Lactoferrin stimulates erythrocyte Na+/K+ -adenosine triphosphatase: effect of some modulators of membrane phosphorylation.

نویسندگان

  • Ana Maneva
  • Pavlina Angelova-Gateva
  • Borislava Taleva
  • Lilia Maneva-Radicheva
  • Vladi Manev
چکیده

We studied the effect of some modulators of signal transduction on the erythrocyte Na+/ K+-ATPase. Go6976 and Go6983 (protein kinase C inhibitors) showed a stimulatory effect and calyculin A (protein phosphatase inhibitor) exerted an inhibitory effect on the Na pump activity. Some of the tested modulators of cell-signaling [protein phosphatase(s), phosphodiesterase, calmodulin and some protein kinases] interfered with the lactoferrin (Lf) stimulatory effect on the sodium pump. Lf itself was able to modulate the effect of some agents upon the pump activity. Moreover, an additive effect of stimulation was found when Lf and some agents were used simultaneously. The summarized results showed that: (i) Lf upregulates the Na+/K+-ATPase in erythrocytes and facilitates the K+ influx into the erythrocytes; (ii) the effect of pump stimulation is mediated by phosphorylation processes. These results suggest a potential opportunity for using Lf alone or together with other agents as a stimulator of the erythrocyte Na+/K+-ATPase.

برای دانلود رایگان 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

Comparative properties of high potassium and low potassium sheep erythrocyte membrane sodium-activated adenosine triphosphatase.

A comparative study of the Na+-stimulated adenosine triphosphatase system in high potassium (HK) and low potassium (LK) sheep red cell membranes was carried out. For HK:LK activity, the approximate ratios were as follows: 10 for Na+-ATPase, 13 for Na+, K+-ATPase, and 2.7 for [%+ ADP-ATP exchange activity; the ratio of Na+-stimulated membrane phosphorylation was approximately 7. With Na+ present...

متن کامل

Lead ion activates phosphorylation of electroplax Na+- and K+-dependent adenosine triphosphatase ((NaK)-ATPase) in the absence of sodium ion.

PbCl, in micromolar concentrations stimulates phosphorylation of electroplax microsomal protein in the absence of Nat. Other divalent cations showed little or no such effect. The (Mg’+ + Pb’+)and (Mg”+ + Na+)-dependent membrane-bound protein kinase activities in electroplax particulate preparations exhibit properties in common, including their acid stability, ouabain sensitivity, ATP specificit...

متن کامل

The Levels of Sera Malondialdehyde, Erythrocyte Membrane Na+-K+/Mg++ and Ca++/Mg++ Adenosine 5' Triphosphatase in Patients with Sickle Cell Anemia.

The various membrane abnormalities of sickle erythrocytes may result from excessive accumulation of oxidant damage. We measured the sera levels of malondialdehyde, products of lipid peroxidation, Na+-K+/Mg++ Adenosine 5' triphosphatase (ATPase) and Ca++/Mg++ Adenosine 5' triphosphatase, erythrocyte membrane enzymes, in patients with sickle cell anemia and compared their levels with that of norm...

متن کامل

Abnormal erythrocyte Na, K-ATPase activity in a northeastern Thai population.

We studied the cellular membrane enzyme responsible for potassium transport in different Thai populations. We measured plasma and intraerythrocytic concentrations of sodium and potassium, activities of erythrocytic membrane Na, K-activated adenosine triphosphatase (Na, K-ATPase), ouabain-insensitive ATPase, total ATPase and the activity ratio of Na, K-ATPase/total ATPase in 25 healthy blood don...

متن کامل

The Inhibition of Mitochondrial Adenosine Triphosphatase

Previous studies reported from this and other Laboratories have shown that isolated mitochondria are able to maintain concentration gradients of Na+ and K+ ions. When incubated in media containing an oxidizable substrate and ATP, mitochondria from liver (Macfarlane & Spencer, 1953; Spector, 1953; Price, Fonnesu & Davies, 1956), kidney (Bartley & Davies, 1954; Ulrich, 1961), heart and skeletal m...

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

عنوان ژورنال:
  • Zeitschrift fur Naturforschung. C, Journal of biosciences

دوره 62 11-12  شماره 

صفحات  -

تاریخ انتشار 2007