Blood Group A Activities of Glycoprotein and Glycolipid from Human Erythrocyte Membranes

Yamato, Kunio; Handa, Shizuo; Yamakawa, Tamio

doi:10.1093/oxfordjournals.jbchem.a131018

Cited by 13 publications

(7 citation statements)

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“…The erythrocytes of p and pk individuals appear to be structurally and functionally normal despite their abnormal GSL content, possibly because the total GSL content of these cells is approximately equivalent to that of normal erythrocytes (Table 4). Most of the erythrocyte ABH antigens are GSL (27,28), and "Bombay" cells, which lack ABH antigens, also have a normal life span, in contrast to the accelerated destruction of erythrocytes lacking the Rh antigen complex, which is thought to be a lipoprotein (reviewed in ref. 29).…”

Section: Resultsmentioning

confidence: 99%

Abnormalities in the glycosphingolipid content of human Pk and p erythrocytes.

Marcus¹,

Naiki²,

Kundu³

1976

Proc. Natl. Acad. Sci. U.S.A.

118

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A glycosphingolipid (GSL) with blood group P1 activity was isolated recently from erythrocyte stroma (8) and the P and Pk antigens were identified as the GSL globoside and trihexosyl ceramide (Table 2), respectively, on the basis of hemagglutination inhibition studies (9). The identification of trihexosyl ceramide as the pk antigen was surprising, since this antigen is detectable by immunological techniques only in rare phenotypes, but this compound is present in all normal human red cells (10)(11)(12)(13) (16). The acetylated neutral GSLs (fraction 3) were subjected to analytical and preparative thin-layer chromatography (TLC) on precoated silica gel plates (E. Merck Laboratories, Inc.) with the following solvent systems: dichloroethane-methanol 95:5 (vol/vol) first development, and dichloroethane-methanol 105:3 (vol/vol) second development. a-Naphthol and resorcinol (17, 18) reagents were utilized to detect neutral GSLs and gangliosides, respectively. For preparative TLC the plates were pre-washed with chloroformmethanol-water, 50:50:15 (vol/vol), and analytical samples of the erythrocyte GSLs and standard compounds were applied to one edge of the plate. The segment of the plate containing the analytical samples was separated from the plate with a glass cutter and the GSLs were detected with the a-naphthol reagent. Glycolipids were eluted from the silica gel with chloroformmethanol (1:1, vol/vol) and trimethylsilyl derivatives were prepared for gas chromatographic analysis as described previously (8) with the following modification. After extraction of the fatty acid methyl esters with hexane, N-acetylation of hexosamines was performed by the method of Etchison and Holland (19). Unsubstituted fatty acids were separated from hydroxy fatty acids (15) prior to analysis by gas chromatography.Washed packed erythrocytes obtained from 150 ml of blood from a Japanese p donor (20) and from 10 ml of blood from a P2' donor were lysed in a large volume of 3 mM acetic acid, lyophilized, and extracted with chloroform-methanol 2:1 and 1:1 (vol/vol). The dried lipid extract was acetylated and fractionated on Florisil and the acetylated GSLs (fraction 3) were deacetylated. A portion of the GSL was separated into neutral and acid fractions by chromatography on DEAE-Sephadex.

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Section: Resultsmentioning

confidence: 99%

Abnormalities in the glycosphingolipid content of human Pk and p erythrocytes.

Marcus¹,

Naiki²,

Kundu³

1976

Proc. Natl. Acad. Sci. U.S.A.

118

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“…Yamato et al [27] isolated the glycolipid and glycoprotein fractions from a pool of 10 liters of packed human group A eryth rocytes. Determination of the A-antigenic activities by hemagglutination inhibition on these fractions gave a ratio of glycolipids to glycoproteins of about 6:1.…”

Section: Discussionmentioning

confidence: 99%

Blood Group A Antigen in Human Erythrocytic Membranes and Membrane Fractions

Kent¹,

McKibbin²,

Boggio³

et al. 1977

Vox Sanguinis

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Erythrocytic membranes from blood group A individuals were assayed for A antigen using a quantitative hemagglutination inhibition technique. The membranes were then extracted for lipid and glycoprotein. Although some A antigen was usually found in the glycoprotein fraction, most of the activity was in the lipid fraction. The sum of A antigen activity in the lipid, glycoprotein, and membrane residue fractions only occasionally was equal to the A activity in the erythrocytic ghosts. However, when certain lipid preparations with little or no A antigen (enhancement factors) were added to the glycolipid fractions, the amount of A antigen demonstrated was usually greatly increased. Under these conditions, the sum of the fractions often was much greater than the A antigen demonstrated in erythrocytic membranes. This suggests that the organization or arrangement of A antigenic determinants in the red cell membrane may not always permit a stoichiometric reaction with anti-A molecules.

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“…12),13) However, I believe that the major activity is attributable to glycolipids with relatively short carbohydrate chains of 6 to 8. 15) The number of different minor glycolipids will probably increase as further studies proceed, although the total amounts of these molecules are very small compared to the major glycolipid, globoside I. These glycolipids are believed to be located on the surface of the erythrocyte membrane, with the carbohydrate moiety projecting from the cells and this characteristic feature facilitates the importance of these glycolipids in cell-to-cell and cell-to-macromolecule recognition.…”

Section: )6)mentioning

confidence: 99%

Studies on erythrocyte glycolipids

Yamakawa¹

2005

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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Abstract:The discovery and structural identification of glycolipids in erythrocyte membranes by the author's research group are reviewed. Differences among species and individuals were the characteristic features of glycolipids in erythrocytes. Individual differences were subjected to genetic analysis and led the discovery of genes involved in the genetic regulation of glycolipid expression in dogs and mice.

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Blood Group A Activities of Glycoprotein and Glycolipid from Human Erythrocyte Membranes

Cited by 13 publications

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Abnormalities in the glycosphingolipid content of human Pk and p erythrocytes.

Abnormalities in the glycosphingolipid content of human Pk and p erythrocytes.

Blood Group A Antigen in Human Erythrocytic Membranes and Membrane Fractions

Studies on erythrocyte glycolipids

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