scholarly journals Eosin-5-maleimide binding to band 3 and Rh-related proteins forms the basis of a screening test for hereditary spherocytosis

2003 ◽  
Vol 124 (1) ◽  
pp. 106-113 ◽  
Author(s):  
May-Jean King ◽  
Jonathan S. Smythe ◽  
Rosey Mushens
Keyword(s):  
Screening Test ◽  
Hereditary Spherocytosis ◽  
Band 3 ◽  
Related Proteins

Hereditary Spherocytosis: How the New Information Provided by the Routine Hematology Analysers May Help in Its Differential Diagnosis or Flagging

Blood ◽  
2012 ◽  
Vol 120 (21) ◽  
pp. 5163-5163
Author(s):  
Susanna Barella ◽  
Ramon Simon-Lopez ◽  
Nicola Di Gaetano ◽  
Renzo Galanello
Keyword(s):  
Research Funding ◽  
Roc Analysis ◽  
Hereditary Spherocytosis ◽  
Osmotic Fragility ◽  
Peripheral Blood Smear ◽  
Band 3 ◽  
Screening Tests ◽  
New Information ◽  
Related Proteins ◽  
Best Parameters

Abstract Abstract 5163 Introduction: Hereditary Spherocytosis (HS) is one of the most common inherited hemolytic anemias. Many of them are autosomal dominant, being about 25% of the cases transmitted recessively. Diagnostic of HS: Classic testing for HS includes: Hematologic testing of red blood cell indices (RDW, MCHC, Reticulocyte count), peripheral blood smear (presence of spherocytes), osmotic fragility and Eosin-5-maleimide binding to band 3 and Rh-related proteins forms that may be used as screening tests for hereditary spherocytosis. Objective: Recently have been developed new parameters and information in the new automated hematology analyzer called DxH8008™ from Beckman Coulter as @MSCV (@Mean Sphered Cell Volume), @RSF, @MAF, @ LHD%. All this parameters may be used to create flagging for laboratory use only (LUO) or Research use only (RUO). The purpose of this study is to investigate the possible use or utility of this new information for the screening/flagging of Hereditary Spherocytosis. There are previous studies showing the possible benefit of using MCV minus @MSCV for the detection/flagging of cases with spherocytes. Patient and Methods: We have collected 28 patients with Hereditary Spherocytosis. All of them were confirmed by red cell morphology, osmotic fragility and Eosin-5-maleimide binding to band 3 and Rh-related proteins forms. Results: Using ROC analysis, the best parameters differentiating the Hereditary Spherocytosis from the normals were: RET% (AUC 0. 996), MCV - @MSCV (AUC 0. 996), @MSCV (AUC 0. 969), RDW(AUC 0. 892), MCHC (AUC 0. 860), HGB (AUC 0. 787). Using ROC analysis, the best parameters differentiating the Hereditary Spherocytosis from other anemias (excluding normals)were: MCV - @MSCV (AUC 0. 991), MCHC (AUC 0. 987), RET% (AUC 0. 857). Disclosures: Simon-Lopez: Beckman Coulter: @LHD, @MAF, @RSF, @LHD, @MAF, @RSF Patents & Royalties, Employment. Di Gaetano:Instrumentation Laboratory spa: Work for a distributor of Beckman Coulter Instruments in Italy Other. Galanello:Novartis: Research Funding, Speakers Bureau; Apopharma: Research Funding, Speakers Bureau; Ferrokin: Research Funding.

scholarly journals Band 3 Cape Town (E90K) causes severe hereditary spherocytosis in combination with band 3 Prague III

2001 ◽  
Vol 113 (3) ◽  
pp. 689-693 ◽  
Author(s):  
Natalie A. Bracher ◽  
Cheryl A. Lyons ◽  
Glynn Wessels ◽  
Erna Mansvelt ◽  
Thérèsa L. Coetzer
Keyword(s):  
Hereditary Spherocytosis ◽  
Cape Town ◽  
Band 3

scholarly journals Modulation of Clinical Expression and Band 3 Deficiency in Hereditary Spherocytosis

Blood ◽  
1997 ◽  
Vol 90 (1) ◽  
pp. 414-420 ◽  
Author(s):  
N. Alloisio ◽  
P. Texier ◽  
A. Vallier ◽  
M.L. Ribeiro ◽  
L. Morlé ◽  
...  
Keyword(s):  
Binding Sites ◽  
Hereditary Spherocytosis ◽  
Novel Mutation ◽  
Band 3 ◽  
Anion Exchanger 1 ◽  
Severe Clinical Picture ◽  
In Trans ◽  
Novel Alleles ◽  
Pronounced Reduction ◽  
Compound Heterozygotes

