scholarly journals Up-Regulation of Sodium Channel Subunit mRNAs and Their Cell Surface Expression by Antiepileptic Valproic Acid: Activation of Calcium Channel and Catecholamine Secretion in Adrenal Chromaffin Cells

2002 ◽  
Vol 68 (4) ◽  
pp. 1655-1662 ◽  
Author(s):  
Ryuichi Yamamoto ◽  
Toshihiko Yanagita ◽  
Hideyuki Kobayashi ◽  
Hiroki Yokoo ◽  
Akihiko Wada
Keyword(s):  
Valproic Acid ◽  
Cell Surface ◽  
Calcium Channel ◽  
Sodium Channel ◽  
Chromaffin Cells ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Acid Activation ◽  
Adrenal Chromaffin Cells ◽  
Adrenal Chromaffin

Functional interaction of COMMD3 and COMMD9 with the epithelial sodium channel

2013 ◽  
Vol 305 (1) ◽  
pp. F80-F89 ◽  
Author(s):  
Yong Feng Liu ◽  
Marianne Swart ◽  
Ying Ke ◽  
Kevin Ly ◽  
Fiona J. McDonald
Keyword(s):  
Cell Surface ◽  
Sodium Channel ◽  
Collecting Duct ◽  
Extracellular Fluid ◽  
Copper Metabolism ◽  
Epithelial Sodium Channel ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Endogenous Regulators ◽  
Collecting Duct Cells

The epithelial sodium channel (ENaC) plays an important role in controlling Na+ homeostasis, extracellular fluid volume, and blood pressure. Copper metabolism Murr1 domain-containing protein 1 (COMMD1) interacts with ENaC and downregulates ENaC. COMMD1 belongs to the COMMD family consisting of COMMD1–10, and all COMMD family members share a C-terminal COMM domain. Here, we report that COMMD2–10 also interacts with ENaC, and COMMD3 and COMMD9 were selected for further study. Amiloride-sensitive current in mammalian epithelia expressing ENaC was significantly reduced by COMMD3 or COMMD9, and ENaC expression at the cell surface was significantly decreased in the presence of COMMD3 or COMMD9. COMMD3 and COMMD9 retained their ability to reduce current when COMMD1 was knocked down. COMMD3 and COMMD9 were widely expressed in kidney and were colocalized with ENaC in renal collecting duct cells. These data suggest that COMMD3 and COMMD9 may be endogenous regulators of ENaC to regulate Na+ transport through altering ENaC cell surface expression.

scholarly journals Amyloid Precursor Protein Enhances Nav1.6 Sodium Channel Cell Surface Expression

2015 ◽  
Vol 290 (19) ◽  
pp. 12048-12057 ◽  
Author(s):  
Chao Liu ◽  
Francis Chee Kuan Tan ◽  
Zhi-Cheng Xiao ◽  
Gavin S. Dawe
Keyword(s):  
Cell Surface ◽  
Amyloid Precursor Protein ◽  
Sodium Channel ◽  
Surface Expression ◽  
Precursor Protein ◽  
Cell Surface Expression

Regulation of Voltage-Dependent Sodium Channel Expression in Adrenal Chromaffin Cells

2002 ◽  
Vol 971 (1) ◽  
pp. 127-134 ◽  
Author(s):  
HIDEYUKI KOBAYASHI ◽  
SEIJI SHIRAISHI ◽  
TOSHIHIKO YANAGITA ◽  
HIROKI YOKOO ◽  
RYUICHI YAMAMOTO ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Voltage Dependent ◽  
Channel Expression ◽  
Adrenal Chromaffin

scholarly journals Protein Kinase C-α and -ε Down-Regulate Cell Surface Sodium Channels via Differential Mechanisms in Adrenal Chromaffin Cells

2002 ◽  
Vol 74 (4) ◽  
pp. 1674-1684 ◽  
Author(s):  
Toshihiko Yanagita ◽  
Hideyuki Kobayashi ◽  
Ryuichi Yamamoto ◽  
Hiroaki Kataoka ◽  
Hiroki Yokoo ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Surface ◽  
Sodium Channels ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Kinase C ◽  
Adrenal Chromaffin

Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel

FEBS Letters ◽  
2013 ◽  
Vol 587 (19) ◽  
pp. 3159-3165 ◽  
Author(s):  
Pedro Beltran-Alvarez ◽  
Alexsandra Espejo ◽  
Ralf Schmauder ◽  
Carlos Beltran ◽  
Ralf Mrowka ◽  
...  
Keyword(s):  
Cell Surface ◽  
Sodium Channel ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Cardiac Sodium Channel
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