A clinically applicable method for determining the three major alleles at the Duffy (FY) blood group locus using polymerase chain reaction with allele‐specific primers

Olsson, Martin L.; Hansson, Carola; Avent, Neil D.; Åkesson, Ingvar; Green, C A; Daniels, G.L.

doi:10.1046/j.1537-2995.1998.38298193099.x

Cited by 80 publications

(71 citation statements)

References 19 publications

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“…Patient A's sample was typed by serology as Fy (a-b-) which is very rare in Europeans but common in West Africans. 48 Subsequent molecular investigations, using allele-specific primers 49,50 and the blood group genotyping system BLOODchip, 42,51 demonstrated that patient A has the rare FY*0/FY*X genotype which predicts weakened Fy b antigen expression on erythrocytes. This weakened antigen expression, coupled with hemizygosity for the FY*B allele, made serological detection of the Fy b antigen very difficult and could have led to the erroneous interpretation that the Duffy antigen was diminished, as is the case in the 4.1R(-) mouse.…”

Section: Blood Group Antigen Expression On 41r(-) Erythrocytesmentioning

confidence: 99%

4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins

Jeremy¹,

Plummer²,

Head³

et al. 2009

Haematologica

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BackgroundProtein 4.1R is an important component of the red cell membrane skeleton. It imparts structural integrity and has transmembrane signaling roles by direct interactions with transmembrane proteins and other membrane skeletal components, notably p55 and calmodulin. Design and MethodsSpontaneous and ligation-induced phosphatidylserine exposure on erythrocytes from two patients with 4.1R deficiency were studied, using CD47 glycoprotein and glycophorin C as ligands. We also looked for protein abnormalities in the 4.1R -based multiprotein complex. ResultsPhosphatidylserine exposure was significantly increased in 4.1R-deficient erythrocytes obtained from the two different individuals when ligands to CD47 glycoprotein were bound. Spontaneous phosphatidylserine exposure was normal. 4.1R, glycophorin C and p55 were missing or sharply reduced. Furthermore there was an alteration or deficiency of CD47 glycoprotein and a lack of CD44 glycoprotein. Based on a recent study in 4.1R-deficient mice, we found that there are clear functional differences between interactions of human red cell 4.1R and its murine counterpart. ConclusionsGlycophorin C is known to bind 4.1R, and we have defined previously that it also binds CD47. From our evidence, we suggest that 4.1R plays a role in the phosphatidylserine exposure signaling pathway that is of fundamental importance in red cell turnover. The linkage of CD44 to 4.1R may be relevant to this process. CD44 and CD47 glycoproteins. Haematologica 2009;94:1354-1361. doi:10.3324/haematol.2009 This is an open-access paper. 4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins

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Section: Blood Group Antigen Expression On 41r(-) Erythrocytesmentioning

confidence: 99%

4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins

Jeremy¹,

Plummer²,

Head³

et al. 2009

Haematologica

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“…El programa de PCR, los oligonucleótidos partidores y la estrategia de amplificación utilizada fueron tomadas de Olsson y cols 41 . Una vez realizada la amplificación, los productos obtenidos se resolvieron en geles de agarosa 1,5 a 2% en buffer TAE, y visualizados a fuente de radiación UV por adición de bromuro de etidio.…”

Section: Rev Méd Chile 2004; 132: 663-672 a R T í C U L O D E I N V Eunclassified

“…El gen FY se ubica en el cromosoma 1, en la posición 1q21-q22 y codifica para una proteína de 338 aminoáci-dos 38 . Este sistema posee dos alelos FYA y FYB con relación de codominancia entre ellos y donde el polimorfismo FYA/FYB radica en una mutación en el nucleótido 131 (G A) que genera un cambio aminoacídico y que otorga la especificidad antigénica exhibida [39][40][41] . Además de éstos, se ha caracterizado otro alelo que presenta frecuencias inusualmente altas denominado FY nulo o silente (FY-) en población de origen negroide.…”

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Caracterización genético molecular de habitantes de Caleta Paposo, último reducto Chango en Chile

Moraga

et al. 2004

Rev. méd. Chile

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“…Because we did not have access to the Fy phenotype in our cohort, we genotyped the c.-67 nucleotide position of the DARC gene by direct sequencing, which is characterized by a T>C substitution at the homozygous state in Fy(a-b-) samples [32]. 31 out of 47 samples (66.0%) were predicted to be Fy(a-b-) (table 2), which is in the range of what reported before (63.0%; χ 2 = 0.12; p = 0.7276) [33] and confirms the African origin of our cohort. Of this subset, 17 were potentially of clinical interest (table 2), which is significantly more than what was observed by Kappler-Gratias et al [30] (6.5% vs. 54.8% in this study; χ 2 = 17.07; p = 0.000036).…”

Section: Resultsmentioning

confidence: 68%

Insights into <b>RHCE</b> Molecular Analysis in Samples with Partial <b>D</b> Variants: the Experience of Western France

Fichou¹,

Maréchal

Scotet³

et al. 2015

Transfus Med Hemother

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Background: Although systematic blood group genotyping of patients/donors is virtually possible, serological studies remain the gold standard to identify samples of clinical interest that may be further genotyped. In this context, we sought to identify variant D alleles that are likely to be clinically relevant in terms of other Rh antigens in a subset of population genotyped in Western France. Methods: Samples presenting with the RHD*weak D type 4.2.2 allele (n = 47) were selected for the study. RHCE exons 1-7 were directly sequenced, and expression of Rh antigens was predicted on the basis of the molecular data. Results: Of the 47 samples tested, 19 (40.4%) were predicted to be of potential clinical interest. Moreover, we could show that selecting the samples to be genotyped by the nature of their variant D allele (i.e., RHD*weak D type 4.2.2 allele) rather than by their Duffy-null status appears to increase significantly the likelihood of identifying clinically relevant individuals for Rh status. Conclusion: On the basis of our findings we suggest that all individuals genotyped as weak D type 4.2.2 should be systematically screened for RHCE variants by molecular analysis on a routine basis.

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A clinically applicable method for determining the three major alleles at the Duffy (FY) blood group locus using polymerase chain reaction with allele‐specific primers

Cited by 80 publications

References 19 publications

4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins

4.1R-deficient human red blood cells have altered phosphatidylserine exposure pathways and are deficient in CD44 and CD47 glycoproteins

Caracterización genético molecular de habitantes de Caleta Paposo, último reducto Chango en Chile

Insights into <b>RHCE</b> Molecular Analysis in Samples with Partial <b>D</b> Variants: the Experience of Western France

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