TY - JOUR
T1 - The actin cytoskeleton and small G protein RhoA are not involved in flow-dependent activation of ENaC
AU - Karpushev, Alexey V.
AU - Ilatovskaya, Daria V.
AU - Staruschenko, Alexander
N1 - Funding Information:
Glen Slocum is recognized for excellent technical assistance with microscopy experiments. This research was supported by American Heart Association (SDG 0730111N), American Society of Nephrology Carl W. Gottschalk Research Scholar Grant, and American Physiological Society S&R Foundation Ryuji Ueno Award (to AS). We thank Rob Menzies for critical reading of the manuscript.
PY - 2010
Y1 - 2010
N2 - Background. Epithelial cells are exposed to a variety of mechanical stimuli. Epithelial Na+ channels (ENaC) mediate sodium transport across apical membranes of epithelial cells that line the distal nephron, airway and alveoli, and distal colon. Early investigations into stretch sensitivity of ENaC were controversial. However, recent studies are supportive of ENaC's mechanosensitivity. This work studied whether flow-dependent activation of ENaC is modulated by changes in the state of the actin cytoskeleton and whether small GTPase RhoA is involved in flow-mediated increase of ENaC activity. Findings. Pretreatment with Cytochalasin D and Latrunculin B for 20 min and 1-2 hrs to disassemble F-actin had no effect on flow-mediated increase of amiloride-sensitive current. Overexpression of ENaC with constitutively active (G14V) or dominant negative (T19N) RhoA similarly had no effect on flow-dependent activation of ENaC activity. In addition, we did not observe changes when we inhibited Rho-kinase with Y27632. Conclusions. Our results suggest that the flow-dependent activation of ENaC is not influenced by small GTPase RhoA and modifications in the actin cytoskeleton.
AB - Background. Epithelial cells are exposed to a variety of mechanical stimuli. Epithelial Na+ channels (ENaC) mediate sodium transport across apical membranes of epithelial cells that line the distal nephron, airway and alveoli, and distal colon. Early investigations into stretch sensitivity of ENaC were controversial. However, recent studies are supportive of ENaC's mechanosensitivity. This work studied whether flow-dependent activation of ENaC is modulated by changes in the state of the actin cytoskeleton and whether small GTPase RhoA is involved in flow-mediated increase of ENaC activity. Findings. Pretreatment with Cytochalasin D and Latrunculin B for 20 min and 1-2 hrs to disassemble F-actin had no effect on flow-mediated increase of amiloride-sensitive current. Overexpression of ENaC with constitutively active (G14V) or dominant negative (T19N) RhoA similarly had no effect on flow-dependent activation of ENaC activity. In addition, we did not observe changes when we inhibited Rho-kinase with Y27632. Conclusions. Our results suggest that the flow-dependent activation of ENaC is not influenced by small GTPase RhoA and modifications in the actin cytoskeleton.
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U2 - 10.1186/1756-0500-3-210
DO - 10.1186/1756-0500-3-210
M3 - Article
AN - SCOPUS:77955580094
SN - 1756-0500
VL - 3
JO - BMC Research Notes
JF - BMC Research Notes
M1 - 210
ER -