The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Analysis of the Native Quaternary Structure of Vanilloid Receptor 1
Open accessAbstract
Vanilloid receptor subtype 1 (VR1) is a ligand-gated channel that can be activated by capsaicin and other vanilloids as well as by protons and heat. In the present study, we have analyzed the oligomeric state of VR1. Co-immunoprecipitation of differently tagged VR1 molecules indicated that VR1 can form oligomers. Using two different heterologous VR1 expression systems as well as endogenous VR1 expressed in dorsal root ganglion cells, we analyzed oligomer formation using perfluoro-octanoic acid polyacrylamide gel electrophoresis. Results were confirmed both with chemical cross-linking agents as well as through endogenous cross-linking mediated by transglutaminase. Our results clearly show that VR1 forms multimers in each of the expression systems with a homotetramer as a predominant form. The oligomeric structure of VR1 may contribute to the complexity of VR1 pharmacology. Finally, differences in glycosylation between the systems were observed, indicating the need for caution in the use of the heterologous expression systems for analysis of VR1 properties.
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Cites
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Impaired nociception and pain sensation in mice lacking the capsaicin receptor
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The Cloned Capsaicin Receptor Integrates Multiple Pain-Producing Stimuli
Tominaga, M., Caterina, M. J., Malmberg, A. B., Rosen, T. A., Gilbert, H., Skinner, K., Raumann, B. E., Basbaum, A. I., & Julius, D. (1998) · Neuron · doi:10.1016/s0896-6273(00)80564-4 · Cited by 3,081
Vanilloid receptor-1 is essential for inflammatory thermal hyperalgesia
Davis, J. B., Gray, J., Gunthorpe, M. J., Hatcher, J. P., Davey, P. T., Overend, P., Harries, M. H., Latcham, J., Clapham, C., Atkinson, K., et al. (2000) · Nature · doi:10.1038/35012076 · Cited by 1,760
A capsaicin-receptor homologue with a high threshold for noxious heat
Caterina, M. J., Rosen, T. A., Tominaga, M., Brake, A. J., & Julius, D. (1999) · Nature · doi:10.1038/18906 · Cited by 1,603
Structure and Function of Voltage-Sensitive Ion Channels
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Cited by
Brauchi, S., Orio, P., & Latorre, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406773101 · Cited by 375
The ion channel TRPV1 regulates the activation and proinflammatory properties of CD4+ T cells
Bertin, S., Aoki-Nonaka, Y., de Jong, P. R., Nohara, L. L., Xu, H., Stanwood, S. R., Srikanth, S., Lee, J., To, K., Abramson, L., et al. (2014) · Nature Immunology · doi:10.1038/ni.3009 · Cited by 260
Dimerization of Human XPA and Formation of XPA2−RPA Protein Complex
Yang, Z.-G., Liu, Y., Mao, L. Y., Zhang, J.-T., & Zou, Y. (2002) · Biochemistry · doi:10.1021/bi026064z · Cited by 70
Metadata
- Authors
- Kedei, N., Szabo, T., Lile, J. D., Treanor, J. J., Olah, Z., Iadarola, M. J., & Blumberg, P. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-07
- Volume
- 276
- Issue
- 30
- Pages
- 28613-28619
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2059742450
- Cited by
- 313
- References
- 38
- FWCI
- 11.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kedei, N., Szabo, T., Lile, J. D., Treanor, J. J., Olah, Z., Iadarola, M. J., & Blumberg, P. M. (2001). Analysis of the Native Quaternary Structure of Vanilloid Receptor 1. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m103272200
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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