Sodium channel activity in leukemia cells is directly controlled by actin polymerization

Negulyaev YA, Khaitlina SY, Hinssen H, Shumilina EV, Vedernikova EA (2000)
JOURNAL OF BIOLOGICAL CHEMISTRY 275(52): 40933-40937.

Download
No fulltext has been uploaded. References only!
Journal Article | Original Article | Published | English

No fulltext has been uploaded

Author
; ; ; ;
Abstract / Notes
The actin cytoskeleton has been shown to be involved in the regulation of sodium-selective channels in nonexcitable cells. However, the molecular mechanisms underlying the changes in channel function remain to be defined. In the present work, inside-out patch experiments were employed to elucidate the role of submembranous actin dynamics in the control of sodium channels in human myeloid leukemia K562 cells. We found that the application of cytochalasin D to the cytoplasmic surface of membrane fragments resulted in activation of non-voltage-gated sodium channels of 12 picosiemens conductance. Similar effects could be evoked by addition of the actin-severing protein gelsolin to the bath cytosol-like solution containing 1 muM [Ca2+](i). The sodium channel activity induced by disassembly of submembranous microfilaments with cytochalasin D or gelsolin could be abolished by intact actin added to the bath cytosol-like solution in the presence of 1 mM MgCl2, to induce actin polymerization, In the absence of MgCl2, addition of intact actin did not abolish the channel activity. Moreover, the sodium currents were unaffected by heat-inactivated actin or by actin whose polymerizability was strongly reduced by cleavage with specific Escherichia coli A2 protease ECP32, Thus, the inhibitory effect of actin on channel activity was observed only under conditions promoting rapid polymerization. Taken together, our data show that sodium channels are directly controlled by dynamic assembly and disassembly of submembranous F-actin.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Negulyaev YA, Khaitlina SY, Hinssen H, Shumilina EV, Vedernikova EA. Sodium channel activity in leukemia cells is directly controlled by actin polymerization. JOURNAL OF BIOLOGICAL CHEMISTRY. 2000;275(52):40933-40937.
Negulyaev, Y. A., Khaitlina, S. Y., Hinssen, H., Shumilina, E. V., & Vedernikova, E. A. (2000). Sodium channel activity in leukemia cells is directly controlled by actin polymerization. JOURNAL OF BIOLOGICAL CHEMISTRY, 275(52), 40933-40937. doi:10.1074/jbc.M008219200
Negulyaev, Y. A., Khaitlina, S. Y., Hinssen, H., Shumilina, E. V., and Vedernikova, E. A. (2000). Sodium channel activity in leukemia cells is directly controlled by actin polymerization. JOURNAL OF BIOLOGICAL CHEMISTRY 275, 40933-40937.
Negulyaev, Y.A., et al., 2000. Sodium channel activity in leukemia cells is directly controlled by actin polymerization. JOURNAL OF BIOLOGICAL CHEMISTRY, 275(52), p 40933-40937.
Y.A. Negulyaev, et al., “Sodium channel activity in leukemia cells is directly controlled by actin polymerization”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 275, 2000, pp. 40933-40937.
Negulyaev, Y.A., Khaitlina, S.Y., Hinssen, H., Shumilina, E.V., Vedernikova, E.A.: Sodium channel activity in leukemia cells is directly controlled by actin polymerization. JOURNAL OF BIOLOGICAL CHEMISTRY. 275, 40933-40937 (2000).
Negulyaev, YA, Khaitlina, SY, Hinssen, Horst, Shumilina, EV, and Vedernikova, EA. “Sodium channel activity in leukemia cells is directly controlled by actin polymerization”. JOURNAL OF BIOLOGICAL CHEMISTRY 275.52 (2000): 40933-40937.
This data publication is cited in the following publications:
This publication cites the following data publications:

15 Citations in Europe PMC

Data provided by Europe PubMed Central.

Serum- and glucocorticoid-inducible kinase SGK1 regulates reorganization of actin cytoskeleton in mast cells upon degranulation.
Schmid E, Gu S, Yang W, Münzer P, Schaller M, Lang F, Stournaras C, Shumilina E., Am J Physiol Cell Physiol 304(1), 2013
PMID: 23015548
Role of submembranous actin cytoskeleton in regulation of non-voltage-gated sodium channels.
Chubinskiy-Nadezhdin VI, Sudarikova AV, Nikolsky NN, Morachevskaya EA., Dokl Biochem Biophys 450(), 2013
PMID: 23824452
Common mechanisms regulating cell cortex properties during cell division and cell migration.
Roubinet C, Tran PT, Piel M., Cytoskeleton (Hoboken) 69(11), 2012
PMID: 23125194
Heat shock protein DnaK--substrate of actin-specific bacterial protease ECP32.
Morozova AV, Khaitlina SY, Malinin AY., Biochemistry (Mosc) 76(4), 2011
PMID: 21585321
Properties of Mg(2+)-dependent cation channels in human leukemia K562 cells.
Semenova SB, Fomina AF, Vassilieva IO, Negulyaev YA., J Cell Physiol 205(3), 2005
PMID: 15895364
Increased focal Kv4.2 channel expression at the plasma membrane is the result of actin depolymerization.
Wang Z, Eldstrom JR, Jantzi J, Moore ED, Fedida D., Am J Physiol Heart Circ Physiol 286(2), 2004
PMID: 14551056
Hydrogen-deuterium exchange effects on beta-endorphin release from AtT20 murine pituitary tumor cells.
Ikeda M, Suzuki S, Kishio M, Hirono M, Sugiyama T, Matsuura J, Suzuki T, Sota T, Allen CN, Konishi S, Yoshioka T., Biophys J 86(1 pt 1), 2004
PMID: 14695301
Syntrophin gamma 2 regulates SCN5A gating by a PDZ domain-mediated interaction.
Ou Y, Strege P, Miller SM, Makielski J, Ackerman M, Gibbons SJ, Farrugia G., J Biol Chem 278(3), 2003
PMID: 12429735
Sodium loading changes urinary protein excretion: a proteomic analysis.
Thongboonkerd V, Klein JB, Pierce WM, Jevans AW, Arthur JM., Am J Physiol Renal Physiol 284(6), 2003
PMID: 12582004
Regulation of sodium channel activity by capping of actin filaments.
Shumilina EV, Negulyaev YA, Morachevskaya EA, Hinssen H, Khaitlina SY., Mol Biol Cell 14(4), 2003
PMID: 12686620
Non-hydrolyzable analog of GTP induces activity of Na+ channels via disassembly of cortical actin cytoskeleton.
Shumilina EV, Khaitlina SY, Morachevskaya EA, Negulyaev YA., FEBS Lett 547(1-3), 2003
PMID: 12860381
CFTR in K562 human leukemic cells.
Assef YA, Damiano AE, Zotta E, Ibarra C, Kotsias BA., Am J Physiol Cell Physiol 285(2), 2003
PMID: 12842835

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 11016945
PubMed | Europe PMC

Search this title in

Google Scholar