1994American Journal of HematologyRequires access

Erythrocyte membrane vesicles and irreversibly sickled cells bind protein S

Peter A. Lane, Jacquie L O'Connell, Richard A. Marlar

Open publisher page 26 citations

Abstract

Plasma levels of free protein S, a vitamin K-dependent anticoagulant, are decreased in persons with sickle cell anemia, but the etiology of the low levels is unknown. Protein S binds to phosphatidylserine-containing phospholipids in a calcium-dependent manner. Other studies have indicated that phosphatidylserine may be abnormally present on the outer surface of the membrane lipid bilayer of sickle cells and of the spectrin-depleted vesicles they shed in vivo. We studied the binding of purified, radiolabeled protein S to spectrin-depleted erythrocyte membrane vesicles and to density-separated fractions of sickle and normal erythrocytes. Calcium-dependent binding of protein S occurred with vesicles and with well-aerated dense irreversibly sickled cells, but not with well-aerated sickle discocytes or with normal erythrocytes. These data provide further evidence that phosphatidylserine is abnormally present on the outer surface of spectrin-depleted vesicles and of irreversibly sickled cells. In addition, protein S binding to such sickle membranes in vivo may be responsible, in part, for the decreased levels of free protein S in sickle cell plasma.

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What this paper is about

Plasma levels of free protein S, a vitamin K-dependent anticoagulant, are decreased in persons with sickle cell anemia, but the etiology of the low levels is unknown. Protein S binds to phosphatidylserine-containing phospholipids in a calcium-dependent manner. Other studies have indicated that phosphatidylserine may be abnormally present on the outer surface of the membrane lipid bilayer of sickle cells and of the spectrin-depleted vesicles they shed in vivo. We studied the binding of purified, radiolabeled protein S to spectrin-depleted erythrocyte membrane vesicles and to density-separated fractions of sickle and normal erythrocytes. Calcium-dependent binding of protein S occurred with vesicles and with well-aerated dense irreversibly sickled cells, but not with well-aerated sickle discocytes or with normal erythrocytes. These data provide further evidence that phosphatidylserine is abnormally present on the outer surface of spectrin-depleted vesicles and of irreversibly sickled cells. In addition, protein S binding to such sickle membranes in vivo may be responsible, in part, for the decreased levels of free protein S in sickle cell plasma.

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Available abstract

Plasma levels of free protein S, a vitamin K-dependent anticoagulant, are decreased in persons with sickle cell anemia, but the etiology of the low levels is unknown. Protein S binds to phosphatidylserine-containing phospholipids in a calcium-dependent manner. Other studies have indicated that phosphatidylserine may be abnormally present on the outer surface of the membrane lipid bilayer of sickle cells and of the spectrin-depleted vesicles they shed in vivo. We studied the binding of purified, radiolabeled protein S to spectrin-depleted erythrocyte membrane vesicles and to density-separated fractions of sickle and normal erythrocytes. Calcium-dependent binding of protein S occurred with vesicles and with well-aerated dense irreversibly sickled cells, but not with well-aerated sickle discocytes or with normal erythrocytes. These data provide further evidence that phosphatidylserine is abnormally present on the outer surface of spectrin-depleted vesicles and of irreversibly sickled cells. In addition, protein S binding to such sickle membranes in vivo may be responsible, in part, for the decreased levels of free protein S in sickle cell plasma.

Key concepts: Vesicle, Chemistry, Erythrocyte membrane, Cell biology, Biophysics, Membrane, Biochemistry, Biology

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