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Blood, 1 August 2002, Vol. 100, No. 3, pp. 1038-1047
RED CELLS
Cell-surface expression of RhD blood group polypeptide is
posttranscriptionally regulated by the RhAG glycoprotein
Isabelle Mouro-Chanteloup,
Anne Marie D'Ambrosio,
Pierre Gane,
Caroline Le Van
Kim,
Virginie Raynal,
Didier Dhermy,
Jean-Pierre Cartron, and
Yves Colin
From the Institut National de la Santé et de la
Recherche Médicale (INSERM) U76, Institut National de la
Transfusion Sanguine (INTS); and (D.D.) INSERM U409, Faculté de
Médecine Xavier Bichat, Paris, France.
In most cases, the lack of Rh in Rhnull red cells is
associated with RHAG gene mutations. We explored the role
of RhAG in the surface expression of Rh. Nonerythroid HEK293 cells,
which lack Rh and RhAG, or erythroid K562 cells, which endogenously express RhAG but not Rh, were transfected with RhD and/or RhAG cDNAs using cytomegalovirus (CMV) promoter-based expression
vectors. In HEK293 cells, a low but significant expression of RhD was
obtained only when RhAG was expressed at a high level. In K562 cells,
as expected from the opposite effects of the phorbol ester
12-O-tetradecanoyl phorbol 13-acetate (TPA) on erythroid
and CMV promoters, the levels of endogenous RhAG and recombinant RhD
transcripts were substantially decreased and enhanced upon TPA
treatment of RhD-transfected cells (K562/RhD), respectively. However,
flow cytometry and fluorescence microscopy analysis revealed a
decreased cell-surface expression of both RhAG and RhD proteins.
Conversely, TPA treatment of RhAG-transfected cells increased both the
transcript and surface expression levels of RhAG. When K562/RhD cells
were cotransfected by the RhAG cDNA, the TPA-mediated induction of
recombinant RhAG and RhD transcription was associated with an increased
membrane expression of both RhAG and RhD proteins. These results
demonstrate the role of RhAG as a strictly required posttranscriptional
factor regulating Rh membrane expression. In addition, because the
postulated 2:2 stoichiometry between Rh and RhAG observed in the native
red cell membrane could not be obtained in cotransfected K562 cells,
our study also suggests that as yet unidentified protein(s) might be
involved for optimal membrane expression of Rh.
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