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Multiple Rh messenger RNA isoforms are produced by alternative splicing
C Le Van Kim, B Cherif-Zahar, V Raynal, I Mouro, M Lopez, JP Cartron and Y Colin
Unite INSERM U76, Institut National de Transfusion Sanguine, Paris, France.
Three Rh-related cDNAs have been isolated from a human bone marrow cDNA
library and by polymerase chain reaction (PCR) amplification of human bone
marrow and erythroblast mRNAs. They potentially encode a family of Rh
protein isoforms that exhibit several unexpected structural properties as
compared with the Rh polypeptide encoded by the cDNA clone identified
previously. These modifications include several peptide deletions, the
predicted alteration of Rh protein topology within the cell membrane,
variations in the number and surface exposition of cysteine residues, and
the generation of new C-terminal polypeptide segments caused by frameshift
mutations. The four Rh mRNAs now described correspond to different splicing
isoforms transcribed from the same Rh gene, and all exist in the same cell
lineage (erythroid). Moreover, PCR experiments indicated that at least
three of these RNA species exist in reticulocytes from donors with
different commonly expressed Rh phenotypes. Although the translated
proteins have not yet been characterized, these results suggest that the
two genes at the RH locus may direct the synthesis of several protein
species possibly corresponding to different Rh antigenic variants.
Volume 80,
Issue 4,
pp. 1074-1078,
08/15/1992
Copyright © 1992 by The American Society of Hematology

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