The Action of Seed and Other Reagents on HEMPAS Erythrocytes

Bird, G. W. G.; Wingham, June

doi:10.1159/000208011

Cited by 14 publications

(2 citation statements)

References 8 publications

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“…with anti-i, has recently been reported by Baines et a1 (1982). None of the erythrocytes from the CDA I1 patients studied here were agglutinated by the lectins from Arachis hypogaea (peanut, anti-T) or Safvia sclarea (anti-Tn); this has been reported by Bird & Wingham (1976) for the erythrocytes from other patients with CDA 11. Table I shows the sialic acid contents of red blood cells from CDA I1 patients A.H., J.H.…”

Section: Resultsmentioning

confidence: 43%

Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia Type II (CDA II)

et al. 1983

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The alterations in the erythrocyte membrane proteins of individuals with congenital dyserythropoietic anaemia (CDA II) were studied. Alterations were observed in both the erythrocyte sialoglycoproteins and erythrocyte anion transport protein (Band 3). There was a decrease in the apparent molecular weight of the major sialoglycoprotein alpha (glycophorin A) as well as a general reduction in the intensity of staining of all the sialoglycoproteins by the PAS stain. Sialoglycoprotein alpha isolated from CDA II erythrocytes contained 30% less sialic acid than normal alpha. The anion transport protein of CDA II erythrocytes migrated as a band with a lower molecular weight than the normal protein on SDS-gel electrophoresis. The CDA II anion transport protein had a substantially reduced content of N-acetylglucosamine and galactose, which probably reflects a reduction in the number of N-acetyl-lactosamine units carried by the protein. Our results suggest that there is a general defect in glycosylation of the major membrane glycoproteins of CDA II erythrocytes. We suggest that this glycosylation defect is a consequence of bone marrow stress.

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Section: Resultsmentioning

confidence: 43%

Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia Type II (CDA II)

et al. 1983

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“…The subunits have been sequenced [7,8] and are highly homologous to that of Jacalin. It was reported that this lectin reacts more strongly with polyagglutinable red cells from patients with hereditary erythroblastic multinuclearity than with En (a ) ) erythrocytes which lack glycophorin [9]. MPA can interact with certain bacterial polysaccharides [10] and can also be used as a specific marker for a glycoprotein on type 2 aveolar cells [11].…”

Section: Introductionmentioning

confidence: 99%

Polyvalent GalNAcα1→Ser/Thr (Tn) and Galβ1→3GalNAcα1→Ser/Thr (T α) as the most potent recognition factors involved in Maclura pomifera agglutinin–glycan interactions

2005

J Biomed Sci

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The agglutinin isolated from the seeds of Maclura pomifera (MPA) recognizes a mucin-type disaccharide sequence, Galbeta1-->3GalNAc (T) on a human erythrocyte membrane. We have utilized the enzyme-linked lectinosorbent assay (ELLSA) and inhibition assay to more systematically analyze the carbohydrate specificity of MPA with glyco-recognition factors and mammalian Gal/GalNAc structural units in lectin-glycoform interactions. From the results, it is concluded that the high densities of polyvalent GalNAcalpha1-->Ser/Thr (Tn) and Galbeta1-->3GalNAcalpha1-->Ser/Thr (T(alpha)) glycotopes in macromolecules are the most critical factors for MPA binding, being on a nanogram basis 2.0 x 10(5), 4.6 x 10(4) and 3.9 x 10(4) more active than monovalent Gal, monomeric T and Tn glycotope, respectively. Other carbohydrate structural units in mammalian glycoconjugates, such as human blood group Sd (a+) related disaccharide (GalNAcbeta1-->4Gal) and Pk/P1 active disaccharide (Galalpha1-->4Gal) were inactive. These results demonstrate that the configurations of carbon-4 and carbon-2 are essential for MPA binding and establish the importance of affinity enhancement by high-density polyvalencies of Tn/T glycotopes in MPA-glycan interactions. The overall binding profile of MPA can be defined in decreasing order as high density of polyvalent Tn/T(alpha) (M.W. > 4.0 x 10(4)) >> Tn-containing glycopeptides (M.W. < 3.0 x 10(3)) > monomeric T/Tn and P (GalNAcbeta1-->3Gal) > GalNAc > Gal >> Man, L: ARA: , D: Fuc and Glc (inactive). Our findings should aid in the selection of this lectin for elucidating functions of carbohydrate chains in life processes and for applications in the biomedical sciences.

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Other Red Cell Antigens

Klein¹,

Anstee²

2005

Mollison's Blood Transfusion in Clinical Medicine

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The Action of Seed and Other Reagents on HEMPAS Erythrocytes

Cited by 14 publications

References 8 publications

Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia Type II (CDA II)

Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia Type II (CDA II)

Polyvalent GalNAcα1→Ser/Thr (Tn) and Galβ1→3GalNAcα1→Ser/Thr (T α) as the most potent recognition factors involved in Maclura pomifera agglutinin–glycan interactions

Other Red Cell Antigens

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