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Characterization and photoaffinity labeling of receptor sites for the Ca2+ channel inhibitors d-cis-diltiazem, (+/-)-bepridil, desmethoxyverapamil, and (+)-PN 200-110 in skeletal muscle transverse tubule membranes.
Open accessAbstract
In order to further understand the molecular nature of the voltage-sensitive Ca2+ channel in skeletal muscle, we have performed classical radioligand binding studies and photoaffinity labeling with different types of tritiated inhibitors of the Ca2+ channel. The equilibrium dissociation constants (KD) for (-)-[3H]desmethoxyverapamil, d-cis-[3H]diltiazem, and (+/-)-[3H]bepridil at their receptor sites in skeletal muscle transverse tubule membranes are: 1.5 +/- 0.5, 50 +/- 5, and 20 +/- 5 nM, respectively. Maximum binding capacities in picomoles/milligram of protein were: 70 +/- 10 for (-)-[3H]desmethoxyverapamil, 50 +/- 15 for d-cis-[3H]diltiazem, and 75 +/- 15 for (+/-)-[3H]bepridil. The kinetics of association at 10 degrees C for the three types of tritiated compounds were relatively slow (3 X 10(5) M-1 S-1 for (-)-[3H]desmethoxyverapamil, 8 X 10(3) M-1 S-1 for d-cis-[3H]diltiazem, and 4.2 X 10(5) M-1 S-1 for (+/-)-[3H]bepridil). The dissociation of (-)-[3H]desmethoxyverapamil and d-cis-[3H]diltiazem from their receptor sites was also a slow process with half-lives of dissociation of 33 and 36 min, respectively. Competition studies using the three tritiated ligands suggest that they bind to the same receptor site which appears to be in a 1:1 stoichiometry with the dihydropyridine receptor. Photoaffinity labeling with high intensity ultraviolet light in the presence of (+/-)-[3H]bepridil or d-cis[3H]diltiazem resulted in the specific covalent incorporation of radioactivity into a polypeptide of Mr 170,000 +/- 10,000. A polypeptide of Mr 170,000 was also specifically labeled in photoaffinity labeling experiments using the high affinity dihydropyridine derivative (+)-[3H]PN 200-100.
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Citations
Cited by
Stys, P., Waxman, S., & Ransom, B. (1992) · The Journal of Neuroscience · doi:10.1523/jneurosci.12-02-00430.1992 · Cited by 662
Subunit structure of dihydropyridine-sensitive calcium channels from skeletal muscle.
Takahashi, M., Seagar, M. J., Jones, J. F., Reber, B. F., & Catterall, W. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5478 · Cited by 473
Regulation of cardiac ion channels by catecholamines, acetylcholine and second messenger systems
Hartzell, H. C. (1988) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(88)90014-4 · Cited by 398
Agrawal, S., & Fehlings, M. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-02-00545.1996 · Cited by 279
Metadata
- Authors
- Galizzi, J. P., Borsotto, M., Barhanin, J., Fosset, M., & Lazdunski, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-01
- Volume
- 261
- Issue
- 3
- Pages
- 1393-1397
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1563654697
- Cited by
- 190
- References
- 0
- FWCI
- 15.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Characterization and photoaffinity labeling of receptor sites for the Ca2+ channel inhibitors d-cis-diltiazem, (+/-)-bepridil, desmethoxyverapamil, and (+)-PN 200-110 in skeletal muscle transverse tubule membranes. https://app.cochat.ai/papers/10.1016/s0021-9258(17)36105-7
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- Galizzi, J. P., Borsotto, M., Barhanin, J., Fosset, M., & Lazdunski, M. (1986). Characterization and photoaffinity labeling of receptor sites for the Ca2+ channel inhibitors d-cis-diltiazem, (+/-)-bepridil, desmethoxyverapamil, and (+)-PN 200-110 in skeletal muscle transverse tubule membranes. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)36105-7
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