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Blood, 15 August 2000, Vol. 96, No. 4, pp. 1566-1573
TRANSFUSION MEDICINE
Molecular heterogeneity of the Jknull phenotype:
expression analysis of the Jk(S291P) mutation found in
Finns
Frederic Sidoux-Walter,
Nicole Lucien,
Riikka Nissinen,
Pertti Sistonen,
Stephen Henry,
Joann Moulds,
Jean-Pierre Cartron, and
Pascal Bailly
From INSERM U76, INTS, Paris, France;
Finnish Red Cross Blood Transfusion Service, Helsinki,
Finland; Auckland Institute of Technology, Auckland,
New Zealand; University of Texas-Houston Medical School,
Houston, TX.
Polymerase chain reaction genotyping of 32 unrelated
Jknull individuals originating predominantly from Polynesia
and Finland indicated that all were homozygous for the JK*B
polymorphism and that 17 of 32, including the 14 Polynesians, carried a
3'-acceptor splice site mutation of intron 5 that resulted in the
skipping of exon 6 (called mutation Jk 6). The remaining 15 Jknull donors from Finland were homozygous for a new T871C
transition resulting in a S291P amino acid substitution at a consensus
N-glycosylation site of the Jk polypeptide.
Transcription-translation assays revealed that the Jk(S291P) mutant was
translated into a glycosylated component as efficiently as the
wild-type Jk polypeptide (wt Jk)] in the presence of microsomes, thus
indicating that the S291P mutation has no effect on the
N-glycosylation pattern of the Jk protein. Expression
studies in Xenopus oocytes revealed that the Jk(S291P) polypeptide functions as a urea transporter, but the transport activity
and the membrane expression level of the mutant protein was reduced to
a similar extent. A substantial fraction of the mutant protein was
retained intracellularly suggesting that the transit to the plasma
membrane was reduced, presumably because of the S P
mutation. After transfection in erythroleukemia K562 cells the
wild-type, but not the mutant, protein was efficiently expressed at the
cell surface. Because the Jk(S291P) mutant polypeptide was not present
in human red cells from Jknull individuals, expression data
in the erythroid context clearly indicates that the
SP mutation is the molecular basis of the
Finnish Jknull phenotype.
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