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Amylin evokes phosphorylation of P20 in rat skeletal muscle
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , |
| In: | FEBS Letters, 457, 1999, 1, S. 149-152 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Wang, Yu Xu, Aimin Cooper, Garth J.S Wang, Yu Xu, Aimin Cooper, Garth J.S |
|---|---|
| author |
Wang, Yu Xu, Aimin Cooper, Garth J.S |
| spellingShingle |
Wang, Yu Xu, Aimin Cooper, Garth J.S FEBS Letters Amylin evokes phosphorylation of P20 in rat skeletal muscle Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
wang, yu |
| spelling |
Wang, Yu Xu, Aimin Cooper, Garth J.S 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(99)01029-7 <jats:p>To investigate the signal transduction events underlying amylin's actions, the amylin‐evoked protein phosphorylation cascade was analysed using two‐dimensional gel electrophoresis. We found that phosphorylation of three isoelectric variants of P20 (termed ARPP1, ARPP2 and ARPP3) was associated with amylin's actions in rat skeletal muscle. Amylin decreased phosphorylation of ARPP1 and increased phosphorylation of ARPP2 and ARPP3 in a dose‐dependent manner. Insulin inhibited amylin‐evoked phosphorylation of ARPP2 and ARPP3. The amylin‐selective antagonist rat amylin‐(8–37) completely reversed amylin's action on ARPP3 and partially decreased phosphorylation of ARPP2. By contrast, the CGRP‐selective antagonist, human CGRP‐(8–37) blocked phosphorylation of ARPP2 but had little effect on ARPP3. These results suggest that amylin modifies phosphorylation of P20 via two independent mechanisms, and that P20 might be a molecule mediating amylin's biological functions.</jats:p> Amylin evokes phosphorylation of P20 in rat skeletal muscle FEBS Letters |
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Wiley, 1999 |
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Wiley, 1999 |
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0014-5793 1873-3468 |
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0014-5793 1873-3468 |
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1999 |
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Wiley |
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FEBS Letters |
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| title |
Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_unstemmed |
Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_full |
Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_fullStr |
Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_full_unstemmed |
Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_short |
Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_sort |
amylin evokes phosphorylation of p20 in rat skeletal muscle |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/s0014-5793(99)01029-7 |
| publishDate |
1999 |
| physical |
149-152 |
| description |
<jats:p>To investigate the signal transduction events underlying amylin's actions, the amylin‐evoked protein phosphorylation cascade was analysed using two‐dimensional gel electrophoresis. We found that phosphorylation of three isoelectric variants of P20 (termed ARPP1, ARPP2 and ARPP3) was associated with amylin's actions in rat skeletal muscle. Amylin decreased phosphorylation of ARPP1 and increased phosphorylation of ARPP2 and ARPP3 in a dose‐dependent manner. Insulin inhibited amylin‐evoked phosphorylation of ARPP2 and ARPP3. The amylin‐selective antagonist rat amylin‐(8–37) completely reversed amylin's action on ARPP3 and partially decreased phosphorylation of ARPP2. By contrast, the CGRP‐selective antagonist, human CGRP‐(8–37) blocked phosphorylation of ARPP2 but had little effect on ARPP3. These results suggest that amylin modifies phosphorylation of P20 via two independent mechanisms, and that P20 might be a molecule mediating amylin's biological functions.</jats:p> |
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| author | Wang, Yu, Xu, Aimin, Cooper, Garth J.S |
| author_facet | Wang, Yu, Xu, Aimin, Cooper, Garth J.S, Wang, Yu, Xu, Aimin, Cooper, Garth J.S |
| author_sort | wang, yu |
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| container_start_page | 149 |
| container_title | FEBS Letters |
| container_volume | 457 |
| description | <jats:p>To investigate the signal transduction events underlying amylin's actions, the amylin‐evoked protein phosphorylation cascade was analysed using two‐dimensional gel electrophoresis. We found that phosphorylation of three isoelectric variants of P20 (termed ARPP1, ARPP2 and ARPP3) was associated with amylin's actions in rat skeletal muscle. Amylin decreased phosphorylation of ARPP1 and increased phosphorylation of ARPP2 and ARPP3 in a dose‐dependent manner. Insulin inhibited amylin‐evoked phosphorylation of ARPP2 and ARPP3. The amylin‐selective antagonist rat amylin‐(8–37) completely reversed amylin's action on ARPP3 and partially decreased phosphorylation of ARPP2. By contrast, the CGRP‐selective antagonist, human CGRP‐(8–37) blocked phosphorylation of ARPP2 but had little effect on ARPP3. These results suggest that amylin modifies phosphorylation of P20 via two independent mechanisms, and that P20 might be a molecule mediating amylin's biological functions.</jats:p> |
| doi_str_mv | 10.1016/s0014-5793(99)01029-7 |
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| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTAxNi9zMDAxNC01NzkzKDk5KTAxMDI5LTc |
| imprint | Wiley, 1999 |
| imprint_str_mv | Wiley, 1999 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2 |
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| last_indexed | 2024-03-01T14:27:11.902Z |
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| physical | 149-152 |
| publishDate | 1999 |
| publishDateSort | 1999 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | FEBS Letters |
| source_id | 49 |
| spelling | Wang, Yu Xu, Aimin Cooper, Garth J.S 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/s0014-5793(99)01029-7 <jats:p>To investigate the signal transduction events underlying amylin's actions, the amylin‐evoked protein phosphorylation cascade was analysed using two‐dimensional gel electrophoresis. We found that phosphorylation of three isoelectric variants of P20 (termed ARPP1, ARPP2 and ARPP3) was associated with amylin's actions in rat skeletal muscle. Amylin decreased phosphorylation of ARPP1 and increased phosphorylation of ARPP2 and ARPP3 in a dose‐dependent manner. Insulin inhibited amylin‐evoked phosphorylation of ARPP2 and ARPP3. The amylin‐selective antagonist rat amylin‐(8–37) completely reversed amylin's action on ARPP3 and partially decreased phosphorylation of ARPP2. By contrast, the CGRP‐selective antagonist, human CGRP‐(8–37) blocked phosphorylation of ARPP2 but had little effect on ARPP3. These results suggest that amylin modifies phosphorylation of P20 via two independent mechanisms, and that P20 might be a molecule mediating amylin's biological functions.</jats:p> Amylin evokes phosphorylation of P20 in rat skeletal muscle FEBS Letters |
| spellingShingle | Wang, Yu, Xu, Aimin, Cooper, Garth J.S, FEBS Letters, Amylin evokes phosphorylation of P20 in rat skeletal muscle, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_full | Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_fullStr | Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_full_unstemmed | Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_short | Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| title_sort | amylin evokes phosphorylation of p20 in rat skeletal muscle |
| title_unstemmed | Amylin evokes phosphorylation of P20 in rat skeletal muscle |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/s0014-5793(99)01029-7 |