| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-142 |
Sentence |
denotes |
GRK2 protein-mediated transphosphorylation contributes to loss of function of μ-opioid receptors induced by neuropeptide FF (NPFF2) receptors. |
| T1 |
0-142 |
Sentence |
denotes |
GRK2 protein-mediated transphosphorylation contributes to loss of function of μ-opioid receptors induced by neuropeptide FF (NPFF2) receptors. |
| TextSentencer_T2 |
143-259 |
Sentence |
denotes |
Neuropeptide FF (NPFF) interacts with specific receptors to modulate opioid functions in the central nervous system. |
| T2 |
143-259 |
Sentence |
denotes |
Neuropeptide FF (NPFF) interacts with specific receptors to modulate opioid functions in the central nervous system. |
| TextSentencer_T3 |
260-483 |
Sentence |
denotes |
On dissociated neurons and neuroblastoma cells (SH-SY5Y) transfected with NPFF receptors, NPFF acts as a functional antagonist of μ-opioid (MOP) receptors by attenuating the opioid-induced inhibition of calcium conductance. |
| T3 |
260-483 |
Sentence |
denotes |
On dissociated neurons and neuroblastoma cells (SH-SY5Y) transfected with NPFF receptors, NPFF acts as a functional antagonist of μ-opioid (MOP) receptors by attenuating the opioid-induced inhibition of calcium conductance. |
| TextSentencer_T4 |
484-564 |
Sentence |
denotes |
In the SH-SY5Y model, MOP and NPFF(2) receptors have been shown to heteromerize. |
| T4 |
484-564 |
Sentence |
denotes |
In the SH-SY5Y model, MOP and NPFF(2) receptors have been shown to heteromerize. |
| TextSentencer_T5 |
565-771 |
Sentence |
denotes |
To understand the molecular mechanism involved in the anti-opioid activity of NPFF, we have investigated the phosphorylation status of the MOP receptor using phospho-specific antibody and mass spectrometry. |
| T5 |
565-771 |
Sentence |
denotes |
To understand the molecular mechanism involved in the anti-opioid activity of NPFF, we have investigated the phosphorylation status of the MOP receptor using phospho-specific antibody and mass spectrometry. |
| TextSentencer_T6 |
772-976 |
Sentence |
denotes |
Similarly to direct opioid receptor stimulation, activation of the NPFF(2) receptor by [D-Tyr-1-(NMe)Phe-3]NPFF (1DMe), an analog of NPFF, induced the phosphorylation of Ser-377 of the human MOP receptor. |
| T6 |
772-976 |
Sentence |
denotes |
Similarly to direct opioid receptor stimulation, activation of the NPFF(2) receptor by [D-Tyr-1-(NMe)Phe-3]NPFF (1DMe), an analog of NPFF, induced the phosphorylation of Ser-377 of the human MOP receptor. |
| TextSentencer_T7 |
977-1193 |
Sentence |
denotes |
This heterologous phosphorylation was unaffected by inhibition of second messenger-dependent kinases and, contrarily to homologous phosphorylation, was prevented by inactivation of G(i/o) proteins by pertussis toxin. |
| T7 |
977-1193 |
Sentence |
denotes |
This heterologous phosphorylation was unaffected by inhibition of second messenger-dependent kinases and, contrarily to homologous phosphorylation, was prevented by inactivation of G(i/o) proteins by pertussis toxin. |
| TextSentencer_T8 |
1194-1371 |
Sentence |
denotes |
Using siRNA knockdown we could demonstrate that 1DMe-induced Ser-377 cross-phosphorylation and MOP receptor loss of function were mediated by the G protein receptor kinase GRK2. |
| T8 |
1194-1371 |
Sentence |
denotes |
Using siRNA knockdown we could demonstrate that 1DMe-induced Ser-377 cross-phosphorylation and MOP receptor loss of function were mediated by the G protein receptor kinase GRK2. |
| TextSentencer_T9 |
1372-1692 |
Sentence |
denotes |
In addition, mass spectrometric analysis revealed that the phosphorylation pattern of MOP receptors was qualitatively similar after treatment with the MOP agonist Tyr-D-Ala-Gly (NMe)-Phe-Gly-ol (DAMGO) or after treatment with the NPFF agonist 1DMe, but the level of multiple phosphorylation was more intense after DAMGO. |
| T9 |
1372-1692 |
Sentence |
denotes |
In addition, mass spectrometric analysis revealed that the phosphorylation pattern of MOP receptors was qualitatively similar after treatment with the MOP agonist Tyr-D-Ala-Gly (NMe)-Phe-Gly-ol (DAMGO) or after treatment with the NPFF agonist 1DMe, but the level of multiple phosphorylation was more intense after DAMGO. |
| TextSentencer_T10 |
1693-1826 |
Sentence |
denotes |
Finally, NPFF(2) receptor activation was sufficient to recruit β-arrestin2 to the MOP receptor but not to induce its internalization. |
| T10 |
1693-1826 |
Sentence |
denotes |
Finally, NPFF(2) receptor activation was sufficient to recruit β-arrestin2 to the MOP receptor but not to induce its internalization. |
| TextSentencer_T11 |
1827-2015 |
Sentence |
denotes |
These data show that NPFF-induced heterologous desensitization of MOP receptor signaling is mediated by GRK2 and could involve transphosphorylation within the heteromeric receptor complex. |
| T11 |
1827-2015 |
Sentence |
denotes |
These data show that NPFF-induced heterologous desensitization of MOP receptor signaling is mediated by GRK2 and could involve transphosphorylation within the heteromeric receptor complex. |
