rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2003-12-15
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pubmed:abstractText |
To identify binding partners of the A1AR (A1 adenosine receptor), yeast two-hybrid screening of a rat embryonic cDNA library was performed. This procedure led to the identification of erythrocyte membrane cytoskeletal protein (represented as 4.1G) as an A1AR-binding partner. Truncation studies revealed that the C-terminal domain of 4.1G was essential for binding to A1ARs and that the C-terminal domain of 4.1G and the third intracellular loop of A1ARs interacted. A1AR-4.1G interaction was also confirmed in studies using brain tissue. Studies in HEK-293 (human embryonic kidney 293) cells and Chinese-hamster ovary cells showed that 4.1G interfered with A1AR signal transduction, as 4.1G reduced A1AR-mediated inhibition of cAMP accumulation and intracellular calcium release. 4.1G also altered cell-surface A1AR expression. These observations identify 4.1G as a novel A1AR-binding partner that can regulate adenosine action.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
377
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-9
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pubmed:dateRevised |
2011-6-20
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pubmed:meshHeading |
pubmed-meshheading:12974671-Humans,
pubmed-meshheading:12974671-Animals,
pubmed-meshheading:12974671-Brain,
pubmed-meshheading:12974671-Rats,
pubmed-meshheading:12974671-Male,
pubmed-meshheading:12974671-Cricetinae,
pubmed-meshheading:12974671-Models, Molecular,
pubmed-meshheading:12974671-Binding Sites,
pubmed-meshheading:12974671-CHO Cells,
pubmed-meshheading:12974671-Cell Line,
pubmed-meshheading:12974671-Rats, Sprague-Dawley,
pubmed-meshheading:12974671-Cyclic AMP,
pubmed-meshheading:12974671-Protein Structure, Tertiary,
pubmed-meshheading:12974671-Calcium Signaling,
pubmed-meshheading:12974671-Cytoskeletal Proteins,
pubmed-meshheading:12974671-Two-Hybrid System Techniques
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