The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Dopamine D 1 and adenosine A 1 receptors form functionally interacting heteromeric complexes
Open accessAbstract
The possible molecular basis for the previously described antagonistic interactions between adenosine A 1 receptors (A 1 R) and dopamine D 1 receptors (D 1 R) in the brain have been studied in mouse fibroblast Ltk − cells cotransfected with human A 1 R and D 1 R cDNAs or with human A 1 R and dopamine D 2 receptor (long-form) (D 2 R) cDNAs and in cortical neurons in culture. A 1 R and D 1 R, but not A 1 R and D 2 R, were found to coimmunoprecipitate in cotransfected fibroblasts. This selective A 1 R/D 1 R heteromerization disappeared after pretreatment with the D 1 R agonist, but not after combined pretreatment with D 1 R and A 1 R agonists. A high degree of A 1 R and D 1 R colocalization, demonstrated in double immunofluorescence experiments with confocal laser microscopy, was found in both cotransfected fibroblast cells and cortical neurons in culture. On the other hand, a low degree of A 1 R and D 2 R colocalization was observed in cotransfected fibroblasts. Pretreatment with the A 1 R agonist caused coclustering (coaggregation) of A 1 R and D 1 R, which was blocked by combined pretreatment with the D 1 R and A 1 R agonists in both fibroblast cells and in cortical neurons in culture. Combined pretreatment with D 1 R and A 1 R agonists, but not with either one alone, substantially reduced the D 1 R agonist-induced accumulation of cAMP. The A 1 R/D 1 R heteromerization may be one molecular basis for the demonstrated antagonistic modulation of A 1 R of D 1 R receptor signaling in the brain. The persistence of A 1 R/D 1 R heteromerization seems to be essential for the blockade of A 1 R agonist-induced A 1 R/D 1 R coclustering and for the desensitization of the D 1 R agonist-induced cAMP accumulation seen on combined pretreatment with D 1 R and A 1 R agonists, which indicates a potential role of A 1 R/D 1 R heteromers also in desensitization mechanisms and receptor trafficking.
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Cites
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Cited by
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Self-citationAdenosine Receptors: Expression, Function and Regulation
Sheth, S., Brito, R., Mukherjea, D., Rybak, L., & Ramkumar, V. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15022024 · Cited by 401
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Self-citationThe G protein-coupled receptor heterodimer network (GPCR-HetNet) and its hub components
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Metadata
- Authors
- Ginés, S., Hillion, J., Torvinen, M., Le Crom, S., Casadó, V., Canela, E. I., Rondin, S., Lew, J. Y., Watson, S., Zoli, M., Agnati, L. F., Vernier, P., Lluis, C., Ferré, S., Fuxe, K., & Franco, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-07-11
- Volume
- 97
- Issue
- 15
- Pages
- 8606-8611
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2163369915
- Cited by
- 445
- References
- 26
- FWCI
- 16.53
- Type
- journal article
- Language
- en
- Open access
- green
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- Ginés, S., Hillion, J., Torvinen, M., Le Crom, S., Casadó, V., Canela, E. I., Rondin, S., Lew, J. Y., Watson, S., Zoli, M., Agnati, L. F., Vernier, P., Lluis, C., Ferré, S., Fuxe, K., & Franco, R. (2000). Dopamine D 1 and adenosine A 1 receptors form functionally interacting heteromeric complexes. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.150241097
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