Abstract We present two novel alleles of the anion-exchanger 1 (AE1) gene, allele Coimbra and allele Mondego. Allele Coimbra (V488M, GTG → ATG) affects a conserved position in the putative second ectoplasmic loop of erythrocyte band 3. In 15 simple heterozygotes, it yielded a mild form of hereditary spherocytosis (HS) with band 3 deficiency (−20% ± 2%) and a reduced number of 4,4′-diisothiocyano-1,2-diphenylethane-2,2′-disulfonate (H2DIDS) binding sites (−35%). However, two additional heterozygotes presented with an aggravated HS and a more pronounced reduction of band 3 (−40%) and of H2DIDS binding sites (−48%). They carried, in trans to allele Coimbra, allele Mondego, defined by two mutations: E40K, GAG → AAG, the known mutation Montefiore, and P147S, CCT → TCT, a novel mutation, both located in the cytoplasmic domain of band 3. Allele Mondego itself resulted in no clinical or hematologic HS signs in the simple heterozygous state. Yet it yielded a slight decrease in band 3 (−6% to −12%) and in the number of H2DIDS binding sites (−19%). Thus, the more pronounced decrease in band 3 in the two compound heterozygotes derived from the additive effects of two unequally expressed AE1 alleles, resulting in a more severe clinical picture.

scholarly journals Combined spectrin and ankyrin deficiency is common in autosomal dominant hereditary spherocytosis

Blood ◽  
1993 ◽  
Vol 82 (10) ◽  
pp. 2953-2960 ◽  
Author(s):  
P Savvides ◽  
O Shalev ◽  
KM John ◽  
SE Lux
Keyword(s):  
Blood Cell ◽  
Red Blood Cell ◽  
Autosomal Dominant ◽  
Hereditary Spherocytosis ◽  
Band 3 ◽  
Normal Range ◽  
Dominant Form ◽  
Autosomal Dominant Form ◽  
The Common ◽  
Ankyrin Deficiency

Abstract The common autosomal dominant form of hereditary spherocytosis (HS) has been genetically linked to defects of the erythroid ankyrin gene in a few families; however, the frequency of ankyrin deficiency and its relationship to red blood cell (RBC) spectrin content are unknown. To test these questions, we measured RBC spectrin and ankyrin by radioimmunoassay in 39 patients from 20 families with dominant HS. Normal RBCs contained 242,000 +/- 20,500 spectrin heterodimers and 124,500 +/- 11,000 ankyrins per cell. In dominant HS, RBC spectrin and ankyrin ranged from about 40% to 100% of normal and were continuously distributed. Measurements in the same patient on different occasions were reproducible (+/- 5% to 10%) and RBCs from affected members of a kindred contained similar amounts of spectrin and ankyrin (+/- 3% to 4%). Spectrin and ankyrin levels were almost always less than the assay controls, but were less than the normal range in only 75% and 80% of kindreds, respectively. Remarkably, the degree of RBC spectrin and ankyrin deficiency was very similar in 19 of 20 HS kindreds. One otherwise typical family differed, with marked ankyrin deficiency (45% of control) and a relatively mild spectrin deficit (81%). We conclude that most patients with dominant HS have combined ankyrin and spectrin deficiency and that the two proteins are usually about equally deficient, suggesting that defects in ankyrin expression, ankyrin stability, or ankyrin band 3 (AE1) interactions may be common in dominant HS.

scholarly journals Characterization of 13 novel band 3 gene defects in hereditary spherocytosis with band 3 deficiency

Blood ◽  
1996 ◽  
Vol 88 (11) ◽  
pp. 4366-4374 ◽  
Author(s):  
P Jarolim ◽  
JL Murray ◽  
HL Rubin ◽  
WM Taylor ◽  
JT Prchal ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Autosomal Dominant ◽  
Hereditary Spherocytosis ◽  
Gene Mutations ◽  
Band 3 ◽  
Red Cell Membrane ◽  
Cell Membrane Proteins ◽  
Gene Defects ◽  
Relative Deficiency ◽  
Peripheral Blood Smears

