Enhanced Mg2+-ATPase activity in ghosts from HS erythrocytes and in normal ghosts stripped of membrane skeletal proteins may reflect enhanced aminophospholipid translocase activity
| Autor: | Ben Roelofsen, Jacob J. Briedé, J.A.F. Op den Kamp, R.J. Kraaijenhagen, G. Bunt, Willem P. Vermeulen |
|---|---|
| Přispěvatelé: | Biochemie, RS: NUTRIM School of Nutrition and Translational Research in Metabolism |
| Rok vydání: | 1995 |
| Předmět: |
Adult
Male Adolescent ATPase Spherocytosis Hereditary Buffers medicine Humans Translocase Spectrin Phospholipid Transfer Proteins Child Magnesium ion Ca(2+) Mg(2+)-ATPase biology Chemistry Erythrocyte Membrane Neuropeptides Osmolar Concentration Membrane Proteins Hematology Middle Aged medicine.disease Actins Cytoskeletal Proteins Red blood cell medicine.anatomical_structure Membrane protein Biochemistry Child Preschool Biophysics biology.protein Electrophoresis Polyacrylamide Gel Female Carrier Proteins Congenital hemolytic anemia |
| Zdroj: | British Journal of Haematology, 90(1), 56-64. Wiley |
| ISSN: | 1365-2141 0007-1048 |
| DOI: | 10.1111/j.1365-2141.1995.tb03380.x |
| Popis: | Hereditary spherocytosis (HS) is a congenital haemolytic anaemia which is characterized by a great variety of structural defects in the red cell's membrane skeleton and/or deficiencies in particular membrane (skeletal) proteins. Enhanced (Mg2+)-dependent adenosine triphosphatase (Mg(2+)-ATPase) activities, varying from 115% to 160%, were invariably found in erythrocyte ghosts derived from 13 HS patients. Similarly, an enhancement of Mg(2+)-ATPase activity by 30% is observed in normal red cell ghosts that have been stripped of the greater part of their membrane skeletal proteins by treatment with a low ionic strength buffer. Reassociation of those stripped ghosts with spectrin reduces the enhanced Mg(2+)-ATPase activity to its original level. Since in both cases, HS ghosts and stripped normal ghosts, the stabilizing effects that the membrane skeleton exerts on the maintenance of an endofacial localization of the aminophospholipids are impaired, the enhanced Mg(2+)-ATPase activity is interpreted to reflect an increased activity of the aminophospholipid translocase. The present observations therefore support a role of the membrane skeleton in the stabilization of phospholipid asymmetry in the red cell membrane and consequently in reducing the energy consumption of the translocase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text