EurekaMag.com logo
+ Site Statistics
References:
53,214,146
Abstracts:
29,074,682
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

The amiloride sensitive sodium proton antiport in 3t3 fibroblasts characterization and stimulation by serum


Journal of Biological Chemistry 258(10): 6272-6276
The amiloride sensitive sodium proton antiport in 3t3 fibroblasts characterization and stimulation by serum
BALB/c 3T3 [mouse] fibroblasts have an amiloride-sensitive Na+ uptake mechanism which is hardly detectable under normal physiological conditions. The activity of this Na+ transport system can be increased to a large extent by treatments that decrease the internal pH such as loss of intracellular NH4+ as NH3 or incubation with nigericin in the presence of a low external K+ concentration. These treatments made possible an analysis of the interaction of the Na+/H+ antiport with amiloride and of the external pH dependence of the system. The addition of fetal bovine serum to quiescent 3T3 cells stimulates the initial rate of the amiloride-sensitive 22Na+ uptake by only 50%. However, after treatment of the cells with ammonia or nigericin, serum produces a 40-fold stimulation of the rate of the amiloride-sensitive 22Na+ uptake. Control experiments show that serum does not stimulate the activity of the Na+/H+ antiport by an indirect mechanism involving a depolarization of the membrane or a modification of the internal Ca2+ concentration. Some serum component may directly interact with the Na+/H+ exchanger to modify its catalytic properties.

(PDF 0-2 workdays service: $29.90)

Accession: 006599078



Related references

Biochemical characterization of the amiloride sensitive sodium proton antiport in chinese hamster lung fibroblasts. Journal of Biological Chemistry 258(6): 3503-3508, 1983

The amiloride-sensitive Na+/H+ antiport in 3T3 fibroblasts: characterization and stimulation by serum. The Journal of Biological Chemistry 258: 72-6, 1983

The amiloride sensitive sodium proton antiport in guinea pig pancreatic acini characterization and stimulation by caerulein. Febs Letters 187(1): 126-130, 1985

Characterization of the amiloride sensitive sodium proton antiport of human neutrophils. American Journal of Physiology 250(2 PART 1): C283-C291, 1986

On the mechanism of amiloride sensitive nonelectrogenic sodium proton exchange in cell membranes sodium proton antiport or sodium hydroxyl ion symport?. General Physiology & Biophysics 6(5): 449-468, 1987

The sinusoidal domain of the plasma membrane of rat hepatocytes contains an amiloride sensitive sodium proton antiport. Journal of Biological Chemistry 259(9): 5406-5408, 1984

Biochemical characterization of the amiloride-sensitive Na+/H+ antiport in Chinese hamster lung fibroblasts. Journal of Biological Chemistry 258(6): 3503-3508, 1983

The sinusoidal amiloride sensitive sodium proton antiport modulates intracellular ph and gap junction coupling in isolated paired rat hepatocytes. Hepatology 4(5): 1072, 1984

Blockade of the sodium proton antiport abolishes growth factor induced dna synthesis in fibroblasts structure activity relationships in the amiloride series. Journal of Biological Chemistry 259(7): 4313-4319, 1984

The amiloride sensitive Na+/H+ antiport in guinea pig pancreatic acini. Characterization and stimulation by caerulein. Febs Letters 187(1): 126-130, 1985