Ethnic variation in frequency of an allelic polymorphism of human Fcγ RIIA determined with allele specific oligonucleotide probes

Osborne, Jeanne M.; Chacko, George; Brandt, John; Anderson, Clark L.

doi:10.1016/0022-1759(94)90299-2

Cited by 122 publications

(108 citation statements)

References 49 publications

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“…FcgRIIa DNA was amplified as described by Osborne et al using gene-specific primers [32]: sense primer (5 0 -CAA GCC TCT GGT CAA GGT C-3 0 ) and antisense primer (5 0 -GAA GAG CTG CCC ATG CTG-3 0 ). The sense primer is upstream to the polymorphism encoding amino acid 131 in the second extracellular domain and does not distinguish between the genes for FcgRIIa, b or c. The antisense primer is located downstream of the polymorphism in the transmembrane domain and contains nine bases on the 3 0 end of the primer which are unique to FcgRIIa gene.…”

Section: Determination Of Fcgriia Allotypes By Allele-specific Polymementioning

confidence: 99%

“…FcgRIIa genotyping was performed using PCR amplification of genomic DNA (as described above), followed by Southern blotting using allele-specific probes end-labelled with 32 P-gATP as described by Osborne et al [32]. The probes detect a single nucleotide difference (G or A) at base 494 which results in an arginine (R131 allele) or histidine (H131 allele) at amino acid 131 of the FcgRIIa protein.…”

Section: Determination Of Fcgriia Allotypes By Southern Blottingmentioning

confidence: 99%

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No association between neutrophil FcγRIIa allelic polymorphism and anti-neutrophil cytoplasmic antibody (ANCA)-positive systemic vasculitis

Tse¹,

Abadeh

Mctiernan³

et al. 1999

Clinical and Experimental Immunology

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SUMMARYANCA, implicated as having a pathogenic role in systemic vasculitis, can activate tumour necrosis factor-alpha (TNF-a)-primed neutrophils by cross-linking surface-expressed ANCA antigens with neutrophil FcgRIIa receptors to release reactive oxygen species. The FcgRIIa receptor exists as polymorphic variants, R131 and H131, which differ in their ability to ligate human IgG2 and IgG3. Neutrophils homozygous for the FcgRIIa-H131 allotype bind more efficiently to IgG3 than the FcgRIIa-R131 allotype and are the only human FcgR which bind IgG2. Our aim was to determine whether the homozygous FcgRIIa-H131 individuals are more susceptible to developing ANCAassociated systemic vasculitis and nephritis due to differential IgG binding and activation. FcgRIIa allotype was determined by both allele-specific polymerase chain reaction (PCR) and Southern blotting with allele-specific oligonucleotide probes end-labelled with 32 P-gATP, after PCR amplification of genomic FcgRIIa DNA in 107 Caucasian patients with ANCA þ vasculitis (of whom 89 had renal disease) and 100 ethnically matched controls. Phenotyping of neutrophil FcgRIIa alleles was confirmed in some patients by quantitative flow cytometry using murine MoAbs 41H16 and IV.3. Of the patients with ANCA þ systemic vasculitis, 75 had ANCA with specificity for proteinase 3 and 32 with specificity for myeloperoxidase. Overall, no skewing in FcgRIIa allotypes was seen in patients compared with controls. No significant increase of the FcgRIIa-H131 allotype was found amongst patients irrespective of ANCA specificity, and no association between the FcgRIIa allotype and nephritis was found. Our data suggest that the FcgRIIa receptor allotype is not a major factor predisposing to the development of ANCA þ systemic vasculitis, or to nephritis.

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Section: Determination Of Fcgriia Allotypes By Allele-specific Polymementioning

confidence: 99%

Section: Determination Of Fcgriia Allotypes By Southern Blottingmentioning

confidence: 99%

No association between neutrophil FcγRIIa allelic polymorphism and anti-neutrophil cytoplasmic antibody (ANCA)-positive systemic vasculitis

