The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Identification of a New Class of Molecules, the Arachidonyl Amino Acids, and Characterization of One Member That Inhibits Pain
Open accessAbstract
In mammals, specific lipids and amino acids serve as crucial signaling molecules. In bacteria, conjugates of lipids and amino acids (referred to as lipoamino acids) have been identified and found to possess biological activity. Here, we report that mammals also produce lipoamino acids, specifically the arachidonyl amino acids. We show that the conjugate of arachidonic acid and glycine (N-arachidonylglycine (NAGly)) is present in bovine and rat brain as well as other tissues and that it suppresses tonic inflammatory pain. The biosynthesis of NAGly and its degradation by the enzyme fatty acid amide hydrolase can be observed in rat brain tissue. In addition to NAGly, bovine brain produces at least two other arachidonyl amino acids: N-arachidonyl gamma-aminobutyric acid (NAGABA) and N-arachidonylalanine. Like NAGly, NAGABA inhibits pain. These findings open the door to the identification of other members of this new class of biomolecules, which may be integral to pain regulation and a variety of functions in mammals.
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Cited by
Huang, S. M., Bisogno, T., Trevisani, M., Al-Hayani, A., De Petrocellis, L., Fezza, F., Tognetto, M., Petros, T. J., Krey, J. F., Chu, C. J., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122196999 · Cited by 964
Self-citationStructure and function of fatty acid amide hydrolase
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Paracetamol: New Vistas of an Old Drug
Bertolini, A., Ferrari, A., Ottani, A., Guerzoni, S., Tacchi, R., & Leone, S. (2006) · CNS Drug Reviews · doi:10.1111/j.1527-3458.2006.00250.x · Cited by 674
Högestätt, E. D., Jönsson, B. A. G., Ermund, A., Andersson, D. A., Björk, H., Alexander, J. P., Cravatt, B. F., Basbaum, A. I., & Zygmunt, P. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501489200 · Cited by 454
Expression analysis of G Protein-Coupled Receptors in mouse macrophages
Lattin, J. E., Schroder, K., Su, A. I., Walker, J. R., Zhang, J., Wiltshire, T., Saijo, K., Glass, C. K., Hume, D. A., Kellie, S., et al. (2008) · Immunome Research · doi:10.1186/1745-7580-4-5 · Cited by 438
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Metadata
- Authors
- Huang, S. M., Bisogno, T., Petros, T. J., Chang, S. Y., Zavitsanos, P. A., Zipkin, R. E., Sivakumar, R., Coop, A., Maeda, D. Y., De Petrocellis, L., Burstein, S., Di Marzo, V., & Walker, J. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-11
- Volume
- 276
- Issue
- 46
- Pages
- 42639-42644
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2138357748
- Cited by
- 339
- References
- 26
- FWCI
- 4.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Huang, S. M., Bisogno, T., Petros, T. J., Chang, S. Y., Zavitsanos, P. A., Zipkin, R. E., Sivakumar, R., Coop, A., Maeda, D. Y., De Petrocellis, L., Burstein, S., Di Marzo, V., & Walker, J. M. (2001). Identification of a New Class of Molecules, the Arachidonyl Amino Acids, and Characterization of One Member That Inhibits Pain. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m107351200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
