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Epithelial cells purified from choroid plexus have receptors for vasoactive intestinal polypeptide

Nilsson, Christer LU ; Fahrenkrug, Jan; Lindvall-Axelsson, Maria and Owman, Christer LU (1991) In Brain Research 542(2). p.241-247
Abstract
Using the choroid plexus from pig a method has been developed to purify the epithelial cells from the underlying vascularized connective tissue stroma. An epithelial cell fraction was obtained that showed a purity of at least 95%, as determined by light microscopic analysis. The epithelial cells were investigated for the presence of binding sites for the neurotransmitter peptide, vasoactive intestinal polypeptide (VIP). Suspensions of epithelial cells were found to have high affinity binding sites for 125I-labelled VIP, with maximum binding obtained after 30 min incubation at 20 degrees C with a concentration of 50 micrograms cell protein per sample. Competition experiments with displacement of [125I]VIP binding by increasing... (More)
Using the choroid plexus from pig a method has been developed to purify the epithelial cells from the underlying vascularized connective tissue stroma. An epithelial cell fraction was obtained that showed a purity of at least 95%, as determined by light microscopic analysis. The epithelial cells were investigated for the presence of binding sites for the neurotransmitter peptide, vasoactive intestinal polypeptide (VIP). Suspensions of epithelial cells were found to have high affinity binding sites for 125I-labelled VIP, with maximum binding obtained after 30 min incubation at 20 degrees C with a concentration of 50 micrograms cell protein per sample. Competition experiments with displacement of [125I]VIP binding by increasing concentrations of unlabeled VIP indicated the presence of a single class of binding sites with a Kd of 3 nM and a binding capacity of 970 pmol/g cell protein. Cross-linking of [125I]VIP to epithelial cells with disuccinimido dithiobis (propionate) (DSP), followed by SDS-polyacrylamide gel electrophoresis, demonstrated binding to a single 55 kD protein. The receptor was highly specific for VIP as binding was only inhibited in the presence of high concentrations of the related peptides helodermin, growth hormone-releasing factor, secretin, and peptide histidine isoleucine. This is the first demonstration of VIP-binding to choroid plexus epithelial cells. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Choroid plexus, Vasoactive intestinal polypeptide, Vasoactive intestinal polypeptide receptor, Receptor binding
in
Brain Research
volume
542
issue
2
pages
241 - 247
publisher
Elsevier
external identifiers
  • pmid:1851455
  • scopus:0026083216
ISSN
1872-6240
DOI
10.1016/0006-8993(91)91573-J
language
English
LU publication?
yes
id
f18c82a4-6e42-4514-b05c-5b8d0cc974f6 (old id 1105961)
date added to LUP
2008-08-01 11:53:01
date last changed
2017-07-30 03:33:42
@article{f18c82a4-6e42-4514-b05c-5b8d0cc974f6,
  abstract     = {Using the choroid plexus from pig a method has been developed to purify the epithelial cells from the underlying vascularized connective tissue stroma. An epithelial cell fraction was obtained that showed a purity of at least 95%, as determined by light microscopic analysis. The epithelial cells were investigated for the presence of binding sites for the neurotransmitter peptide, vasoactive intestinal polypeptide (VIP). Suspensions of epithelial cells were found to have high affinity binding sites for 125I-labelled VIP, with maximum binding obtained after 30 min incubation at 20 degrees C with a concentration of 50 micrograms cell protein per sample. Competition experiments with displacement of [125I]VIP binding by increasing concentrations of unlabeled VIP indicated the presence of a single class of binding sites with a Kd of 3 nM and a binding capacity of 970 pmol/g cell protein. Cross-linking of [125I]VIP to epithelial cells with disuccinimido dithiobis (propionate) (DSP), followed by SDS-polyacrylamide gel electrophoresis, demonstrated binding to a single 55 kD protein. The receptor was highly specific for VIP as binding was only inhibited in the presence of high concentrations of the related peptides helodermin, growth hormone-releasing factor, secretin, and peptide histidine isoleucine. This is the first demonstration of VIP-binding to choroid plexus epithelial cells.},
  author       = {Nilsson, Christer and Fahrenkrug, Jan and Lindvall-Axelsson, Maria and Owman, Christer},
  issn         = {1872-6240},
  keyword      = {Choroid plexus,Vasoactive intestinal polypeptide,Vasoactive intestinal polypeptide receptor,Receptor binding},
  language     = {eng},
  number       = {2},
  pages        = {241--247},
  publisher    = {Elsevier},
  series       = {Brain Research},
  title        = {Epithelial cells purified from choroid plexus have receptors for vasoactive intestinal polypeptide},
  url          = {http://dx.doi.org/10.1016/0006-8993(91)91573-J},
  volume       = {542},
  year         = {1991},
}