Fibroblast growth factor‐10 upregulates Na,K‐ATPase via the MAPK pathway

@article{Upadhyay2003FibroblastGF,
  title={Fibroblast growth factor‐10 upregulates Na,K‐ATPase via the MAPK pathway},
  author={Daya Upadhyay and Emilia Lecuona and Alejandro P. Comellas and David William Kamp and Jacob I. Sznajder},
  journal={FEBS Letters},
  year={2003},
  volume={545}
}
T3 increases Na-K-ATPase activity via a MAPK/ERK1/2-dependent pathway in rat adult alveolar epithelial cells.
TLDR
Data indicate that activation of MAPK-ERK1/2 was required for the T3-induced increase in Na-K-ATPase activity in addition to the requirement for the PI3K pathway.
Regulation of FGF10 Signaling in Development and Disease
TLDR
Emerging modes of FGF10 signaling regulation will be described, focusing on the role of F GF10 trafficking and sub-cellular localization, heparan sulfate proteoglycans, and miRNAs, and systems biology approaches based on quantitative proteomics will be considered for globally investigating FGF 10 signaling specificity.
Long-term regulation of Na+/K+-ATPase pump in human lymphocytes: Role of JAK/STAT and MAPK signaling pathways
TLDR
It is concluded that the long-term increase of the sodium pump transport activity, which is associated with the IL-2-dependent stage of proliferative response and is based on synthesis of new Na+/K+-ATPase subunits, is controlled through the JAK/STAT and ERK1/2-MAP-kinase pathways of intracellular signaling.
C-Peptide Increases Na,K-ATPase Expression via PKC- and MAP Kinase-Dependent Activation of Transcription Factor ZEB in Human Renal Tubular Cells
TLDR
Despite activation of ERK1/2 and PKC by hyperglycemia, a distinct pool of PKCs and ERK 1/2 is involved in regulation of Na,K-ATPase expression and activity by C-peptide.
C-peptide stimulates Na+, K+-ATPase via activation of ERK1/2 MAP kinases in human renal tubular cells
TLDR
C-peptide stimulates sodium pump activity via ERK1/2-induced phosphorylation of Thr residues on the α subunit of Na+, K+-ATPase in primary human renal tubular cells (HRTCs).
ERK1/2 Mediates Insulin Stimulation of Na,K-ATPase by Phosphorylation of the α-Subunit in Human Skeletal Muscle Cells*
TLDR
In conclusion, insulin stimulates Na+,K+-ATPase activity and translocation to plasma membrane in HSMCs via phosphorylation of the α-subunits by ERK1/2 mitogen-activated protein kinase.
Stimulation of MAP kinase pathways after maternal IL-1β exposure induces fetal lung fluid absorption in guinea pigs
TLDR
Data implicate the ERK MAP kinase pathway as being important for IL-1β induction/stimulation of lung fluid absorption in fetal guinea pigs.
Exogenous FGF10 can rescue an eye‐open at birth phenotype of Fgf10‐null mice by activating activin and TGFα‐EGFR signaling
TLDR
Results verify that FGF10 promotes eyelid closure through activating activin and TGFα‐EGFR signaling.
Alveolar epithelium and Na,K-ATPase in acute lung injury
TLDR
Elucidation of the mechanisms underlying regulation of active Na+ transport, as well as the pathways by which the Na,K-ATPase regulates epithelial barrier function and edema clearance, are of significance to identify interventional targets to improve outcomes of patients with acute lung injury.
Sodium tanshinone iia sulfonate attenuates seawater aspiration–induced acute pulmonary edema by up-regulating Na+,K+-ATPase activity
TLDR
Results indicated that STS could improve seawater aspiration–induced acute pulmonary edema by up-regulating Na+,K+-ATPase activity, and the ERK1/2 signaling pathway may be involved in it.
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PKA stimulates Na+,K+‐ATPase activity, at least in part, by increasing the number of Na+‐K+ pumps in the plasma membrane in proximal convoluted tubule cells, suggesting that cAMP‐PKA pathway was implicated in membrane redistribution control.
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TLDR
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TLDR
Dysregulation of diacylglycerol-sensitive types of protein kinase C (PKC) by pretreatment with phorbol 12-myristate 13-acetate or inhibition with bisindolylmaleimide prevented the DA-mediated increase in Na,K-ATPase activity and exocytosis of Na, K-pumps to the BLM.
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