Glycopeptides of human teratoma stem cells

Rasilo, Maija‐Liisa; Wartiovaara, Jorma; Renkonen, Ossi

doi:10.1351/pac198052010055

Cited by 6 publications

(1 citation statement)

References 12 publications

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“…The presence of monosaccharide constituents like mannose, galactose, sialic acid [lo] and fucose [7,10] in the PA 1 cell glycopeptides of large size suggested that additional components resembling the keratan sulfates [32] may accompany the glycosaminoglycuronans. In order to see whether keratansulfate-like molecules are really present we treated the fraction of the large-sized saccharides and glycopeptides with endo-j-galactosidase from Escherichia ,freundii and analyzed the digests by gel filtration.…”

Section: Action Of Endo-p-galactosidase On the Fraction Of The Large-mentioning

confidence: 99%

Cell‐Associated Glycosaiminoglycans of Human Teratocarcinoma‐Derived Cells of Line PA 1

Rasilo¹,

Renkonen²

1982

European Journal of Biochemistry

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Human teratocarcinoma-derived cells of line PA 1, which are capable of differentiating in vitrn [Zeuthen, J. et al. (1980) Int. J. Cancer,25,[19][20][21][22][23][24][25][26][27][28][29][30][31][32], incorporate label from radioactive sulfate and/or glucosamine into several large-sized glycosaminoglycans including hyaluronate, chondroitin sulfate/dermatan sulfate co-polymers, heparan sulfate and keratan-sulfate-like molecules. All these polysaccharide fractions were identified by specific degradation methods. The labeled hyaluronate was degraded into a mixture of unsaturated octa-, hexa-and tetrasaccharides by a treatment with Strrptomyces hyaluronidase (EC 4.2.2.1). The chondroitin sulfate/dermatan sulfate co-polymers were cleaved with chondroitin AC lyase (EC 4.2.2.5) into unsaturated disaccharides and a series of unsaturated oligosaccharides; the latter were degraded by a treatment with chondroitin ABC lyase (EC 4 Teratocarcinoina cell cultures are being used as models of the embryonic cell surface. Striking similarities between the two have been revealed by several approaches involving the use of immunological methods as well as biochemical analysis (for a recent review, see [I]). The wrface glycoconjugates of murine teratocarcinoma cells have been studied in this connection by a number of groups. Cantor et al. [2] found the presence of chondroitin sulfate andl heparan sulfate in PCC4 azal cells. Prehm [3] detected hyaluronate in F9 cells stimulated by retinoic acid. Muramatsu et al. [4,5] described large-sized fucosyl glycopeptides that were obtained after exhaustive pronase digestion from several lines of undifferentiated teratocarcinoma cells, and also from early mouse embryos. These glycopeptides were absent or present in much smaller amounts in the proteins of differentiated teratocarcinoma cells. Evidence is also presented suggesting that the large glycopeptide fraction containing the mannose, fucose, sialic acid and distal galactose units is reminiscent of keratan sulfate. MATERIALS A N D METHODS EnzymesStreptomycrs hyaluronidase was purchased from Calbiochem, La Jolla, CA. Chondroitin ABC lyase and chondroitin AC lyase were from Seikagaku Kogyo, Tokyo; the latter had to be used in unusually large nominal concentrations. Endo-

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Section: Action Of Endo-p-galactosidase On the Fraction Of The Large-mentioning

confidence: 99%

Cell‐Associated Glycosaiminoglycans of Human Teratocarcinoma‐Derived Cells of Line PA 1

Rasilo¹,

Renkonen²

1982

European Journal of Biochemistry

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Embryoglycan: a highly branched poly-N-acetyllactosamine in pluripotent stem cells and early embryonic cells

