Immunochemical and chemical investigations of the structure of glycoprotein fragments obtained from epiglycanin, a glycoprotein at the surface of the TA3-Ha cancer cell

Codington, John F.; Linsley, Keyes B.; Jeanloz, Roger W.; Irimura, Tatsuro; Osawa, Toshiaki

doi:10.1016/s0008-6215(00)82679-8

Cited by 76 publications

(29 citation statements)

References 20 publications

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“…The occurrence of building units derived from 2-acetamido-2-deoxy-a-D-galactopyranose, which are 0-linked to either serine or threonine, in a wide variety of glycoproteins (1, 2) including glycophorin A (3), epiglycanin (4), antifreeze glycoproteins ( 9 , and the human blood specific glycoproteins (6) is well documented. Both a-and P-glycosidic units derived from N-acetyl-D-galactosamine occur in the oligosaccharidic antigenic determinants of a number of glycosphingolipids (7).…”

Section: Introductionmentioning

confidence: 99%

The azidonitration of tri-O-acetyl-D-galactal

Lemieux¹,

Ratcliffe²

1979

Can. J. Chem.

654

237

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. Can. J. Chem. 57,1244Chem. 57, (1979. Reaction of 3,4,6-tri-0-acetyl-D-galactal with excess ceric ammonium nitrate and sodium azide in acetonitrile produced 2-azido-1-nitrate addition products (53% p-galacto, 22% a-galacto, and 8% a-talo) and N-acetyl-3,4,6-tri-0-acetyl-2-azido-2-deoxy-a-~-galactopyranosylamine was formed, on hydrolysis, in 10% yield. The reaction product provides a convenient source of D-galactosamine and 3,4,6-tri-0-acetyI-2-azido-2-deoxy-a-~-galactopyranosy~ halides. The crystalline j3-chloride is also reported. The use of these glycosyl halides as reactants for the preparation of 2-azido-2-deoxy-a-and -13-D-galactopyranosides under conditions promoted by both mercuric cyanide and silver salts are reported. R. U. LEMIEUX et R. M. RATCLIFFE. Can. J. Chem. 57,1244(1979.La rkaction du tri-0-acktyl-3,4,6 D-galactal avec du nitrate d'ammonium drique en excks et de l'azoture de sodium dans l'adtonitrile conduit aux produits d'addition azido-2 nitrate-1 (53% p-galacto, 22% a-galacto et 8% a-talo); par hydrolyse, il y a formation de la N-acktyltri-0-acktyl-3,4,6 azido-2 dksoxy-2 a-D galactopyrannosylamine avec un rendement de 10%. Le produit de la rkaction s'avkre une source convenable de la D-galactosamine et des halogknures du tri-0-acktyl-3,4,6 azido-2 dksoxy-2 a-D-galactopyrannosyle. On rapporte aussi la formation du chlorure j3 cristallin. On rapporte I'utilisation de ces halogknures de glycosyle cornrne reactifs dans la prkparation des azido-2 dksoxy-2 a-et j3-D-galactopyrannosides dans des conditions favorisks par des sels de cyanure mercurique et d'argent.[Traduit par le journal] Introduction The occurrence of building units derived from 2-acetamido-2-deoxy-a-D-galactopyranose, which are 0-linked to either serine or threonine, in a wide variety of glycoproteins (1, 2) including glycophorin A (3), epiglycanin (4), antifreeze glycoproteins ( 9 , and the human blood specific glycoproteins (6) is well documented. Both a-and P-glycosidic units derived from N-acetyl-D-galactosamine occur in the oligosaccharidic antigenic determinants of a number of glycosphingolipids (7). Thus, there has developed widespread interest in achieving chemical syntheses of oligosaccharides containing these groupings both for immunochemical and enzymological studies (8). However, the lack of a readily accessible supply of either D-galactosamine or of suitable progenitors has curtailed research in this biologically important area. This work was initiated primarily to achieve the syntheses of oligosaccharides related to the A blood determinants (9) but has been extended to the synthesis of the T, T, (lo), and other important human cell-surface antigenic determinants.The major source of D-galactosamine is by way of the acid hydrolysis of chondroitin sulfate (11).

