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Pharmacological Reports
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publication venue for: Modulation of the voltage-gated potassium channel Kv2.1 by the anti-tumor alkylphospholipid perifosine
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type: Generically Dependent Continuant
type: Collection
type: Information Content Entity
type: Periodical

Continuant
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Entity
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Generically Dependent Continuant
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RDF description of Modulation of the voltage-gated potassium channel Kv2.1 by the anti-tumor alkylphospholipid perifosine - http://orbis.uaslp.mx/vivo/individual/scopus4507
rights: termsOfUse
date: 2026-08-24T21:45:46
publisher: vivo
type: Document

Article
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Consejo Nacional de Ciencia y Tecnología, CONACYT
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type: BFO_0000020
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type: Thing
type: Grant
type: Continuant
funding vehicle for: Modulation of the voltage-gated potassium channel Kv2.1 by the anti-tumor alkylphospholipid perifosine

157245
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type: BFO_0000020
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type: Grant
type: Continuant
funding vehicle for: Modulation of the voltage-gated potassium channel Kv2.1 by the anti-tumor alkylphospholipid perifosine

Information Content Entity
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Modulation of the voltage-gated potassium channel Kv2.1 by the anti-tumor alkylphospholipid perifosine
manufactures: Sigma Aldrich, United States
related by: authorship_26409
related by: authorship_26404
abstract: Background The aim of the present study was to assess the effects of perifosine - a third generation alkylphospholipid analog with anti-tumor properties - on the activity of Kv2.1 channels. Methods The whole-cell patch clamp technique was applied to follow the modulatory effect of perifosine on Kv2.1 channels expressed in HEK293 cells. Results Obtained data provide evidence that perifosine application decreases the whole cell Kv2.1 currents in a concentration-independent manner. Perifosine induces a hyperpolarizing shift in the voltage dependence of Kv2.1 channels inactivation without altering the voltage dependence of channels activation. The kinetics of Kv2.1 closed-state inactivation was accelerated by perifosine, with no significant effects on the recovery rate from inactivation. Conclusions Taken together, these results show that perifosine modified the Kv2.1 inactivation gating resulting in a decrease of the current amplitude. These data will help to elucidate the mechanism of action of this promising anti-cancer drug on ion channels and their possible implications. © 2015 Institute of Pharmacology, Polish Academy of Sciences. Published by Elsevier Sp. z o.o. All rights reserved.
has funding vehicle: Consejo Nacional de Ciencia y Tecnología, CONACYT
type: Information Content Entity
estado: published
type: Article
pmid: 26922553
related by: authorship_26407
type: Thing
page end: 461
doi: 10.1016/j.pharep.2015.11.006
volume: 68
freetext keyword: Alkylphospholipid; Kv2.1; Perifosine; Potassium channels perifosine; unclassified drug; voltage gated potassium channel; voltage gated potassium channel Kv2.1; antineoplastic agent; KCNB1 protein, human; perifosine; phosphorylcholine; potassium; Shab potassium channel; voltage gated potassium channel; antineoplastic activity; Article; concentration (parameters); controlled study; drug effect; electric potential; embryo; human; human cell; modulation; voltage clamp technique; whole cell patch clamp; analogs and derivatives; cell line; channel gating; drug effects; HEK293 cell line; kinetics; membrane potential; metabolism; patch clamp technique; procedures; Antineoplastic Agents; Cell Line; HEK293 Cells; Humans; Ion Channel Gating; Kinetics; Membrane Potentials; Patch-Clamp Techniques; Phosphorylcholine; Potassium; Potassium Channels, Voltage-Gated; Shab Potassium Channels
related by: authorship_26405
related by: authorship_26408
type: Document
type: Generically Dependent Continuant
most specific type: Document
has funding vehicle: 157245
type: Continuant
related by: authorship_26406
chemicalscas: perifosine, 157716-52-4; phosphorylcholine, 107-73-3; potassium, 7440-09-7; Antineoplastic Agents; KCNB1 protein, human; perifosine; Phosphorylcholine; Potassium; Potassium Channels, Voltage-Gated; Shab Potassium Channels
crisid: 4508
origen: scopus
most specific type: Article
e iscopus: 2-s2.0-84970917667
issue: 2
page start: 457
type: Entity
date time value: article date 4508
has publication venue: Pharmacological Reports