302 research outputs found
Change of electrical pain threshold as percentage of pre-intervention values after BreEStim and EStim.
<p>Average values and standard errors are presented.</p
The intensity of electrical stimulation from beginning (trial 0) to the end (trial 120) during BreEStim and EStim.
<p>Average values and standard errors are presented.</p
Electrical pain thresholds pre- and post-BreEStim (upper panel) and pre- and post-EStim (lower panel) in all four tested sites on both stimulated and non-stimulated side.
<p>Average values and standard errors are shown.</p
Electrical sensation threshold and electrical pain threshold from the thenar and hypothenar eminences of the treatment (dominant) and non-treatment (non-dominant) hands before and after BreEStim and EStim.
<p>Bold numbers indicate significant difference from pre-treatment measurements.</p
PKC-Mediated USP Phosphorylation at Ser35 Modulates 20-Hydroxyecdysone Signaling in <i>Drosophila</i>
The nuclear receptor complex of the steroid hormone,
20-hydroxyecdysone
(20E), is a heterodimer composed of EcR and USP. Our previous studies
in <i>Drosophila</i> suggest that PKC modulates 20E signaling
by phosphorylating EcR-USP. However, the exact phosphorylation sites
in EcR and USP have not been identified. Using LC–MS/MS analysis,
we first identified Ser35 of USP as a PKC phosphorylation site. Mutation
of USP Ser35 to Ala35 in S2 cells not only eliminated USP phosphorylation,
but also attenuated the 20E-induced luciferase activity, mimicking
the treatment with a PKC-specific inhibitor chelerythrine chloride
in Kc cells. In the larval salivary glands (SG), inhibition of PKC
activity with the binary GAL4/UAS system reduced USP phosphorylation
and down-regulated the 20E primary-response genes, <i>E75B</i> and <i>Br-C</i>, and RNAi knockdown of <i>Rack1</i> had stronger inhibitory effects than overexpression of <i>PKCi</i>. Moreover, RNAi knockdown of four PKC isozyme genes expressed in
the SG exhibited a variety of inhibitory effects on USP phosphorylation
and expression of <i>E75B</i> and <i>Br-C</i>,
with the strongest inhibitory effects occurring when <i>aPKC</i> was knocked down by RNAi. Taken together, we conclude that PKC-mediated
USP phosphorylation at Ser35 modulates 20E signaling in <i>Drosophila</i>
PKC-Mediated USP Phosphorylation at Ser35 Modulates 20-Hydroxyecdysone Signaling in <i>Drosophila</i>
The nuclear receptor complex of the steroid hormone,
20-hydroxyecdysone
(20E), is a heterodimer composed of EcR and USP. Our previous studies
in <i>Drosophila</i> suggest that PKC modulates 20E signaling
by phosphorylating EcR-USP. However, the exact phosphorylation sites
in EcR and USP have not been identified. Using LC–MS/MS analysis,
we first identified Ser35 of USP as a PKC phosphorylation site. Mutation
of USP Ser35 to Ala35 in S2 cells not only eliminated USP phosphorylation,
but also attenuated the 20E-induced luciferase activity, mimicking
the treatment with a PKC-specific inhibitor chelerythrine chloride
in Kc cells. In the larval salivary glands (SG), inhibition of PKC
activity with the binary GAL4/UAS system reduced USP phosphorylation
and down-regulated the 20E primary-response genes, <i>E75B</i> and <i>Br-C</i>, and RNAi knockdown of <i>Rack1</i> had stronger inhibitory effects than overexpression of <i>PKCi</i>. Moreover, RNAi knockdown of four PKC isozyme genes expressed in
the SG exhibited a variety of inhibitory effects on USP phosphorylation
and expression of <i>E75B</i> and <i>Br-C</i>,
with the strongest inhibitory effects occurring when <i>aPKC</i> was knocked down by RNAi. Taken together, we conclude that PKC-mediated
USP phosphorylation at Ser35 modulates 20E signaling in <i>Drosophila</i>
PKC-Mediated USP Phosphorylation at Ser35 Modulates 20-Hydroxyecdysone Signaling in <i>Drosophila</i>
The nuclear receptor complex of the steroid hormone,
20-hydroxyecdysone
(20E), is a heterodimer composed of EcR and USP. Our previous studies
in <i>Drosophila</i> suggest that PKC modulates 20E signaling
by phosphorylating EcR-USP. However, the exact phosphorylation sites
in EcR and USP have not been identified. Using LC–MS/MS analysis,
we first identified Ser35 of USP as a PKC phosphorylation site. Mutation
of USP Ser35 to Ala35 in S2 cells not only eliminated USP phosphorylation,
but also attenuated the 20E-induced luciferase activity, mimicking
the treatment with a PKC-specific inhibitor chelerythrine chloride
in Kc cells. In the larval salivary glands (SG), inhibition of PKC
activity with the binary GAL4/UAS system reduced USP phosphorylation
and down-regulated the 20E primary-response genes, <i>E75B</i> and <i>Br-C</i>, and RNAi knockdown of <i>Rack1</i> had stronger inhibitory effects than overexpression of <i>PKCi</i>. Moreover, RNAi knockdown of four PKC isozyme genes expressed in
the SG exhibited a variety of inhibitory effects on USP phosphorylation
and expression of <i>E75B</i> and <i>Br-C</i>,
with the strongest inhibitory effects occurring when <i>aPKC</i> was knocked down by RNAi. Taken together, we conclude that PKC-mediated
USP phosphorylation at Ser35 modulates 20E signaling in <i>Drosophila</i>
Quantitative measurement of thresholds for both dominant (DH) and non-dominant (NDH) hands before and after BreEStim and EStim.
<p>Quantitative measurement of thresholds for both dominant (DH) and non-dominant (NDH) hands before and after BreEStim and EStim.</p
Change of electrical pain threshold as percentage of pre-intervention values after BreEStim and EStim.
<p>Standard errors are presented.</p
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