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Vol. 57, Issue 1, 24-35, January 2000
Departments of Pharmaceutical Sciences (V.L., D.S., E.G.S.,L.-B.L.,
J.D.S.) and Experimental Hematology (P.H.), St. Jude Children's
Research Hospital, Memphis, Tennessee; and the Department of Medicine & Pharmacology (R.B.K.), Vanderbilt University, Nashville, Tennessee.
Sister of P-glycoprotein (SPGP), a novel murine cDNA and member
of the ATP-binding cassette superfamily highly homologous to
P-glycoprotein (Pgp), was cloned. Moreover, its genomic clone was
isolated and localized to chromosome 2 by fluorescence in situ
hybridization. SPGP was functionally evaluated relative to MDR1
after subcloning SPGP cDNA into a retroviral bicistronic vector capable
of expressing both SPGP and the green fluorescent protein. LLC-PK1 and
MDCKII cells were transduced with this retrovirus and SPGP-positive
clones were isolated. Drug uptake and efflux was compared in cells
ectopically expressing either SPGP or human MDR1. SPGP
cells had decreased uptake of taurocholate and vinblastine compared
with LLC-PK1 cells. Additional studies revealed that vinblastine efflux
was accelerated by SPGP compared with LLC-PK1. Further comparison
revealed that although MDR1 easily impaired uptake of vincristine,
daunomycin, paclitaxel, and digoxin, SPGP had no effect on uptake of
these drugs. However, further studies demonstrated that, like MDR1,
SPGP effluxed calcein-acetoxymethyl ester (AM). Unlike MDR1,
SPGP was incapable of effluxing rhodamine 123. Although cyclosporine A
and reserpine blocked calcein-AM transport by MDR1, these drugs had
either minimal or no effect, respectively, on blocking SPGP efflux of
calcein-AM. In contrast, ditekiren, a linear hexapeptide, readily and
preferentially inhibited SPGP efflux of calcein-AM. Further studies
with three structural analogs of ditekiren revealed that one analog
inhibited SPGP efflux of calcein-AM, although not as potently as
ditekiren. These are the first studies to reveal that SPGP has distinct
transport properties compared with MDR1.
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