Potassium-Induced Relaxation as an Indicator of Na+-K+ ATPase Activity in Vascular Smooth Muscle

1978 ◽  
Vol 15 (1-3) ◽  
pp. 198-207 ◽  
Author(s):  
Clinton Webb ◽  
David F. Bohr
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Atpase Activity

Serum transcriptionally regulates Na(+)-K(+)-ATPase gene expression in vascular smooth muscle cells

1997 ◽  
Vol 273 (3) ◽  
pp. C1088-C1099 ◽  
Author(s):  
J. Nemoto ◽  
S. Muto ◽  
A. Ohtaka ◽  
K. Kawakami ◽  
Y. Asano
Keyword(s):  
Gene Expression ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Atpase Activity ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Fold Increase ◽  
Mrna Levels ◽  
Subunit Protein ◽  
Mrna Induction

The present study was designed to examine the effects of serum on Na(+)-K(+)-ATPase alpha 1- and beta 1-subunit gene expression in cultured vascular smooth muscle cells (VSMC) from rat thoracic aortas. Addition of 10% serum to VSMC for 24 h increased Na(+)-K(+)-ATPase activity 1.5-fold and alpha 1- and beta 1-subunit protein levels 1.9-fold. Serum (10%) caused a 3.5-fold increase in alpha 1-mRNA levels and a 6.7-fold increase in beta 1-mRNA levels, with peak elevations at 12 h. The protein synthesis inhibitor cycloheximide abolished serum-mediated beta 1-mRNA induction but did not affect serum-mediated alpha 1-mRNA induction. Protein kinase C (PKC) inhibitors (staurosporine A or calphostin C) or tyrosine kinase (TK) inhibitors (genistein or herbimycin A) significantly reduced serum-mediated beta 1-mRNA induction but had no effect on serum-mediated alpha 1-mRNA induction. Transfection experiments with the 5'-flanking sequences of the alpha 1- or beta 1-subunit genes linked to the luciferase reporter gene revealed that 10% serum caused 2.8- and 6.5-fold increases in luciferase activity, respectively. Among growth factors, only basic fibroblast growth factor (FGF) enhanced luciferase activities for the alpha 1- and beta 1-subunit genes. We conclude that 1) serum stimulates alpha 1- and beta 1-mRNA expression, alpha 1- and beta 1-subunit protein accumulation, and Na(+)-K(+)-ATPase activity; 2) serum-mediated beta 1-mRNA induction partly requires de novo synthesis of intermediate regulatory proteins and activation of PKC and TK, whereas serum-mediated alpha 1-mRNA induction occurs through PKC- and TK-independent mechanisms; 3) the 5'-flanking regions of the alpha 1- and beta 1-subunit genes are serum responsive; and 4) FGF mimics stimulatory effects of serum on promoter activities for the alpha 1- and beta 1-subunit genes.

Na+-K+-ATPase in vascular smooth muscle

1986 ◽  
Vol 250 (4) ◽  
pp. C536-C539 ◽  
Author(s):  
J. C. Allen ◽  
S. S. Navran ◽  
A. M. Kahn
Keyword(s):  
Enzyme Activity ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Atpase Activity ◽  
Binding Site ◽  
Aortic Tissue ◽  
Ouabain Binding

Na+-K+-ATPase has been isolated and characterized from canine aortic tissue. The ouabain-sensitive enzyme activity was 24 mumol X mg protein-1 X h-1, and the remaining Mg2+-ATPase activity was 54 mumol X mg protein-1 X h-1. The ratio of Na+-K+-ATPase to ouabain-sensitive K+-phosphatase was 13 to 1, similar to other more homogeneous preparations from other tissues. The dissociation characteristics of the enzyme-glycoside complex of this aortic preparation were the same as for cardiac preparations in that it was stabilized by K+. These data suggest that the nature of both the ATP hydrolytic site of Na+-K+-ATPase and the ouabain binding site are the same in preparations from vascular smooth muscle as in preparations from other tissues.

Salt-inducible kinase 1 influences Na+,K+-ATPase activity in vascular smooth muscle cells and associates with variations in blood pressure

2011 ◽  
Vol 29 (12) ◽  
pp. 2395-2403 ◽  
Author(s):  
Sergej Popov ◽  
Angela Silveira ◽  
Dick Wågsäter ◽  
Hiroshi Takemori ◽  
Ryousuke Oguro ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Atpase Activity ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells

Effect of caffeine on the Ca2+pool affecting contractility and actomyosin ATPase activity in vascular smooth muscle of rabbit

1993 ◽  
Vol 23 (1) ◽  
pp. 92
Author(s):  
Jin Min Kim ◽  
Young Ho Lee ◽  
Chang Hyun Moon ◽  
Bok Soon Kang ◽  
Doo Hee Kang
Keyword(s):  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Atpase Activity ◽  
Actomyosin Atpase

scholarly journals Role of an aprotinin-sensitive protease in the activation of Ca2+-ATPase by superoxide radical (O2-.) in microsomes of pulmonary vascular smooth muscle

1996 ◽  
Vol 317 (3) ◽  
pp. 885-890 ◽  
Author(s):  
Tapati CHAKRABORTI ◽  
Salil K. GHOSH ◽  
John R. MICHAEL ◽  
Sajal CHAKRABORTI
Keyword(s):  
Superoxide Dismutase ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Atpase Activity ◽  
Molecular Mass ◽  
Protease Activity ◽  
Superoxide Radical ◽  
Polyclonal Antiserum ◽  
Generating System

We have investigated the role of an aprotinin-sensitive protease in regulating Ca2+-ATPase activity and Ca2+ uptake (ATP-dependent and Na+-dependent) in microsomes of bovine pulmonary vascular smooth muscle during treatment with the O2-•-generating system hypoxanthine plus xanthine oxidase. Treatment of the smooth muscle microsomes with the O2-•-generating system produced a protease in a gelatin-containing zymogram with an apparent molecular mass of 16 kDa. This 16 kDa proteolytic protein was found to be inhibited by superoxide dismutase (SOD) and aprotinin but not by PMSF. Using polyclonal antiserum to aprotinin, we found that it is an ambient antiprotease of the smooth muscle microsomes. Treatment of the microsomes with the O2-•-generating system stimulated protease activity tested with a synthetic substrate N-benzoyl-dl-arginine p-nitroanilide and also enhanced Ca2+-ATPase activity. It also stimulated ATP-dependent Ca2+ uptake. In contrast, Na+-dependent Ca2+ uptake was found to be inhibited by the O2-•-generating system. Pretreatment of the microsomes with SOD and aprotinin preserved the increase in protease activity, Ca2+-ATPase activity and ATP-dependent Ca2+ uptake. In addition, O2-•-caused inhibition of the Na+-dependent Ca2+ uptake which was reversed by SOD and aprotinin. Pretreatment with PMSF did not cause any discernible alteration in the protease activity, Ca2+-ATPase activity, ATP-dependent Ca2+ uptake and Na+-dependent Ca2+ uptake in the microsomes caused by the O2-•-generating system. These results suggest that an aprotinin-sensitive protease plays a pivotal role in regulating Ca2+-ATPase and Ca2+-uptake activities in microsomes of pulmonary vascular smooth muscle under oxidant O2-•-triggered conditions.

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