scholarly journals Differences between the carbohydrate units of cell-surface glycoproteins of moust B- and T-lymphocytes

1979 ◽  
Vol 181 (2) ◽  
pp. 451-456 ◽  
Author(s):  
T Krusius ◽  
J Finne ◽  
L C Andersson ◽  
C G Gahmberg
Keyword(s):  
T Lymphocytes ◽  
Cell Surface ◽  
Affinity Chromatography ◽  
Concanavalin A ◽  
Cell Types ◽  
Galactose Oxidase ◽  
Neuraminidase Treatment ◽  
Cell Surface Glycoproteins ◽  
B And T Lymphocytes ◽  
Surface Glycoproteins

Carbohydrate units of cell-surface glycoproteins of mouse B- and T-lymphocytes, labelled in their sialic acid residues by the periodate/NaB3H4 method and in their galactose residues by the galactose oxidase/NaB3H4 method after neuraminidase treatment, have been studied. Glycopeptides were prepared from the labelled cells by Pronase digestion and fractionated by concanavalin A affinity chromatography into two fractions (A and B). Alkali-labile oligosaccharides were isolated after mild NaOH/NaBH4 treatment by gel filtration. The alkali-labile oligosaccharides were further analysed by t.l.c. To study the relative proportion of neutral mannose-rich carbohydrate units (fraction C) in lymphocyte glycoproteins, glycopeptides were also prepared from unlabelled cells and subjected to concanavalin A affinity chromatography after N-[3H]acetylation of their peptide moiety. The major alkali-labile oligosaccharide component of both cell types was identified as galactosyl-(beta 1 leads to 3)-N-acetylgalactosaminitol. T-Lymphocytes were characterized by a high proportion of this oligosaccharide and a lower proportion of alkali-stable fraction A glycopeptides, whereas the opposite was observed for B-lymphocytes. The relative proportions of the concanavalin A-binding fractions B and C were similar in both cell types. The differences observed may correlate with the different surface properties of B- and T-lymphocytes.

scholarly journals Migrating endothelial cells are distinctly hyperglycosylated and express specific migration-associated cell surface glycoproteins.

1992 ◽  
Vol 119 (2) ◽  
pp. 483-491 ◽  
Author(s):  
H G Augustin-Voss ◽  
B U Pauli
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Cell Surface ◽  
Surface Glycoprotein ◽  
Endothelial Cell Migration ◽  
Con A ◽  
Neuraminidase Treatment ◽  
Cell Surface Glycoprotein ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

Migration of endothelial cells is one of the first cellular responses in the cascade of events that leads to re-endothelialization of an injured vessel and neovascularization of growing tissues and tumors. To examine the hypothesis that endothelial cells express a specific migration-associated phenotype, we analyzed the cell surface glycoprotein expression of migrating bovine aortic endothelial cell (BAECs). Light microscopic analysis revealed an upregulation of binding sites for the lectins Concanavalin A (Con A), wheat germ agglutinin (WGA), and peanut agglutinin after neuraminidase treatment (N-PNA) on migrating endothelial cells relative to contact-inhibited cells. These findings were confirmed and quantitated with an enzyme-linked lectin assay (ELLA) of circularly scraped BAEC monolayers. The expression of migration-associated cell surface glycoproteins was also analyzed by SDS-PAGE. The overall expression of cell surface glycoproteins was upregulated on migrating BAECs. Migrating BAECs expressed Con A- and WGA-binding glycoproteins with apparent molecular masses of 25 and 48 kD that were not expressed by contact-inhibited BAEC monolayers and, accordingly, disappeared as circularly scraped monolayers reached confluence. Subconfluent BAEC monolayers expressed the same cell surface glycoconjugate pattern as migrating endothelial cells. FACS analysis of circularly scraped BAEC monolayers showed that the phenotypic changes of cell surface glycoprotein expression after release from growth arrest occurred before the recruitment of the cells into the cell cycle (3 vs. 12 h). Suramin, which inhibits endothelial cell migration, abrogated the expression of the migration-associated phenotype and induced the expression of a prominent 28-kD Con A- and WGA-binding cell surface glycoprotein. These results indicate that endothelial cells express a specific migration-associated phenotype, which is characterized by the upregulation of distinct cellular glycoconjugates and the expression of specific migration-associated cell surface glycoproteins.

