Total absence of protein 4.2 and partial deficiency of band 3 in hereditary spherocytosis

GAG, and P854L, CCG-->CTG) and, additionally, the mutation: G714R, GGG-->AGG, located in a highly conserved position of transmembrane segment 9. The latter change was responsible for HS. In trans to allele Okinawa, the daughter displayed allele Fukuoka: G130R, GGA-->AGA, an allele known to alter the binding of protein 4.2 to band 3. The daughter presented with a more pronounced decrease of band 3, and lacked protein 4.2, resulting in aggravated haemolytic features. Although the father was not available for study, heterozygosity for allele Fukuoka has been documented in another individual who showed no clinical or haematological signs, and a normal content of band 3. We suggest that band 3 Okinawa binds virtually all the protein 4.2 in red cell precursors, band 3 Fukuoka being unable to do so, and that the impossibility of band 3 Okinawa incorporation into the membrane leads to degradation of the band 3 Okinawa protein 4.2 complex. In contrast, band 3 Fukuoka, free of bound protein 4.2, could then incorporate normally into the bilayer. Thus, protein 4.2 would not appear in the daughter's red cell membrane. -->
ISSN: 1365-2141
0007-1048
DOI: 10.1046/j.1365-2141.1997.4263231.x
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b38658f3693d3acbd2f2f250f44081d1
https://doi.org/10.1046/j.1365-2141.1997.4263231.x
Rights: CLOSED
Přírůstkové číslo: edsair.doi.dedup.....b38658f3693d3acbd2f2f250f44081d1
Autor: Hideho Wada, Takafumi Inoue, Sandrine Hayette, L Morle, A. Vallier, Fumihide Inoue, J. Delaunay, Nicole Alloisio, Yoshihito Yawata, Ayumi Yawata, Akio Kanzaki, Reiko Matsuyama
Rok vydání: 1997
Předmět:
Zdroj: British Journal of Haematology. 99:522-530
ISSN: 1365-2141
0007-1048
DOI: 10.1046/j.1365-2141.1997.4263231.x
Popis: Unlike previously reported cases with total protein 4.2 deficiency due to mutations in the EPB42 gene, we describe a total deficiency in protein 4.2 with normal EPB42 alleles. Hereditary spherocytosis (HS) was observed in a Japanese woman (unsplenectomized) and her daughter (splenectomized). The mother showed a partial deficiency in band 3 and a proportional reduction in protein 4.2. She was heterozygous for a novel allele of the EPB3 gene, allele Okinawa, which contains the two mutations that define the Memphis II polymorphism (K56E, AAG-->GAG, and P854L, CCG-->CTG) and, additionally, the mutation: G714R, GGG-->AGG, located in a highly conserved position of transmembrane segment 9. The latter change was responsible for HS. In trans to allele Okinawa, the daughter displayed allele Fukuoka: G130R, GGA-->AGA, an allele known to alter the binding of protein 4.2 to band 3. The daughter presented with a more pronounced decrease of band 3, and lacked protein 4.2, resulting in aggravated haemolytic features. Although the father was not available for study, heterozygosity for allele Fukuoka has been documented in another individual who showed no clinical or haematological signs, and a normal content of band 3. We suggest that band 3 Okinawa binds virtually all the protein 4.2 in red cell precursors, band 3 Fukuoka being unable to do so, and that the impossibility of band 3 Okinawa incorporation into the membrane leads to degradation of the band 3 Okinawa protein 4.2 complex. In contrast, band 3 Fukuoka, free of bound protein 4.2, could then incorporate normally into the bilayer. Thus, protein 4.2 would not appear in the daughter's red cell membrane.
Databáze: OpenAIRE
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