Rat liver epithelial cell cultures in a serum-free medium: Primary cultures and derived cell lines expressing differentiated functions

In Vitro ◽  
1984 ◽  
Vol 20 (10) ◽  
pp. 780-795 ◽  
Author(s):  
Martine Chessebeuf ◽  
Prudent Padieu
Keyword(s):  
Epithelial Cell ◽  
Cell Lines ◽  
Rat Liver ◽  
Cell Cultures ◽  
Primary Cultures ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Epithelial Cell Cultures

Effects of vitamin A on growth and differentiation of human tracheobronchial epithelial cell cultures in serum-free medium

1989 ◽  
Vol 93 (1) ◽  
pp. 133-142
Author(s):  
D.P. Chopra ◽  
M.M. Klinger ◽  
J.K. Sullivan
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Vitamin A ◽  
Cell Cultures ◽  
Cell Multiplication ◽  
Serum Free Medium ◽  
Free Medium ◽  
Plasma Membrane Vesicles ◽  
Serum Free ◽  
Epithelial Cell Cultures

Differentiating epithelial cell cultures from human tracheobronchial epithelium have been propagated in serum-free medium. The major objective of this study was to examine the trophic effects of vitamin A on cell multiplication and morphology of the tracheal cell cultures. The cellular responses were analyzed in terms of growth kinetics, morphological and ultrastructural alterations and secretion of glycoconjugates. Cell cultures in control medium exhibited characteristics of epithelial cells including microvilli on cell surfaces, desmosomes between cells, and numerous secretory vesicles in the cytoplasm. Vitamin A at 10(−6) M and 10(−7) M inhibited cell replication and enhanced the secretion of [3H]glucosamine-labeled glycoconjugates. Further, vitamin A increased the production of plasma membrane vesicles and acquisition by the cells of a highly secretory ultrastructure. This in vitro model of human epithelial cells will be important in the investigation of various aspects of growth and differentiation.

Human endometrial epithelial cells grown on collagen in serum-free medium. Estrogen responsiveness and morphology

1991 ◽  
Vol 125 (1) ◽  
pp. 101-108 ◽  
Author(s):  
Bertil G. Casslén ◽  
Michael J. K. Harper
Keyword(s):  
Epithelial Cells ◽  
Primary Cultures ◽  
Collagen Matrix ◽  
Human Endometrium ◽  
Serum Free Medium ◽  
Free Medium ◽  
Endometrial Stromal Cells ◽  
Prolonged Incubation ◽  
Serum Free ◽  
Endometrial Epithelial Cells

Abstract. The aim of the study was to explore the possibility of using human endometrial epithelial cells in serum-free culture as a sensitive assay for hormonal effects on the human endometrium. Glands were isolated following enzymatic digestion of the endometrial tissue and plated on a collagen matrix. The epithelial cells were grown in either medium containing serum or in supplemented serum-free medium. No morphologic difference was found between cells grown in these two media for up to 5 days, using either light or scanning electron microscopy. Secretion of prostaglandin F2α (PGF2α) in response to estradiol was not lower in serum-free medium than in medium containing serum for the first 2 days of culture, whereas secretion declined after prolonged incubation in the serum-free medium. This response to estradiol was clearly dose-dependent, and it was further enhanced by addition of arachidonic acid, the precursor for prostaglandin synthesis, to the medium. Co-culture of endometrial stromal cells did not influence the secretion of PGF2α by epithelial cells. We conclude that the secretion of PGF2α from primary cultures of human endometrial epithelial cells grown on collagen in serum-free medium can be used for a limited period as an assay of estrogenic effects on the human endometrium.

Regulation by Dibutyryl Cyclic AMP of Carnosine Synthesis in Astroglia-Rich Primary Cultures Kept in Serum-Free Medium

1989 ◽  
Vol 52 (1) ◽  
pp. 229-234 ◽  
Author(s):  
Michael Schulz ◽  
Bernd Hamprecht ◽  
Horst Kleinkauf ◽  
Karl Bauer
Keyword(s):  
Cyclic Amp ◽  
Primary Cultures ◽  
Serum Free Medium ◽  
Free Medium ◽  
Dibutyryl Cyclic Amp ◽  
Serum Free

scholarly journals Induction of apoptosis by c-Fos protein.

