Enhanced Mg(2+)-ATPase activity in ghosts from HS erythrocytes and in normal ghosts stripped of membrane skeletal proteins may reflect enhanced aminophospholipid translocase activity.

W.P. Vermeulen, J.J. Briedé, G. Bunt, J.A. op den Kamp, R.J. Kraaijenhagen, B. Roelofsen

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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 (mg2+-atpase) activities, varying from 115% to 160%, were invariably found in erythrocyte ghosts derived from 13 hs patients. Similarly, an enhancement of mg2+-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 mg2+-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 mg2+-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.
Original languageEnglish
Pages (from-to)56-64
JournalBritish Journal of Haematology
Issue number1
Publication statusPublished - 1 Jan 1995

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