Scramblase is an enzyme, present in the cell membrane, that can transport (scramble) the negatively charged phospholipids from the inner-leaflet to the outer-leaflet, and vice versa.

Patients with sickle cell disease exhibit a fraction of erythrocytes with an aberrantly enhanced exposure of phosphatidyl serine on their surface.

As the erythrocytes of these patients have an enhanced oxidative stress, it is probable that increased scramblase activity might play a role in the etiology of the disease.

The structure of the nuclear localisation sequence of scramblase PLSCR1 complexed to importin was determined using X-ray diffraction with a resolution of 2.20 Ångströms.

PLSCR3 has been proposed to be involved in this translocation from the inner to the outer membrane that is essential for maintaining the mitochondrial architecture, mass, and transmembrane potential.

Blood plasma of these mice showed elevated levels of non-high-density lipoproteins, cholesterol, triglycerides, non-esterified fatty acids, and leptin, but low adiponectin content.

Several enzyme complexes of blood coagulation cascade such as tenase and prothrombinase are activated by the cell surface exposure of the phosphatidylserine.

PLSCRs are supposed to play an important role in both intrinsic and extrinsic apoptotic responses that are linked to each other via the activation of caspase 8.

Activated caspase 8 causes the cleavage of the amino terminal portion of the cytosolic protein Bid to generate t-Bid that is translocated into mitochondria during apoptosis.

An early morphological event in both the extrinsic and the intrinsic apoptotic pathways is the surface exposure of the phospholipid phosphatidylserine, about 96% of which normally reside in the cytosolic leaflet of the plasma membrane.

Phosphatidylserine is translocated to the exoplasmic leaflet by the activation of scramblases, leading to pro-coagulant properties and providing a phagocytic signal to the macrophages that engulf and clear the apoptotic cells.