Cell surface glycoproteins change during gastrulation in Pleurodeles waltlii

1986 ◽  
Vol 82 (1) ◽  
pp. 23-40
Author(s):  
J.F. Riou ◽  
T. Darribere ◽  
J.C. Boucaut
Keyword(s):  
Cell Surface ◽  
Gel Electrophoresis ◽  
Lectin Binding ◽  
Galactose Oxidase ◽  
Two Dimensional ◽  
Isolated Cells ◽  
Two Dimensional Gel Electrophoresis ◽  
Sodium Metaperiodate ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

Identification of the cell surface glycoproteins is an essential requirement for elucidating the mechanisms that mediate intercellular adhesion and cell migration in gastrulating amphibian embryos. In our experiments the glycoproteins present at the surface of isolated cells at blastula and gastrula stages were labelled with 3H-labelled sodium borohydride. The procedure included the oxidation of either galactosyl and, or, N-acetylgalactosaminyl residues with galactose oxidase or sialic acid with sodium metaperiodate. The tritiated components were analysed by two-dimensional gel electrophoresis. On the surface of isolated embryonic cells, 23 glycoproteins have been identified. The most important observation was the labelling of 15 new glycoproteins during gastrulation. At the late blastula stage, eight glycoproteins containing galactosyl or N-acetyl-galactosaminyl residues are labelled, while 23 are labelled at the late gastrula stage. In other experiments, glycoproteins labelled by [3H]fucose or [3H]mannose or precipitated by concanavalin A(ConA)-, or wheat-germ agglutinin (WGA)-Sepharose were studied by two-dimensional gel electrophoresis in order to provide supplementary data on the synthesis and lectin-binding properties of major cell surface glycoproteins. It appears that approximately 100 different glycoproteins are revealed by these methods. Among them, 13 have been identified as major cell surface glycoproteins, 12 being labelled by [3H]mannose, four by [3H]fucose, 10 bearing an affinity for ConA and five for WGA. These 13 glycoproteins are synthesized throughout gastrulation without qualitative variation.

scholarly journals cell surface glycoproteins of murine cytotoxic T lymphocytes. I. T 145, a new cell surface glycoprotein selectively expressed on Ly 1-2(+) cytotoxic T lymphocytes

1978 ◽  
Vol 147 (5) ◽  
pp. 1418-1434 ◽  
Author(s):  
AK Kimura ◽  
H Wigzell
Keyword(s):  
T Cells ◽  
T Cell ◽  
T Lymphocytes ◽  
Cell Surface ◽  
Cytotoxic T Lymphocytes ◽  
Surface Glycoprotein ◽  
Cell Surface Glycoprotein ◽  
Cell Surface Glycoproteins ◽  
T Lymphoblasts ◽  
Surface Glycoproteins

T lymphocytes at various stages of maturation and differentiation have been isolated by cellular fractionation procedures and characterized by cell surface markers and functional assays, The cell surface glycoproteins of the various T-cell preparations have been selectively radiolabeled by the galactose oxidase-tritiated sodium borohydride technique and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Details are presented on the appearance of a new cell surface glycoprotein (T 145), present on immunocompetent T lymphocytes after activation by either major histocompatibility complex alloantigens or by concanavalin A. The intensity of T 145 expression on T lymphoblasts is shown to be directly correlated in time and extent to the levels of cytotoxicity generated in a variety of T-cell activations. Specific enrichment procedures of purified populations of mixed leukocyte culture blasts have shown Ly 1(+)2(-) blasts to be T 145(-) and Ly 1(-)2(+) blasts to be strongly T 145(+). Similar enrichment procedures on normal peripheral T cells have failed to reveal any significant expression of T 145 on a highly enriched population of Ly 1(-)2(+) T cells, Further studies on the stability of T 145 expression after induction have shown it to be a more permanent-type differentiation structure whose expression is clearly not linked to the blast stage of activation. T 145 would thus appear to represent a membrane glycoprotein whose exclusive expression on T lymphoblasts is further restricted to a defined group of cells endowed with cytolytic activity and bearing the Ly phenotype Ly 1(-)2(+).

Characterization of a human granulocyte differentiation antigen (CDw15) commonly recognized by monoclonal antibodies

1985 ◽  
Vol 5 (10-11) ◽  
pp. 933-941 ◽  
Author(s):  
Noirin C. McCarthy ◽  
Merete T. Albrechtsen ◽  
M. A. Kerr
Keyword(s):  
Monoclonal Antibodies ◽  
Cell Surface ◽  
Cell Types ◽  
Carbohydrate Antigen ◽  
Differentiation Antigen ◽  
Molecular Weights ◽  
Wide Range ◽  
Cell Surface Glycoproteins ◽  
Surface Glycoproteins

Many different anti-human granulocyte monoclonal antibodies recognize the same carbohydrate antigen which contains the trisaccharide 3-fucosyl-N-acetyllactosamine. The antigen is expressed mainly on two cell surface glycoproteins of molecular weights around 105 K and 160K which are apparently not members of the LFA-1 family of proteins. Although specific for granulocytes in blood, the antigen is expressed on a wide range of non-haemopoietic cell types.

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