Muramatsu

2016

Glycoconj J

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Embryonal carcinoma cells, stem cells of teratocarcinomas, are pluripotent stem cells and also prototypes of embryonic stem cells. Embryonal carcinoma cells contain large amounts of a highly branched poly-N-acetyllactosamine called embryoglycan, which has a molecular weight of approximately 10,000 or greater, and is asparagine-linked. This glycan was found by analyses of fucose-labeled glycopeptides, and its characteristics were established by biochemical analyses. The content of embryoglycan progressively decreases during the in vitro differentiation of embryonal carcinoma cells. Embryoglycan is also abundant in mouse embryonic stem cells and preimplantation mouse embryos, and decreases during embryogenesis. Embryoglycan carries a number of carbohydrate markers of murine pluripotent stem cells. Lewis x markers, such as SSEA-1, 4C9 antigen, and binding sites for Lotus tetragonolobus agglutinin are of particular importance. 4C9 antigenicity requires clustering of Lewis x, best accomplished by poly-N-acetyllactosamine branching, whereas SSEA-1 does not. Although in vivo evidence is lacking, these epitopes have been suggested to participate in cell-to-cell and cell-to-substratum adhesion. Other markers on embryoglycan include α-galactosyl antigens such as ECMA-2, and binding sites for Dolichos biflorus agglutinin, the epitope of which is considered to be identical to Sd antigen, namely, GalNAcβ1-4(NeuAcα2-3)Galβ1-4GlcNAc. While embryoglycan is also present in human teratocarcinoma cells, the carbohydrate markers characterized in human pluripotent stem cells to date are largely carried by glycolipids and keratan sulfate. Information on embryoglycan and markers carried by it may assist in the development of new markers of human pluripotent stem cells and their progenies.

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The Centrally Acting β1,6N-Acetylglucosaminyltransferase (GlcNAc to Gal)

Mattila¹,

Salminen²,

Hirvas³

et al. 1998

Journal of Biological Chemistry

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In the present experiments the cDNA coding for a truncated form of the ␤1,6N-acetylglucosaminyltransferase responsible for the conversion of linear to branched polylactosamines in human PA1 cells was expressed in Sf9 insect cells. The catalytic ectodomain of the enzyme was fused to glutathione S-transferase, allowing effective one-step purification of the glycosylated 67-74-kDa fusion protein. Typically a yield of 750 g of the purified protein/liter of suspension culture was obtained. The purified recombinant protein catalyzed the transfer of GlcNAc from UDP-GlcNAc to the linear tetrasaccharide Gal␤1-4GlcNAc␤1-3Gal␤1-4-GlcNAc, converting the acceptor to the branched pentasaccharide Gal␤1-4GlcNAc␤1-3(GlcNAc␤1-6)Gal␤1-4-GlcNAc as shown by matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry, degradative experiments, and 1 H NMR spectroscopy of the product. By contrast, the recombinant enzyme did not catalyze any reaction when incubated with UDP-GlcNAc and the trisaccharide GlcNAc␤1-3Gal␤1-4GlcNAc. Accordingly, we call the recombinant ␤1,6-GlcNAc transferase cIGnT6 to emphasize its action at central rather than peridistal galactose residues of linear polylactosamines in the biosynthesis of blood group I antigens. Taken together this in vitro expression of I-branching enzyme, in combination with the previously cloned enzymes, ␤1,4galactosyltransferase and ␤1,3N-acetylglucosaminyltransferase, should allow the general synthesis of polylactosamines based totally on the use of recombinant enzymes.

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Glycopeptides of human teratoma stem cells

Abstract: -Glycopeptides of human teratoma cells were studied. Two glycopeptide fractions (Fractions

Cited by 6 publications

References 12 publications

Cell‐Associated Glycosaiminoglycans of Human Teratocarcinoma‐Derived Cells of Line PA 1

Cell‐Associated Glycosaiminoglycans of Human Teratocarcinoma‐Derived Cells of Line PA 1

Embryoglycan: a highly branched poly-N-acetyllactosamine in pluripotent stem cells and early embryonic cells

The Centrally Acting β1,6N-Acetylglucosaminyltransferase (GlcNAc to Gal)

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