Developmental potential of nuclei from mouse teratocarcinoma cells

1989 ◽  
Vol 76 (12) ◽  
pp. 582-584 ◽  
Author(s):  
K. Illmensee ◽  
D. Gerh�user ◽  
B. Lioi ◽  
J. A. Modlinski
Keyword(s):  
Developmental Potential ◽  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma

Pleiotropic phenotypic expression in cybrids derived from mouse teratocarcinoma cells fused with rat myoblast cytoplasts

Cell ◽  
1985 ◽  
Vol 43 (3) ◽  
pp. 777-791 ◽  
Author(s):  
Yoichiro Iwakura ◽  
Masami Nozaki ◽  
Masahide Asano ◽  
Michihiro C. Yoshida ◽  
Yutaka Tsukada ◽  
...  
Keyword(s):  
Phenotypic Expression ◽  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma

Immunofluorescence studies on deoxyribonuclease from mouse teratocarcinoma cells during cell differentiation

Development ◽  
1979 ◽  
Vol 54 (1) ◽  
pp. 37-46
Author(s):  
L. Soriano ◽  
D. Paulin
Keyword(s):  
Cell Differentiation ◽  
Embryonal Carcinoma ◽  
Cell Types ◽  
Carcinoma Cells ◽  
Nuclear Staining ◽  
Fluorescence Staining ◽  
Immunofluorescence Method ◽  
Teratocarcinoma Cells ◽  
Different Cell Types ◽  
Mouse Teratocarcinoma

Specific anti-DNase-I IgG have been used to detect deoxyribonuclease in teratocarcinoma cells by an indirect immunofluorescence method. All the cells studied show fluorescence staining. However, the patterns are quite different in embryonal carcinoma cells (amorphous cytoplasmic fluorescence and absence of nuclear staining) as compared to differentiated cell lines (diffuse, bright granular nuclear and fibrillar cytoplasmic fluorescence). It is possible by this method to distinguish different cell types derived from the same origin. Deoxyribonuclease from teratocarcinoma cells can therefore be considered as a marker of cell differentiation in this system.

Comparative protein patterns in chromatins from mouse teratocarcinoma cells

1976 ◽  
Vol 102 (1) ◽  
pp. 169-178 ◽  
Author(s):  
Denise Paulin ◽  
J.-F. Nicolas ◽  
M. Jacquet ◽  
Hedwig Jakob ◽  
F. Gros ◽  
...  
Keyword(s):  
Protein Patterns ◽  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma

Partial structural analysis of concanavalin A binding glycopeptides of large size from human teratocarcinoma-derived cells: cleavage by hydrazinolysis and alkaline borohydride

1982 ◽  
Vol 60 (7) ◽  
pp. 749-756 ◽  
Author(s):  
Maija-Liisa Rasilo ◽  
Ossi Renkonen
Keyword(s):  
Structural Analysis ◽  
Concanavalin A ◽  
Relative Mass ◽  
Human Origin ◽  
Con A ◽  
Large Size ◽  
Teratocarcinoma Cells ◽  
The Individual ◽  
Mouse Teratocarcinoma

Pronase digests of cultured teratocarcinoma-derived cells (PA 1) of human origin have been previously shown to contain large-sized glycopeptides (relative mass (Mr) > 7400), of which 15–23% are retained by columns of concanavalin A (Con A) – Sepharose and can be eluted with 10 mM methyl α-D-mannopyranoside. The present data show that this fraction (A – Con A II) contains a family of glycopeptides that are degradable with anhydrous hydrazine as well as with 0.05 M NaOH – 1 M NaBH4. The cleavage products representing individual oligosaccharide chains, presumably as oligosaccharides and glycopeptides, consisted mostly of medium- (Mr 1400–6000) and small-sized (Mr < 1400) molecules. This implies that glycopeptides bearing several oligosaccharide chains were present in A – Con A II. Most of the individual oligosaccharide chains were not bound to Con A – Sepharose, but some were retained by the lectin column in the same way as the original glycopeptides. Some of the oligosaccharides were degraded partially with endo-β-galactosidase from Escherichia freundii suggesting the presence of GalβGlcNAcβ repeats. The present findings show that A – Con A II may be different from the "embryonic" glycopeptides of mouse teratocarcinoma cells that are reportedly not cleaved by mild alkaline borohydride treatment. Instead, A – Con A II is reminiscent of the T-1 glycopeptide of glycophorin.

scholarly journals High-molecular-weight glycoproteins are the major carriers of the carbohydrate differentiation antigens I, i and SSEA-1 of mouse teratocarcinoma cells

1983 ◽  
Vol 215 (3) ◽  
pp. 491-503 ◽  
Author(s):  
R A Childs ◽  
J Pennington ◽  
K Uemura ◽  
P Scudder ◽  
P N Goodfellow ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cell Lines ◽  
Galactose Oxidase ◽  
Embryonal Carcinoma Cell ◽  
Teratocarcinoma Cell ◽  
Differentiation Antigens ◽  
Carcinoma Cell Lines ◽  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma

The carriers of the carbohydrate differentiation antigens I, i and SSEA-1 were investigated in embryonal carcinoma cell lines of mouse and differentiated cell lines derived from them. Glycoproteins were studied by immunostaining (‘Western blotting’) of total cell lysates and immunoprecipitation from lysates of galactose oxidase/NaB3H4-labelled cells; glycolipids were investigated by immunostaining of thin layer chromatograms. The antigenic activities detected by immunofluorescence of cell smears were reflected in the antigenicities of high-molecular-weight glycoproteins. These were polydisperse and markedly susceptible to digestion with endo-beta-galactosidase. Only the I antigen was detected on minor glycolipids. These observations indicate that glycoproteins rather than glycolipids are the major carriers of carbohydrate differentiation antigens I, i and SSEA-1 in the teratocarcinoma cell lines.

5-Methylcytosine content of DNA during differentiation in mouse teratocarcinoma cells

1979 ◽  
Vol 124 (1) ◽  
pp. 25-29 ◽  
Author(s):  
Jill D. Fabricant ◽  
Erwin F. Wagner ◽  
Bernhard Auer ◽  
Manfred Schweiger
Keyword(s):  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma
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