| 000 | 03061nab a2200373 c 4500 | ||
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| 001 | koha000897588 | ||
| 005 | 20220708131843.0 | ||
| 007 | cr | | ||
| 008 | 220706|2021 xxu s a eng d | ||
| 024 | 7 |
_a10.1007/s00232-021-00209-7 _2doi |
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| 035 | _akoha000897588 | ||
| 040 |
_aRU-ToGU _brus _cRU-ToGU |
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| 245 | 1 | 0 |
_aPhosphorylation of Na+,K+‑ATPase at Tyr10 of the α1‑subunit is suppressed by AMPK and enhanced by ouabain in cultured kidney cells _cP. Metka, A. Vidović, K. Dolinar [et al.] |
| 336 | _aТекст | ||
| 337 | _aэлектронный | ||
| 504 | _aБиблиогр.: с. 546-548 | ||
| 520 | 3 | _aNa+,K+-ATPase (NKA) is essential for maintenance of cellular and whole-body water and ion homeostasis. In the kidney, a major site of ion transport, NKA consumes ~ 50% of ATP, indicating a tight coordination of NKA and energy metabolism. AMP-activated protein kinase (AMPK), a cellular energy sensor, regulates NKA by modulating serine phosphorylation of the α1-subunit, but whether it modulates other important regulatory phosphosites, such as Tyr10, is unknown. Using human kidney (HK-2) cells, we determined that the phosphorylation of Tyr10 was stimulated by the epidermal growth factor (EGF), which was opposed by inhibitors of Src kinases (PP2), tyrosine kinases (genistein), and EGF receptor (EGFR, geftinib). AMPK activators AICAR and A-769662 suppressed the EGF-stimulated phosphorylation of EGFR (Tyr1173) and NKAα1 at Tyr10. The phosphorylation of Src (Tyr416) was unaltered by AICAR and increased by A-769662. Conversely, ouabain (100 nM), a pharmacological NKA inhibitor and a putative adrenocortical hormone, enhanced the EGF-stimulated Tyr10 phosphorylation without altering the phosphorylation of EGFR (Tyr1173) or Src (Tyr416). Ouabain (100–1000 nM) increased the ADP:ATP ratio, while it suppressed the lactate production and the oxygen consumption rate in a dose-dependent manner. Treatment with ouabain or gene silencing of NKAα1 or NKAα3 subunit did not activate AMPK. In summary, AMPK activators and ouabain had antagonistic efects on the phosphorylation of NKAα1 at Tyr10 in cultured HK-2 cells, which implicates a role for Tyr10 in coordinated regulation of NKA-mediated ion transport and energy metabolism. | |
| 653 | _aфосфорилирование | ||
| 653 | _aуабаин | ||
| 653 | _aнатрий-калиевая аденозинтрифосфатаза | ||
| 653 | _aAMP-активированная протеинкиназа | ||
| 655 | 4 |
_aстатьи в журналах _9809203 |
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| 700 | 1 |
_aMetka, Petrič _9809202 |
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| 700 | 1 |
_aVidović, Anja _9809204 |
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| 700 | 1 |
_aDolinar, Klemen _9493059 |
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| 700 | 1 |
_aMiš, Katarina _9809205 |
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| 700 | 1 |
_aChibalin, Alexander V. _9493057 |
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| 700 | 1 |
_aPirkmajer, Sergej _9493058 |
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| 773 | 0 |
_tThe Journal of membrane biology _d2021 _gVol. 254, № 5/6. P. 531-548 _x0022-2631 |
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| 852 | 4 | _aRU-ToGU | |
| 856 | 4 | _uhttp://vital.lib.tsu.ru/vital/access/manager/Repository/koha:000897588 | |
| 908 | _aстатья | ||
| 999 | _c897588 | ||