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Blood, Vol. 92 No. 5 (September 1), 1998:
pp. 1707-1712
Expression of Proteins Controlling Transbilayer Movement of Plasma
Membrane Phospholipids in the B Lymphocytes From a Patient With Scott
Syndrome
Quansheng Zhou,
Peter J. Sims, and
Therese Wiedmer
From the Blood Research Institute of The Blood Center of Southeastern
Wisconsin, Milwaukee, WI.
Scott syndrome is a rare inherited bleeding disorder in which
platelets and other blood cells fail to promote normal assembly of the
membrane-stabilized proteases of the plasma coagulation system. The
defect in Scott blood cells is known to reflect inability to mobilize
phosphatidylserine from inner plasma membrane leaflet to the cell
surface in response to an elevation of Ca2+ at the
endofacial surface. To gain insight into the molecular basis of this
membrane defect, we examined the expression in Scott cells of plasma
membrane proteins that have been implicated to participate in the
accelerated transbilayer movement of plasma membrane PL. By both
reverse transcriptase-polymerase chain reaction (RT-PCR) and functional
assay, the level of expression of the multidrug resistance (MDR)1 and
MDR3 P-glycoproteins in immortalized B-lymphoblast cell lines from the
patient with Scott syndrome were indistinguishable from matched cell
lines derived from normal controls. Whereas the plasma membrane of
Scott cells are insensitive to activation of the plasma membrane PL
scramblase pathway, it had been shown that PL scramblase protein
isolated from detergent-solubilized Scott erythrocytes exhibits normal
function when incorporated into proteoliposomes (Stout JG, Basse F,
Luhm RA, Weiss HJ, Wiedmer T, Sims PJ: J Clin Invest 99:2232,
1997). Consistent with this finding in Scott erythrocytes, we found
that Scott lymphoblasts expressed normal levels of PL scramblase mRNA
and protein, and that the deduced sequence of PL scramblase in Scott
cells is identical to that of normal controls. These data suggest that
the defect in Scott syndrome is related either to aberrant
posttranslational processing of the PL scramblase polypeptide or to a
defect or deficiency in an unknown cofactor that is required for normal expression of plasma membrane PL scramblase function in situ, or
alternatively, reflects the presence of a detergent-dissociable inhibitor of this pathway.
© 1998 by The American Society of Hematology.
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