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Nucleotide sequence of the C-terminal region of the mouse epidermal growth factor receptor and expression in teratoma-derived cell lines with increased tumorigenic properties (1993)

Eisinger, Dominic P. ; Serrero, Ginette

Springer

Cytotechnology 13 (1993), S. 21-27

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ISSN: 1573-0778

Keywords: EGF receptor ; EGF receptor mRNA expression ; teratoma ; tumorigenicity ; EGF receptor nucleotide sequence ; EGF

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology

Notes: Abstract The isolation of a cDNA corresponding to a portion (amino acid 943 to 1073) of the cytoplasmic domain of the mouse EGF receptor surrounding the auto phosphorylation sites was obtained by using the reverse transcriptase polymerase chain reaction (RT-PCR) approach. Deduced amino acid sequence of mouse EGF receptor (EGFr) shows a 92% and 76% homology to corresponding regions in the human and the chicken EGFr, respectively. This cDNA was used to develop a sensitive RNase protection assay to investigate EGF receptor mRNA expression in mouse C3H teratoma derived cell lines with increased tumorigenic properties which display a progressive decrease of EGF binding and response. The results show that increased tumorigenicity was not accompanied by a change in EGF receptor mRNA expression. Moreover, they indicate that the RNase protection assay developed using the probe described here is a sensitive approach to investigate EGF receptor expression in murine cells.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00749972

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Effects of a serum spreading factor on growth and morphology of cells in serum-free medium (1980)

Barnes, David ; Wolfe, Richard ; Serrero, Ginette ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Supramolecular Structure 14 (1980), S. 47-63

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ISSN: 0091-7419

Keywords: serum spreading factor ; cell proliferation ; cell morphology ; cell substratum ; serum-free medium ; Life Sciences ; Molecular Cell Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: A heat-sensitive, trypsin-sensitive factor that promoted growth and spreading of cells in serum-free, hormone-supplemented medium was partially purified from human serum. The major portion of the proteins in these preparations migrated upon SDS-polyacrylamide gel electrophoresis with a mobility consistent with molecular weights between 60,000 and 90,000. The spreading activity, which we have termed serum spreading factor, stimulated growth and spreading of a wide variety of cell types. The serum spreading factor was similar to fibronectin in that it showed an affinity for the plastic cell culture substrate but was shown to be distinct from fibronectin by several criteria. This factor may prove useful in studies of cell attachment and spreading and in studies of the relationship of cell shape and cell proliferation.

Additional Material: 9 Ill.