Quantitative Measurement of Membrane Na+-K+ ATPase Activity using Thallium-201: Comparison with Rubidium-86 / 대한핵의학회잡지
Korean Journal of Nuclear Medicine
;
: 121-128, 1998.
Article
in Korean
| WPRIM
| ID: wpr-169342
ABSTRACT
PURPOSE:
Na+-K+ ATPase Activity has beem estimated by the degree of inhibition of cation transport by cardiac glycosides (ouabain) using Rb-86 as a substrate. The biological characterist-Isc of T1-201 is known to be simiIar to those of potassium as a transport substrate in the presence of glucose, insulin or phobol myristate acetate (PMA). The purpose of this study was to measure ouabain sensitive Na+-K+ ATPase activity using T1-201 and compare with that using Rb-86. MATERIALS ANDMETHODS:
Smooth muscle cells isolated from rat aorta or human placental umbilical artery were cultured, and used to measure cellular Na+-K+ ATPase activity. Na+-K+ ATPase activity was measured as a percentage decrease in cellular uptake of T1-201 or Rb-86 by ouabain under the presence of glucose, insulin or PMA in media.RESULTS:
Na+-K+ ATPase ase activity measured with T1-201, as a transport substrate, was not different from those measured with Rb-86 in rat or human smooth muscle cell preparation. Incubation with high concentration glucose resulted in about 30% decrease in enzyme activity. In contrast, insulin or PMA resulted in 50-70% or 28% increases from baseline activity, respectively.CONCLUSION:
These results suggests that T1-201 could replace Rb-86 in measurement of ouabain sensititive Na+-K+ ATPase activity in vitro. High level of glucose concentration decreased cellular Na+-K+ ATPase activity, but insulin or PMA increased it.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Aorta
/
Ouabain
/
Potassium
/
Umbilical Arteries
/
Cardiac Glycosides
/
Adenosine Triphosphatases
/
Myristic Acid
/
Myocytes, Smooth Muscle
/
Glucose
/
Insulin
Limits:
Animals
/
Humans
Language:
Korean
Journal:
Korean Journal of Nuclear Medicine
Year:
1998
Type:
Article
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