Growth of preadipocyte cell lines and cell strains from rodents in serum-free hormone-supplemented medium

In Vitro ◽  
1984 ◽  
Vol 20 (2) ◽  
pp. 79-88 ◽  
Author(s):  
D. Gaillard ◽  
R. Négrel ◽  
G. Serrero-Davé ◽  
C. Cermolacce ◽  
G. Ailhaud
Keyword(s):  
Cell Lines ◽  
Serum Free ◽  
Cell Strains

scholarly journals Serum-free growth of normal and transformed fibroblasts in milk: differential requirements for fibronectin.

1981 ◽  
Vol 88 (2) ◽  
pp. 294-300 ◽  
Author(s):  
K S Steimer ◽  
M Klagsbrun
Keyword(s):  
Cell Lines ◽  
Normal Cell ◽  
Transformed Cells ◽  
Temperature Sensitive ◽  
Fibroblastic Cell ◽  
Serum Free ◽  
Transformed Fibroblasts ◽  
Cell Strains ◽  
Free Growth ◽  
Fibroblastic Cells

Bovine milk may be used as a supplement for the serum-free growth of certain fibroblastic cells in culture. The growth properties of three representative cell types in milk-supplemented medium were examined; fibroblastic cell strains, fibroblastic cell lines, and transformed fibroblasts. Transformed fibroblasts, which included RNA and DNA tumor virus-transformed cells and carcinogen-transformed cells, grew in milk. Instead of growing attached to the culture dishes, as they normally do in serum, transformed fibroblasts grew in milk as large clusters in suspension. In contrast, nontransformed fibroblastic cell strains and cell lines did not grow in milk-supplemented medium. Fibroblasts transformed by a temperature-sensitive transformation mutant of Rous sarcoma virus were temperature-sensitive for growth in milk. The failure of cells to adhere to the substratum in milk-supplemented medium suggested that milk might be deficient in attachment factors for fibroblasts. When the attachment of fibroblastic cells in milk-supplemented medium was facilitated by pretreating culture dishes with fibronectin, (a) transformed cells grew attached rather than in suspension, (b) normal cell lines attached and grew to confluence, and (c) normal cell strains adhered and survived but did not exhibit appreciable cell proliferation.

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.

Serum-Free Transfection of CHO Cells with Chemically Defined Transfection Systems to Generate Transient and Stable Cell Lines

2010 ◽  
pp. 475-478
Author(s):  
Reisinger Hannes ◽  
Vorauer-Uhl Karola ◽  
Steinfellner Willibald ◽  
Wagner Andreas ◽  
Katinger Hermann ◽  
...  
Keyword(s):  
Cell Lines ◽  
Cho Cells ◽  
Serum Free ◽  
Stable Cell Lines

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.

Establishment of Recombinant CHO Cell Lines Under Serum-free Conditions

2007 ◽  
pp. 57-61
Author(s):  
Maya Kuchenbecker ◽  
Bernd Rehberger ◽  
Michael Schriek ◽  
Judith Gackowski ◽  
Ralf Fehrenbach
Keyword(s):  
Cell Lines ◽  
Cho Cell ◽  
Serum Free ◽  
Serum Free Conditions
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