Tse¹,

Abadeh

Mctiernan³

et al. 1999

Clinical and Experimental Immunology

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“…The sequences for all oligonucleotides are given in Table L In order to identify the l1Fc7R.II isoform distribution of EBV-B cell lines, a partial sequence of hFc7R.II was amplified using two primers that do not distinguish between the different isoforms of I1FC7RII: P63 [21], that anneals in the extracellular region, and BECFII-3 annealing in the transmembrane region. Subsequent hybridization of amplified DNA on Southern blots was then performed either with the hFc7RIIa-specific oligonucleotide probe P52 [21], or with BEC3int that anneals to the extracellular part of all isoforms of hFc7RII.…”

Section: A T E R Ia L S and M E T H O D Smentioning

confidence: 99%

“…Subsequent hybridization of amplified DNA on Southern blots was then performed either with the hFc7RIIa-specific oligonucleotide probe P52 [21], or with BEC3int that anneals to the extracellular part of all isoforms of hFc7RII.…”

Section: A T E R Ia L S and M E T H O D Smentioning

confidence: 99%

“…Southern blotting was performed by transferring DNA to Hybond-N + (Amersham International, Amersham, UK) in 0.4m NaOH, 25mM EDTA. Membranes were washed (2x SSC) and incubated in 30 ml Standard Hybridisation mix [21] (5x SSC, 0.1% laurylsarcosine, 0.02% SDS 1% Blocking Reagent (BoehringerMannheim, Mannheim, Germany) for 1.5 h at the optimal annealing temperature. After adding 25pmol hybridization probe incubation was continued for 2 h at the same temperature followed by a washing procedure at stringency of 2x SSC, 0.1% SDS, twice at room temperature (20°C) and twice at the hybridization temperature.…”

Section: A T E R Ia L S and M E T H O D Smentioning

confidence: 99%

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Analysis at the DNA Level of Human FcγRII Isoforms in Relation to the Polymorphic Binding of Murine IgG2b to Human B Cells

Tax¹,

Tamboer²,

Mensink

et al. 1996

Scand J Immunol

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Three classes o f hum an leucocyte FC7 receptors (I1FC7 R) have been identified so far: I1FC7 R I, hFc7 R II, and I1FC7RIIL Previous studies have dem onstrated th a t genetically determ ined differences between individuals exist both with respect to the binding of m urine Ig G l (m lg G l) to h F c7 receptors, and with respect to the binding of m urine IgG2b (mIgG2b). The polym orphism in binding o f m lg G l could be ascribed to I1FC7 R IIA , an isoform of UFbyRIL The authors have now investigated w hether one o f the isoforms of I1FC7 R II is also responsible for the polym orphism in binding o f m IgG 2b. In these studies the authors used EBV -transform ed hum an B cells th at dem onstrated either binding or no binding of m IgG2b in EA-rosetting assays. m R N A obtained from these cells was amplified by reverse transcriptase and polymerase chain reaction (RT-PCR). H ybridization experiments with the R T -P C R products revealed that the h F c7 RIIB but not the hFc7 R IIA isoform was present in these cells. D N A sequencing further dem onstrated that the nucleotide sequence of both the extracellular p a rt an d the cytoplasm ic moiety of I1FC7 RIIB was identical for all individuals tested, regardless o f their ability to bind m IgG 2b. These findings indicate that the polym orphic binding o f m IgG 2b cannot be ascribed to one o f the isoforms of I1FC7 RIL Since I1FC7 RI and h F c7 R III are not present on the cell surface of these cells, the authors conclude th at an Fc receptor different from the know n I1 FC7 receptors m ust be responsible for the polymorphic binding of m IgG 2b. These data further expand the com plexity of I1 FC7 R.

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Analysis of factors contributing to the formation of mononuclear cell aggregates (?escapees?) in flow cytometric immunophenotyping

et al. 1997

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Ethnic variation in frequency of an allelic polymorphism of human Fcγ RIIA determined with allele specific oligonucleotide probes

Cited by 122 publications

References 49 publications

No association between neutrophil FcγRIIa allelic polymorphism and anti-neutrophil cytoplasmic antibody (ANCA)-positive systemic vasculitis

No association between neutrophil FcγRIIa allelic polymorphism and anti-neutrophil cytoplasmic antibody (ANCA)-positive systemic vasculitis

Analysis at the DNA Level of Human FcγRII Isoforms in Relation to the Polymorphic Binding of Murine IgG2b to Human B Cells

Analysis of factors contributing to the formation of mononuclear cell aggregates (?escapees?) in flow cytometric immunophenotyping

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