METT-1: A karyotypically normal in vitro line of developmentally totipotent mouse teratocarcinoma cells

1981 ◽  
Vol 7 (4) ◽  
pp. 489-505 ◽  
Author(s):  
Beatrice Mintz ◽  
Claire Cronmiller
Keyword(s):  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma

In Vitro Cytotoxicity of 24 Chemicals to Mouse Teratocarcinoma Cells

1989 ◽  
Vol 17 (1) ◽  
pp. 34-37
Author(s):  
Karen Atkinson ◽  
Lesley Hulme ◽  
Richard H. Clothier ◽  
Michael Balls
Keyword(s):  
In Vitro Cytotoxicity ◽  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma

A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites

1992 ◽  
Vol 103 (1) ◽  
pp. 131-143 ◽  
Author(s):  
N. Sato ◽  
N. Funayama ◽  
A. Nagafuchi ◽  
S. Yonemura ◽  
S. Tsukita ◽  
...  
Keyword(s):  
Gene Family ◽  
Plasma Membranes ◽  
Immunofluorescence Microscopy ◽  
Membrane Association ◽  
Protein Sequence Analysis ◽  
Teratocarcinoma Cells ◽  
Specific Localization ◽  
End Capping ◽  
Mouse Teratocarcinoma

Radixin is a barbed end-capping actin-modulating protein which was previously reported to be concentrated at cell-to-cell adherens junctions (AJ) and cleavage furrows. Recently, cDNA encoding mouse radixin was isolated, showing that radixin is highly homologous to but distinct from ezrin. From mouse teratocarcinoma cells we isolated and analyzed cDNA encoding another radixin-related protein. Sequence analysis has demonstrated that this protein is a mouse homologue of human moesin (98.3% identity) and that it shares 71.7% and 80.1% identity with ezrin and radixin, respectively. Translation experiments in vitro combined with immunoblot analyses led us to conclude that there is a gene family consisting of ezrin, radixin and moesin. These members are coexpressed in various types of cells. Then, by immunofluorescence microscopy, we closely analyzed their distribution using polyclonal and monoclonal antibodies, which could recognize all three members. In addition to cell-to-cell AJ and cleavage furrows, it was shown that they were concentrated at microvilli and ruffling membranes in various types of cells. Furthermore, the cell-to-substrate AJ (focal contacts) were clearly stained by anti-radixin pAb only after the apical/lateral membranes and cytoplasm were removed by the zinc method. We conclude that at least one of the members of the ezrin-radixin-moesin family is concentrated at specific regions where actin filaments are densely associated with plasma membranes.

In vitro Differentiation of Mouse Teratocarcinoma Cells Monitored by Intermediate Filament Expression

1982 ◽  
Vol 22 (1-3) ◽  
pp. 90-99 ◽  
Author(s):  
DENISE PAULIN ◽  
HEDWIG JAKOB ◽  
FRANÇOIS JACOB ◽  
KLAUS WEBER ◽  
MARY OSBORN
Keyword(s):  
Intermediate Filament ◽  
In Vitro Differentiation ◽  
Teratocarcinoma Cells ◽  
Mouse Teratocarcinoma

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.

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