Low nanomolar concentrations of ouabain may induce higher activity of the Na+/K+-ATPase in human erythrocytes

نویسنده

  • Roberto Antolović
چکیده

The inhibitor g-Strophantin, also known as ouabain, is a specific inhibitor of the Na+/K+-ATPase. In this work ouabain has been used for the inhibition of the Na+/K+-ATPase in human erythrocytes and isolated enzyme from pig kidney. Enzymatic activity of the Na+/K+-ATPase has been measured in a broad concentration range of ouabain in two different in vitro investigations. As a potent inhibitor of the sodium pump the cardiotonic steroid ouabain inhibits its enzymatic activity on both isolated human red blood cells and on the purified enzyme from pig kidney. Na+/K+-ATPase activity in erythrocyte can be determined by measuring the ouabain-sensitive uptake of 86Rb (as a congener for potassium). This work provides evidence that very low concentrations of ouabain in the nM range can stimulate increase of Na+/K+-ATPase activity in human erythrocytes, in contrast to inhibition of the purified enzyme from pig kidney, where such an effect was not observed.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

O-10: A Marked Animal-Vegetal Polarity in The Localization of Na+,K+-ATPase Activity and Its Down-Regulation Following Progesterone-Induced Maturation

Background: Polarized cells are key to the process of differentiation. Xenopus oocyte is a polarized cell that has complete blue-print to differentiate 3 germ layers following fertilization, as key determinant molecules (Proteins and RNAs) are asymmetrically localized. The objective of this work was to localize Na+, K+-ATPase activity along animal-vegetal axis of polarized Xenopus oocyte and fo...

متن کامل

Ouabain stimulates Na-K-ATPase through a sodium/hydrogen exchanger-1 (NHE-1)-dependent mechanism in human kidney proximal tubule cells.

Recent investigations demonstrate increased Na/H exchanger-1 (NHE-1) activity and plasma levels of ouabain-like factor in spontaneously hypertensive rats. At nanomolar concentrations, ouabain increases Na-K-ATPase activity, induces cell proliferation, and activates complex signaling cascades. We hypothesize that the activity of NHE-1 and Na-K-ATPase are interdependent. To test whether treatment...

متن کامل

Electrolyte Composition of Mink (Mustela vison) Erythrocytes and Active Cation Transporters of the Cell Membrane

Red blood cells from mink (Mustela vison) were characterized with respect to their electrolyte content and their cell membranes with respect to enzymatic activity for cation transport. The intra- and extracellular concentrations of Na+, K+, Cl-, Ca2+ and Mg2+ were determined in erythrocytes and plasma, respectively. Plasma and red cell water content was determined, and molal electrolyte concent...

متن کامل

O-13: Na+/K+-ATPase Alpha1 Isoform Mediates Ouabain-Induced Expression of Cyclin D1 and Proliferation of Rat Sertoli Cells

Background: Novel roles for the interaction of cardiotonic steroids to Na+/K+-ATPase have been established in recent years. The aim of the present study was to investigate the intracellular signaling events downstream the action of ouabain on Na+/K+-ATPase in Sertoli cell obtained from immature rats. Treatment of Sertoli cells with ouabain (1 μM) induced a rapid and transient increase in the ex...

متن کامل

[3H]ouabain binding of red blood cells in whites and blacks.

In a previous study, we demonstrated that the red blood cell Na+ concentration and Na+,K+-ATPase activity are sex-dependent and race-dependent: a higher intracellular Na+ concentration in blacks and men was associated with a lower Na+,K+-ATPase activity. To examine whether the low Na+,K+-ATPase activity is due to a decreased number of enzyme units, altered structure of the enzyme, or the presen...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2007