The Degradation of M and N Blood Group Glycoproteins and Glycopeptides with Alkaline Borohydride

Lisowska, Elwira

doi:10.1111/j.1432-1033.1969.tb00727.x

Cited by 55 publications

(32 citation statements)

References 19 publications

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“…[ 35] have shown that the polyagglutinable cell population has a diminuition or abolition of the receptor sites for MN-antibodies and the lectins from Vicia graminea and Arachis hypogoea which are directed against alkali labile NA and Gal, respectively [11,13,16,26,32,33].…”

Section: -Jv-acetylneuraminyl-(2-*-3)-/j-d-galactosyl-(l-*-3)-[a-7v-amentioning

confidence: 99%

“…In Tn-syndrome a rare condition of acquired mixed field polyagglutinability with facultative hemolytic anemia, leucocytopenia and thrombocy topenia, a proportion of the red cells has a lowered sialic acid (NA) content and consequently a decreased electrophoretic mobility [ [26,37,38], the hypothesis was put forward that Tn-polyagglutinable erythro cytes have a deficiency of alkali-labile NA and galactose (Gal) [8], Experi mental evidence for this was obtained from the following observations : Tnantigen is uncovered by removal of NA and Gal from normal erythrocyte glycoproteins. Subsequent alkaline borohydride degradation in order to split off the peptide-linked GalNAc leads to a destruction of the receptor site.…”

Section: Introductionmentioning

confidence: 99%

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Molecular Basis of Tn-Polyagglutinability

Dahr¹,

Uhlenbruck²,

Gunson³

et al. 1975

Vox Sanguinis

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Spectrophotometric and gas-liquid chromatographic analyses on the carbohydrate moiety of tryptic erythrocyte glycopeptides from persons with Tn-syndrome reveal a selective lowering of the galactose and sialic acid content, the degree being dependent on the percentage of polyagglutinable cells. Alkaline borohydride specifically releases N-acetylgalactosaminitol, and the amount is correlated to the percentage of pathological erythrocytes. It is concluded that the alkali-labile carbohydrate chains of Tn-polyagglutinable red cells solely consist of TV-acetylgalactosamine linked to serine or threonine. Experiments with heterophile agglutinins whose specificity is known are in line with the above-mentioned results. As judged from SDS-polyacrylamide gel electrophoresis the three major membrane glycoproteins are affected to a different extent by the defect.

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Section: -Jv-acetylneuraminyl-(2-*-3)-/j-d-galactosyl-(l-*-3)-[a-7v-amentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular Basis of Tn-Polyagglutinability

Dahr¹,

Uhlenbruck²,

Gunson³

et al. 1975

Vox Sanguinis

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“…The NV, activity is also confined to alkali-labile oligosaccharide chains [8], but is significantly enhanced after the release of sialic acid from the glycoproteins [14-161. The increase of Nvg activity on desialization of M and N antigens reached for both antigens a similar level.…”

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confidence: 99%

Modification of Amino Groups of Human‐Erythrocyte Glycoproteins and the New Concept on the Structural Basis of M and N Blood‐Group Specificity

Lisowska¹,

Duk²

1975

European Journal of Biochemistry

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1.Various kinds of modification of amino groups of M and N blood group glycoproteins abolished their capacity to inhibit rabbit and human anti-M and anti-N sera.2. The reversible modification of amino groups revealed that M and N blood group activity was restored after the removal of amino-group-blocking residues.3. Modification of amino groups had an entirely different effect on the reactivity of red cell glycoproteins with Vicia graminea agglutinin. The serological activity of N glycoprotein towards Vicia graminea anti-N agglutinin was unchanged, whereas the weak activity of M glycoprotein towards this anti-N agglutinin was increased to the level of that of N glycoprotein.4. These results indicate that there is a structural difference between M and N glycoproteins, which resides beyond the oligosaccharide chains. It suggests in turn that M and N blood group specificity is determined by amino acid sequence in the peptide chains of red cell glycoproteins.The M and N blood group receptors are located on the major glycoprotein of human erythrocyte membrane. It has been known that for M and N blood group activity sialic acid residues are required [l -71, and that this activity is associated with alkali-labile, sialic-acid-rich oligosaccharide chains [8 -101. Springer et al. [11,12] reported that N receptors were differentiated from M receptors by the presence of terminal b-galactosyl residues. The small amount of specific receptors among many unspecific oligosaccharide chains could justify the fact that no conclusive chemical evidence for the difference in structure of oligosaccharides of M and N glycoproteins has been reported so far. We found [13] that modification of amino groups of the glycoproteins abolished their capacity to inhibit rabbit anti-M and anti-N sera, and this finding was confirmed later by Ebert et ul. [4]. It drew attention to the possible role of the peptide chain in M and N blood group activity.The activity of red cell glycoproteins against anti-N lectin from Viciu graminea seeds (NVg activity) has entirely different structural requirements. The NV, activity is also confined to alkali-labile Abbreviation. Nyg activity, the serological activity directed toward Viciu graminea anti-N agglutinin.oligosaccharide chains [8], but is significantly enhanced after the release of sialic acid from the glycoproteins [14-161. The increase of Nvg activity on desialization of M and N antigens reached for both antigens a similar level. The Nvg activity was not affected by the modification of amino groups of N glycoprotein To shed more light on the structural differences between M and N antigenic determinants, further experiments on the modification of erythrocyte glycoprotein amino groups were undertaken, with special attention to the following problems. (a) The significance of amino groups in the reaction of glycoproteins with human anti-M and anti-N sera; (b) the reversibility of the serological effects of modification of amino groups, and (c) the effect of modification of amino groups on the NYg activity of...

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“…The alkalilabile oligosaccharides [4,8,20] with un changed sialic acid residues [4,5,7,9,14] are required for the reaction of M and N antigens with specific antisera. Chemical studies have not revealed, so far, any struc tural difference between M and N glyco proteins.…”

Section: Introductionmentioning

confidence: 99%

Specific Antibodies for Desialized M and N Blood group Antigens

Lisowska

Kordowicz²

1977

Vox Sanguinis

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Antisera obtained by immunizing rabbits with desialized M and N blood group glycoproteins (M' and N' glycoproteins) agglutinate desialized erythrocytes and precipitate desialized glycoproteins, but they do not react with sialic acid containing erythrocytes or glycoproteins. By absorption of anti-M' serum with N' glycoprotein, and of anti-N' serum with M' glycoprotein, reagents specifically agglutinating M' or N' erythrocytes were obtained. The absorbed anti-M' and anti-N' sera were specifically inhibited by M' or N' glycoproteins, respectively. The results show that sialic acid residues of red cell glycoproteins are not essential for the differentiation of M and N blood group determinants.

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The Degradation of M and N Blood Group Glycoproteins and Glycopeptides with Alkaline Borohydride

Cited by 55 publications

References 19 publications

Molecular Basis of Tn-Polyagglutinability

Molecular Basis of Tn-Polyagglutinability

Modification of Amino Groups of Human‐Erythrocyte Glycoproteins and the New Concept on the Structural Basis of M and N Blood‐Group Specificity

Specific Antibodies for Desialized M and N Blood group Antigens

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