Effect of a Hyperlipidic Diet on Lipid Composition, Fluidity, and (Na+-K+)ATPase Activity of Rat Erythrocyte Membranes

1989 ◽  
Vol 8 (1) ◽  
pp. 11-18 ◽  
Author(s):  
A. Bordoni ◽  
P. L. Biagi ◽  
G. Parenti Castelli ◽  
S. Hrelia ◽  
C. A. Rossi ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Lipid Composition ◽  
Erythrocyte Membranes ◽  
Hyperlipidic Diet

scholarly journals Lipid composition and Na+,K+-ATPase activity in erythrocyte membranes of patients with type 2 diabetes mellitusand dyslipoproteinemia

2010 ◽  
Vol 13 (1) ◽  
pp. 41-44 ◽  
Author(s):  
Elena Borisovna Kravets ◽  
Elena Alekseevna Stepovaya ◽  
Tatiana Yur'evna Koshchevets ◽  
Olesya Dmitrievna Medvedeva ◽  
Natalya Mikhailovna Yakovleva ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Atpase Activity ◽  
Carbohydrate Metabolism ◽  
Lipid Composition ◽  
Erythrocyte Membranes ◽  
Therapeutic Modalities

Aim. To study lipid composition and Na+,K+-Na+,K+-ATPase activity in erythrocyte membranes of patients with type 2 diabetes mellitus and dyslipoproteinemia. Materials and methods. The study included 40 patients (22 men and 18 women) aged 40-65 years with DM2. Results. The patients had abnormal lipid composition and impaired Na+,K+-Na+,K+-ATPase activity in erythrocyte membranes. The magnitude of thesechanges depended on the duration of pathology, severity of diabetic dyslipoproteinemia, and quality of compensation of carbohydrate metabolism. Conclusion. Aim. Investigation of lipid dysorganization in erythrocyte membranes in patients with type 2 diabetes mellitus yields data for the developmentof therapeutic modalities to correct dyslipoproteinemia.

scholarly journals Calcium-ATPase Activity in Cystic Fibrosis Erythrocyte Membranes: Decreased Activity in Patients with Pancreatic Insufficiency

1984 ◽  
Vol 18 (9) ◽  
pp. 890-895 ◽  
Author(s):  
Dorr G Dearborn ◽  
Robert J Wityk ◽  
Lynelle R Johnson ◽  
Louis Poncz ◽  
Robert C Stern
Keyword(s):  
Cystic Fibrosis ◽  
Atpase Activity ◽  
Pancreatic Insufficiency ◽  
Calcium Atpase ◽  
Erythrocyte Membranes

Changes in Erythrocyte Membrane Ouabain-Sensitive Adenosine Triphosphatase after Renal Transplantation

1975 ◽  
Vol 48 (3) ◽  
pp. 239-242 ◽  
Author(s):  
C. H. Cole ◽  
R. Maletz
Keyword(s):  
Renal Transplantation ◽  
Atpase Activity ◽  
Erythrocyte Membrane ◽  
Adenosine Triphosphatase ◽  
Inorganic Phosphorus ◽  
Erythrocyte Membranes ◽  
Healthy Controls ◽  
Intracellular Electrolytes ◽  
Transplant Patients ◽  
The Mean

1. Intracellular electrolytes, and erythrocyte membrane adenosine triphosphatase (ATPase) activity, was studied in twenty patients after renal transplantation. 2. The mean ouabain-sensitive ATPase activity in the erythrocyte membranes of the transplant patients was 122 nmol of inorganic phosphorus (Pi) h−1 mg of tissue−1 (sem 14), compared with 62 nmol of Pi h−1 mg of tissue−1 (sem 8) in a group of paired, healthy controls. 3. The increase in ouabain-sensitive ATPase was most marked in the 4 months after transplantation. However, a significant increase in ouabain-sensitive ATPase persisted for more than 8 months after transplantation. 4. This increase in ouabain-sensitive ATPase was associated with a decrease in intracellular sodium in the erythrocytes of the transplant patients.

Combined effects of lead and edta on Na+,K+‐ATPase activity of erythrocyte membranes

1983 ◽  
Vol 12 (4-6) ◽  
pp. 721-730 ◽  
Author(s):  
Ichiro Karai ◽  
Su Ill Lee ◽  
Shun'ichi Horiguchi ◽  
Koichi Fukumoto ◽  
Shinya Matsumura ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Erythrocyte Membranes ◽  
Combined Effects

scholarly journals A protein activator of Mg2+-dependent, Ca2+-stimulated ATPase in human erythrocyte membranes distinct from calmodulin

1980 ◽  
Vol 187 (2) ◽  
pp. 507-513 ◽  
Author(s):  
Douglas Mauldin ◽  
Basil D. Roufogalis
Keyword(s):  
Atpase Activity ◽  
Sucrose Gradient ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Erythrocyte Membranes ◽  
Dependent Manner ◽  
Calmodulin Binding ◽  
Heat Stable ◽  
Protein Activator ◽  
Human Erythrocyte Membranes

Treatment of extensively washed erythrocyte membranes with 0.1mm-EDTA decreased their Mg2+-dependent, Ca2+-stimulated ATPase [(Mg2++Ca2+)-ATPase] activity. An activator released by this treatment restored the (Mg2++Ca2+)-ATPase to its original value in a Ca2+-dependent manner. This activator was different from calmodulin, as determined by a number of criteria. It was retained on an Amicon XM-100 ultrafiltration membrane (molecular-weight cut-off 100000); it appeared in the void volume of Sephadex G-100 and G-75 columns; it was not retained on a DEAE-cellulose ion-exchange column at ionic strengths similar to those used to retain calmodulin; and it maximally activated (Mg2++Ca2+)-ATPase activity less than calmodulin and at a higher Ca2+ concentration. Like calmodulin, the activator is heat-stable. The activator fraction isolated on a 2.5–15% sucrose gradient in 0.16m-KCl showed a single band of mol.wt. 63000 and no calmodulin on 10%-polyacrylamide/sodium dodecyl sulphate gels. A trace amount of calmodulin was detected in the activator fraction by radioimmunoassay (approx. 10pg/ml of ‘ghosts’), but this amount was insufficient to account for the (Mg2++Ca2+)-ATPase activation. Furthermore, calmodulin-binding protein failed to inhibit (Mg2++Ca2+)-ATPase activity by more than 10–20% in the membrane preparations from which the activator was extracted. It was concluded that erythrocyte membranes contain a (Mg2++Ca2+)-ATPase activator that may attenuate the activation of the Ca2+-transport ATPase by calmodulin.

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