1 (OATP3A1_v1 and OATP3A1_v2) from human brain. OATP3A1_v2 lacks 18 amino acids (aa) at the COOH-terminal end (692 aa) but is otherwise similar in sequence to OATP3A1_v1 (710 aa). OATP3A1_v1 exhibits a wide tissue distribution, with expression in testis, various brain regions, heart, lung, spleen, peripheral blood leukocytes, and thyroid gland, whereas OATP3A1_v2 is predominantly expressed in testis and brain. On the cellular and subcellular levels OATP3A1_v1 could be immunolocalized in testicular germ cells, the basolateral plasma membrane of choroid plexus epithelial cells, and neuroglial cells of the gray matter of human frontal cortex. Immunolocalization of OATP3A1_v2 included Sertoli cells in testis, apical and/or subapical membranes in choroid plexus epithelial cells, and neurons (cell bodies and axons) of the gray and white matter of human frontal cortex. The rodent ortholog Oatp3a1 was also widely distributed in rat brain, and its localization included somatoneurons as well as astroglial cells. Transport studies in cRNA-injected Xenopus laevis oocytes and in stably transfected Chinese hamster ovary FlpIn cells revealed a similar broad substrate specificity for both splice variants. Transported substrates include prostaglandin (PG)E1 and PGE2, thyroxine, and the cyclic oligopeptides BQ-123 (endothelin receptor antagonist) and vasopressin. These studies provide further evidence for the involvement of OATPs in oligopeptide transport. They specifically suggest that OATP3A1 variants might be involved in the regulation of extracellular vasopressin concentration in human brain and thus might influence the neuromodulation of neurotransmission by cerebral neuropeptides such as vasopressin.

Sign in / Sign up

Export Citation Format

Share Document