The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The Transient Receptor Potential Protein Homologue TRP6 Is the Essential Component of Vascular α1-Adrenoceptor–Activated Ca2+-Permeable Cation Channel
Open accessAbstract
Abstract—The Drosophila transient receptor potential protein (TRP) and its mammalian homologues are thought to be Ca 2+-permeable cation channels activated by G protein (G q/11)–coupled receptors and are regarded as an interesting molecular model for the Ca 2+entry mechanisms associated with stimulated phosphoinositide turnover and store depletion. However, there is little unequivocal evidence linking mammalian TRPs with particular native functions. In this study, we have found that heterologous expression of murine TRP6 in HEK293 cells reproduces almost exactly the essential biophysical and pharmacological properties of α 1-adrenoceptor–activated nonselective cation channels (α 1-AR–NSCC) previously identified in rabbit portal vein smooth muscle. Such properties include activation by diacylglycerol; S-shaped current-voltage relationship; high divalent cation permeability; unitary conductance of 25 to 30 pS and augmentation by flufenamate and Ca 2+; and blockade by Cd 2+, La 3+, Gd 3+, SK&F96365, and amiloride. Reverse transcriptase–polymerase chain reaction and confocal laser scanning microscopy using TRP6-specific primers and antisera revealed that the level of TRP6 mRNA expression was remarkably high in both murine and rabbit portal vein smooth muscles as compared with other TRP subtypes, and the immunoreactivity to TRP6 protein was localized near the sarcolemmal region of single rabbit portal vein myocytes. Furthermore, treatment of primary cultured portal vein myocytes with TRP6 antisense oligonucleotides resulted in marked inhibition of TRP6 protein immunoreactivity as well as selective suppression of α 1-adrenoceptor–activated, store depletion–independent cation current and Ba 2+influx. These results strongly indicate that TRP6 is the essential component of the α 1-AR–NSCC, which may serve as a store depletion–independent Ca 2+entry pathway during increased sympathetic activity.
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Citations
Cites
Activation of a TRPC3-Dependent Cation Current through the Neurotrophin BDNF
Li, H.-S., Xu, X.-Z. S., & Montell, C. (1999) · Neuron · doi:10.1016/s0896-6273(00)80838-7 · Cited by 345
Cited by
TRP channels as cellular sensors
Clapham, D. E. (2003) · Nature · doi:10.1038/nature02196 · Cited by 2,779
Store-Operated Calcium Channels
Parekh, A. B., & Putney, J. W. (2005) · Physiological Reviews · doi:10.1152/physrev.00057.2003 · Cited by 2,089
The TRP Superfamily of Cation Channels
Montell, C. (2005) · Science's STKE · doi:10.1126/stke.2722005re3 · Cited by 989
Zhang, M., Ma, Y., Ye, X., Zhang, N., Pan, L., & Wang, B. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01464-x · Cited by 522
TRPV2 Is a Component of Osmotically Sensitive Cation Channels in Murine Aortic Myocytes
Muraki, K., Iwata, Y., Katanosaka, Y., Ito, T., Ohya, S., Shigekawa, M., & Imaizumi, Y. (2003) · Circulation Research · doi:10.1161/01.res.0000097263.10220.0c · Cited by 521
Metadata
- Authors
- Inoue, R., Okada, T., Onoue, H., Hara, Y., Shimizu, S., Naitoh, S., Ito, Y., & Mori, Y.
- Venue
- Circulation Research
- Published
- 2001-02-16
- Volume
- 88
- Issue
- 3
- Pages
- 325-332
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- OpenAlex
- W2166046655
- Cited by
- 596
- References
- 1
- FWCI
- 18.90
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Inoue, R., Okada, T., Onoue, H., Hara, Y., Shimizu, S., Naitoh, S., Ito, Y., & Mori, Y. (2001). The Transient Receptor Potential Protein Homologue TRP6 Is the Essential Component of Vascular α1-Adrenoceptor–Activated Ca2+-Permeable Cation Channel. Circulation Research. https://doi.org/10.1161/01.res.88.3.325
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