Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-5-6
pubmed:abstractText
We have identified by Scatchard analysis both high (124 pM, 14.4 x106 sites/micrograms protein, 7600 sites/cell) and low (1.6 nM, 7.7x106 sites/micrograms protein, 4100 sites/cell) affinity receptors for [125I]-rat ciliary neurotrophic factor (rCNTF) on astrocytes. Ligand competition studies showed that the binding of [125I]-rCNTF was effectively competed by rCNTF and human CNTF, but not by hLIF, mIL-6 or mIL-1B. Three proteins specifically crossed-linked to [125I]-rCNTF, with the molecular weights of 190, 100, and 43 kDa, were immunoprecipitated by anti-rCNTF antibodies. Anti-LIFR or anti-gp130 antibodies immunoprecipitated the 100 and the 190 kDa proteins. CNTF induced the tyrosine phosphorylation of LIFR and gp130, as well as of proteins with the molecular weights of 88/91 and 42 kDa. The phosphorylation of the 88/91 kDa protein(s) was inhibited by pretreating the cells with staurosporine, 12-myristate 13-acetate phorbol (PMA), W7, chlorpromazine, or the intracellular Ca+2 chelator BAPTA/AM. In contrast, CNTF and PMA acted synergistically to induce the phosphorylation of two proteins with the molecular weights of 42 and 44 kDa. At later time points following CNTF treatment, c-fos messenger RNA and protein levels were increased. Collectively, these data indicate that hippocampal astrocytes express high-affinity, biologically functional receptor complexes for CNTF.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-8993
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Elsevier Science B.V.
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
818
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
236-51
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10082809-Animals, pubmed-meshheading:10082809-Astrocytes, pubmed-meshheading:10082809-Binding, Competitive, pubmed-meshheading:10082809-Cells, Cultured, pubmed-meshheading:10082809-Ciliary Neurotrophic Factor, pubmed-meshheading:10082809-Endocytosis, pubmed-meshheading:10082809-Enzyme Inhibitors, pubmed-meshheading:10082809-Hippocampus, pubmed-meshheading:10082809-Humans, pubmed-meshheading:10082809-Nerve Growth Factors, pubmed-meshheading:10082809-Nerve Tissue Proteins, pubmed-meshheading:10082809-Phorbol Esters, pubmed-meshheading:10082809-Phosphatidylinositols, pubmed-meshheading:10082809-Phosphorylation, pubmed-meshheading:10082809-Protein-Tyrosine Kinases, pubmed-meshheading:10082809-Radioligand Assay, pubmed-meshheading:10082809-Rats, pubmed-meshheading:10082809-Rats, Sprague-Dawley, pubmed-meshheading:10082809-Type C Phospholipases
pubmed:year
1999
pubmed:articleTitle
Characterization of receptors for ciliary neurotrophic factor on rat hippocampal astrocytes.
pubmed:affiliation
Regeneron Pharmaceuticals, 777 Old Saw Mill River Road, Tarrytown, NY., USA. ralph_alderson@hgsi.com
pubmed:publicationType
Journal Article