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Section: Introductionmentioning

confidence: 99%

The azidonitration of tri-O-acetyl-D-galactal

Lemieux¹,

Ratcliffe²

1979

Can. J. Chem.

654

237

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“…The TA3-Ha cell is able to transgress both strain and species histocompatibility barriers (3,5). By comparison, the strain-specific ascites cell, TA3-St, from the same mammary tumor was not found to have a morphologically distinct surface coat.…”

Section: Discussionmentioning

confidence: 95%

“…1 and 2) are even more striking when cells are examined by scanning electron microscopy (Figs. [4][5][6]. The strain-specific TA3-St cells have numerous filopodia which are bent, branched, and highly irregular (Fig.…”

Section: Cell Surface Morphologymentioning

confidence: 99%

Ultrastructural and histochemical differences in cell surface properties of strain-specific and nonstrain-specific TA3 adenocarcinoma cells.

Miller

Hay

Codington

1977

The Journal of Cell Biology

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Transmission and scanning electron microscopy and histochemical and biochemical methods were used to investigate differences in cell structure and cell surface properties between the strain-specific TA3-St and nonstrain-specific TA3-Ha ascites sublines of the TA3 murine mammary adenocarcinoma. The TA3-St subline is lethal only to the syngeneic strain A mouse (the strain of origin), whereas the TA3-Ha subline is lethal even to foreign species. In contrast to the TA3-St cell surface, which has numerous folds and irregular microprojections, the TA3-Ha cell has abundant long microvilli of uniform dimensions. An extensive cell surface coat which resembles the "fuzz" coat found on microviUi of normal epithelium was present on the TA3-Ha, but not on the TA3-St cells. After routine fixation, the surface coat of the TA3-Ha cell usually appeared as a filamentous network extending 30-50 nm from the plasmalemma; occasionally, longer filamentous or rod-like structures were found extending 200-400 nm from the plasmalemma. The cell coat material was more extensive on the microvilli than on the intermicrovillous membranes. Free virus-like particles associated with TA3-Ha cells have a similar-appearing surface coat on their outer membranes. The density of surface anionic sites, determined with polycationic ferritin, was greater on the TA3-Ha than on the TA3-St cell surface, consistent with the presence at the TA3-Ha cell surface of several-fold more neuraminidase-susceptible sialic acid groups. The observed surface features of the nonstrain-specific TA3-Ha cell, in comparison to the strain-specific TA3-St cell, are consistent with the suggestion that sialic acid-rich glycoproteins at the TA3-Ha cell surface mask histocompatibility antigens and enhance the ability of malignant cells to invade foreign species.Transformed cells demonstrate a variety of physiological and morphological changes which have been implicated in the altered behavior and malignant growth of these cells (12,18). However, these cells generally behave like normal cells with regard to transplantation rejection by incompati-

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“…The galactopyranosyl-like group may, for example, be attached directly to a protein. This explanation has more credibility in light of the well known a-glycosidic linkages between N-acetyl-galactosamine and hydroxyl groups of serine and threonine in many glycoproteins (Thomas and Winzler, 1969;Bahl et al, 1972;Baenziger and Kornfeld, 1974;Kieras, 1974;Spiro and Bhoyroo, 1974;Codington et al, 1975;Shier, 1975;Newman et al, 1976).…”

Section: Displayed Inmentioning

confidence: 95%

“…Glycolipids have also been shown to contain galactose within membranes (Cuatrecases, 197J). More importantly, galactose has been shown to be the terminal residue of oligosaccharide chains among many different cell types through chemical analysis, including TAJ-Ha murine mammary carcinoma ascites cells (Codington et al, 1975), calf thymocytes (Kornfeld, 1978), and as determinants for type A antigens on human erythrocytes . Terminal galactose identification has been accomplished through lectin studies.…”

Section: L\)mentioning

confidence: 99%