Abstract Hereditary spherocytosis (HS) is a common hemolytic anemia of variable clinical expression. Pathogenesis of HS has been associated with defects of several red cell membrane proteins including erythroid band 3. We have studied erythrocyte membrane proteins in 166 families with autosomal dominant HS. We have detected relative deficiency of band 3 in 38 kindred (23%). Band 3 deficiency was invariably associated with mild autosomal dominant spherocytosis and with the presence of pincered red cells in the peripheral blood smears of unsplenectomized patients. We hypothesized that this phenotype is caused by band 3 gene defects. Therefore, we screened band 3 DNA from these 38 kindred for single strand conformational polymorphisms (SSCP). In addition to five mutations detected previously by SSCP screening of cDNA, we detected 13 new band 3 gene mutations in 14 kindred coinherited with HS. These novel mutations consisted of two distinct subsets. The first subset included seven nonsense and frameshift mutations that were all associated with the absence of the mutant mRNA allele from reticulocyte RNA, implicating decreased production and/or stability of mutant mRNA as the cause of decreased band 3 synthesis. The second group included five substitutions of highly conserved amino acids and one in-frame deletion. These six mutations were associated with the presence of comparable levels of normal and mutant band 3 mRNA. We suggest that these mutations interfere with band 3 biosynthesis leading thus to the decreased accumulation of the mutant band 3 allele in the plasma membrane.

scholarly journals Modulation of Clinical Expression and Band 3 Deficiency in Hereditary Spherocytosis

Blood ◽  
1997 ◽  
Vol 90 (1) ◽  
pp. 414-420 ◽  
Author(s):  
N. Alloisio ◽  
P. Texier ◽  
A. Vallier ◽  
M.L. Ribeiro ◽  
L. Morlé ◽  
...  
Keyword(s):  
Binding Sites ◽  
Hereditary Spherocytosis ◽  
Novel Mutation ◽  
Band 3 ◽  
Anion Exchanger 1 ◽  
Severe Clinical Picture ◽  
In Trans ◽  
Novel Alleles ◽  
Pronounced Reduction ◽  
Compound Heterozygotes

We present two novel alleles of the anion-exchanger 1 (AE1) gene, allele Coimbra and allele Mondego. Allele Coimbra (V488M, GTG → ATG) affects a conserved position in the putative second ectoplasmic loop of erythrocyte band 3. In 15 simple heterozygotes, it yielded a mild form of hereditary spherocytosis (HS) with band 3 deficiency (−20% ± 2%) and a reduced number of 4,4′-diisothiocyano-1,2-diphenylethane-2,2′-disulfonate (H2DIDS) binding sites (−35%). However, two additional heterozygotes presented with an aggravated HS and a more pronounced reduction of band 3 (−40%) and of H2DIDS binding sites (−48%). They carried, in trans to allele Coimbra, allele Mondego, defined by two mutations: E40K, GAG → AAG, the known mutation Montefiore, and P147S, CCT → TCT, a novel mutation, both located in the cytoplasmic domain of band 3. Allele Mondego itself resulted in no clinical or hematologic HS signs in the simple heterozygous state. Yet it yielded a slight decrease in band 3 (−6% to −12%) and in the number of H2DIDS binding sites (−19%). Thus, the more pronounced decrease in band 3 in the two compound heterozygotes derived from the additive effects of two unequally expressed AE1 alleles, resulting in a more severe clinical picture.

cDNA cloning and localization of a band 3-related protein from ileum

1992 ◽  
Vol 263 (3) ◽  
pp. G345-G352 ◽  
Author(s):  
A. Chow ◽  
J. W. Dobbins ◽  
P. S. Aronson ◽  
P. Igarashi
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Basolateral Membrane ◽  
Membrane Vesicles ◽  
Band 3 ◽  
Related Protein ◽  
Rabbit Ileum ◽  
Molecular Identity ◽  
Polymerase Chain ◽  
Related Proteins

A Cl(-)-HCO3- exchanger in the brush-border membrane mediates active Cl- absorption and regulates intracellular pH in rabbit ileum. The molecular identity of the ileal Cl(-)-HCO3- exchanger has not been established. The best-characterized plasma membrane Cl(-)-HCO3- exchanger is erythroid band 3. Structurally related proteins in nonerythroid tissues comprise an anion exchanger (AE) family. We used the polymerase chain reaction to amplify and clone a cDNA encoding an ileal band 3-related protein (B3RP) from rabbit ileal enterocytes. The composite sequence is 3,909 bp and is predicted to encode a protein of 136 kDa. The deduced amino acid sequence is 95% identical to murine renal AE2, indicating that ileal B3RP is rabbit AE2. Antisera generated against a cytoplasmic fragment of ileal B3RP recognized a 160- to 170-kDa polypeptide in the brush-border membrane, but not the basolateral membrane, of ileal crypt and villus enterocytes. This correlates with previous studies indicating that a Cl(-)-HCO3- exchange is present in brush-border but not basolateral membrane vesicles from rabbit ileal enterocytes. We conclude that ileal B3RP is a product of the AE gene family, and is present in the brush-border of ileal enterocytes, where it may mediate Cl(-)-HCO3- exchange.

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