1996 ◽  
Vol 16 (1) ◽  
pp. 211-218 ◽  
Author(s):  
G A Preston ◽  
T T Lyon ◽  
Y Yin ◽  
J E Lang ◽  
G Solomon ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Colorectal Carcinoma ◽  
Cell Lines ◽  
Transcriptional Activation ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Fos Protein ◽  
Induced Apoptosis ◽  
I Cells

The role of c-Fos in apoptosis was examined in two Syrian hamster embryo cell lines (sup+I and sup-II) and a human colorectal carcinoma cell line (RKO), using the chimeric Fos-estrogen receptor fusion protein c-FosER. As previously reported, contrasting responses were observed when these two cell lines were placed under growth factor deprivation conditions; sup+I cells were highly susceptible to apoptosis, whereas sup-II cells were resistant. In this report, we show that the activated c-FosER protein induces apoptosis in sup-II preneoplastic cells in serum-free medium, indicating that c-Fos protein can induce apoptotic cell death in these cells. c-Fos-induced apoptosis was not blocked by the protein synthesis inhibitor cycloheximide, suggesting that the c-Fos transcriptional activation activity is not involved. This conclusion was further supported by the observation that overexpression of v-Fos, which is highly proficient in transcriptional activation but deficient in the transcriptional repression activity associated with c-Fos, did not induce apoptosis. Constitutively expressed Bcl-2 delayed the onset of low-serum-induced apoptosis in sup+I cells and enhanced survival in sup-II cells. Further, coexpression of Bcl-2 and c-FosER in sup+I or sup-II cells protected the cells from c-FosER-induced apoptosis. The possibility that c-FosER-induced apoptosis requires a p53 function was examined. Colorectal carcinoma RKOp53+/+ cells, which do not normally undergo apoptosis in serum-free medium, showed apoptotic DNA fragmentation upon expression and activation of c-FosER. Further, when the wild-type p53 protein was diminished in the RKO cells by infection with the papillomavirus E6 gene, subsequent c-FosER-induced apoptosis was blocked. The data suggest that c-Fos protein plays a causal role in the activation of apoptosis in a p53-dependent manner. This activity does not require new protein synthesis and is blocked by overexpression of Bcl-2 protein.

scholarly journals Biologically Active Fas Antigen and Its Cognate Ligand Are Expressed on Plasma Membrane-Derived Extracellular Vesicles

Blood ◽  
1998 ◽  
Vol 91 (10) ◽  
pp. 3862-3874 ◽  
Author(s):  
Joseph Albanese ◽  
Sarkis Meterissian ◽  
Maria Kontogiannea ◽  
Catherine Dubreuil ◽  
Arthur Hand ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Cell Lines ◽  
Extracellular Vesicles ◽  
Metastatic Potential ◽  
Biologically Active ◽  
Serum Free Medium ◽  
Free Medium ◽  
Fas Antigen ◽  
Serum Free ◽  
Shed Vesicles

Abstract Exfoliation of plasma membrane components is a directed process that consumes energy and requires active cell metabolism. Proteins involved in regulating the survival and proliferation of eukaryotic cells are released on exfoliated vesicles. We examine here whether the Fas receptor and its cognate ligand (FasL) are present on vesicles shed from high metastatic potential CX-1 cells and low metastatic potential MIP-101 cells and from HuT 78 cells, respectively. Rates of exfoliation at 2 hours and cumulative levels of extracellular vesicles in serum-free medium conditioned by CX-1 cells are increased by 1.8-fold and 1.6-fold, respectively, relative to that in medium conditioned by MIP-101 cells. Although vesicles shed from both cancer cell lines contain Fas antigen, the amount of Fas per vesicle and the percentage of vesicles containing Fas are increased for vesicles isolated from MIP-101 cells, relative to those from CX-1 cells, as determined by immunogold particle labeling and electron microscopy and by immunofluorescence microscopy and flow cytometry. Results of metabolic labeling with 35S-methionine indicate that Fas biosynthesis is reduced by up to 3.3-fold for CX-1 cells, relative to that of MIP-101 cells, consistent with the finding of decreased Fas on vesicles shed from the plasma membrane of CX-1 cells. Although mRNA for soluble Fas receptor is detectable in both cell lines, depletion of shed vesicles from serum-free medium by ultracentrifugation removes all detectable biological activity. FasL is detected on vesicles exfoliated from HuT 78 cells by immunoelectron microscopy and Western blot analysis. FasL-bearing vesicles induce apoptosis of Fas-expressing cancer cells at the same level as observed by treatment with monoclonal anti-Fas antibody. Furthermore, Fas-bearing extracellular vesicles from MIP-101 but not from CX-1 cells protect the CX-1 cell line from FasL-induced and anti-Fas–mediated apoptosis, indicating that Fas present on shed vesicles is biologically active. We conclude that the Fas antigen and its cognate ligand are exfoliated from the cell surface in a bioactive configuration. Exfoliation may provide a mechanism for long-range signal-directed apoptosis while maintaining Fas/FasL on a membrane surface.

Autonomous proliferation of mewo human melanoma cell lines in serum-free medium: Secretion of growth-stimulating activities

1986 ◽  
Vol 37 (1) ◽  
pp. 123-132 ◽  
Author(s):  
Sylvie Sauvaigo ◽  
Ruth E. Fretts ◽  
Richard J. Riopelle ◽  
Alain E. Lagarde
Keyword(s):  
Cell Lines ◽  
Melanoma Cell ◽  
Human Melanoma ◽  
Human Melanoma Cell ◽  
Serum Free Medium ◽  
Free Medium ◽  
Serum Free ◽  
Melanoma Cell Lines
Sign in / Sign up

Export Citation Format

Share Document