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| Nikolai M. Soldatov, Ph.D., Investigator Molecular and Clinical Pharmacology Section |
 Dr. Nikolai Soldatov received his Ph.D. degree in bioorganic chemistry in 1981 from Shemyakin Institute of Bioorganic Chemistry of the USSR Academy of Sciences, Moscow. In 1983, while on postdoctoral training in Shemyakin Institute, he initiated research directed to the identification and isolation of skeletal muscle dihydropyridine-sensitive calcium channel. In 1986 he joined the Institute of Medical Biotechnology led by cosmonaut Prof. B. Egorov and studied the relationship between calcium channels and primary and secondary messengers of human fibroblasts proliferation and memory, learning and nootropic effects in the brain. In 1990 he joined the laboratory of Dr. G. Blobel at the Rockefeller University, New York, as a HHMI Research Associate. He cloned the first human L-type calcium channel from fibroblasts and investigated its genomic structure. Since 1993 he has worked as an Assistant at the Department of Pharmacology of the University of Bern, Switzerland. He constructed a representative panel of human calcium channel splice variants and investigated, in collaboration with Prof. H. Reuter, their pharmacological and electrophysiological properties. In 1996 he moved to Georgetown University Medical Center, Washington, D.C., where he worked as an Assistant Professor of the Department of Pharmacology. He studied mechanisms of voltage- and calcium-induced inactivation, and the role of C-terminal tail of the channel in calcium signaling. In July 1999 Dr. Soldatov joined NIA as an Investigator. He is an adjunct Associate Professor at Georgetown University. |
| Research Interests: Calcium Sensitivity of Calcium Channel: The voltage-gated L-type Ca2+ channel is inhibited by Ca2+ but not Ba2+ ions on the cytoplasmic side of the pore. This Ca2+-induced inactivation serves as an important feedback mechanism against Ca2+ overloading of the cell. We found that the 650-amino acid carboxyl-terminal tail of the channel is critically important for the feedback. Our studies showed that Ca2+-induced inactivation of the L-type Ca2+ channel and its modulation by calmodulin is differentially mediated by two short carboxyl-terminal motifs. One of these motifs is a Ca2+ sensor site that binds calmodulin at low resting free Ca2+ concentration. Increase in Ca2+ concentration causes release of calmodulin from this motif and in turn stimulates its binding to the IQ-region of the adjacent motif. These data imply that Ca2+-dependent transfer of calmodulin between the two spatially close binding sites leads to Ca2+-induced inactivation of the channel. Further investigation of this region by NMR spectrometry and electron diffraction will allow us to compare involved structural determinants which may lead to development of new drugs. |
| Contact Information: Laboratory of Clinical Investigation Gerontology Research Center 5600 Nathan Shock Drive Baltimore, MD 21224-6825 Phone 410-558-8343 Fax 410-558-8318 E mail soldatovn@grc.nia.nih.gov For more information about the Laboratory: http://www.grc.nia.nih.gov/branches/lci/lci.htm |
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