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T-cell dependency on Kv1.3 or KCa3.1 might be irreversibly modulated by antigen exposure.
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In this work, we showed that although both Kv1.1 and Kv1.3 channels are expressed in U87 (glioblastoma), MDA-MB-231 (breast cancer) and LS174 (colon adenocarcinoma) cells, these respond differently to KAaH1 or KAaH2, two homologous Kv1 blockers from scorpion venom
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Kv1.3 methylation may serve as diagnostic and prognostic markers in colorectal cancer.
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the tertiary structure of the C-terminal domain of Kv1.3 is necessary and sufficient for Kv1.3- KCNE4 interaction.
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results identify a caveolin-binding domain in Kv1 channels and highlight the mechanisms that govern the regulation of channel surface localization during cellular processes
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we report that Kv1.3-NPs reduced NFAT activation and CD40L expression exclusively in CD45RO(+) T cells. Furthermore, Kv1.3-NPs suppressed cytokine release and induced a phenotype switch of T cells from predominantly memory to naive.
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The implication of Kv1.3 in a wide repertoire of human pathologies indicates this channel is an important therapeutic target.
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Results contribute to the characterization of leukemic B cells, as it shows that upregulation of Kv1.3 in pathologic B lymphocytes is linked to the oncogenic B-RAF signaling.
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Data suggest that C-terminus is necessary for Kv1.3-induced cell proliferation; the mechanism involves accessibility of key docking sites at the C terminus; phosphorylation of Tyr-447 by MAP kinase signal cascade appears crucial.
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concluded that Kv1.3 may stimulate macrophage migration through the activation of ERK.
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The inhibition of Kv1.3 channels might be involved in antiproliferative and proapoptotic effects of the compounds observed in cancer cell lines expressing these channels.
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Kv1.3 channels modulate human vascular smooth muscle cells proliferation independently of mTOR signaling pathway.
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actin dynamics regulates the membrane motility of Kv1.3 channels.
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The increment and decrement of the basic residue number in a positively charged S4 sensor of Kv1.3 channel yields conductance-voltage relationship curves in the positive direction by approximately 31.2 mV and 2-4 mV
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the association between Kv1.3 and the COPII cargo adaptor subunit isoform Sec24a
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Findings reveal that alpha-defensins are endogenous inhibitors of potassium voltage-gated channel subfamily A member 3 (Kv1.3) with distinct interaction mechanisms.
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JAK2 participates in the signalling, regulating the voltage-gated K(+) channel KCNA3.
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This study demonstrated that Potassium channel Kv1.3 is highly expressed by microglia in human Alzheimer's disease.
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These results demonstrate that Kv1.3 channels are primarily localized in the nucleus of several types of cancer cells and human brain tissues where they are capable of regulating nuclear membrane potential and activation of transcription factors
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the small molecule Kv1.3 blocker PAP-1 dose-dependently inhibited proliferation and suppressed IL-2 and IFN-gamma production.