Substratum-growth factor collaborations are required for the mitogenic activities of activin and FGF on embryonal carcinoma cells.

Schubert, David; Kimura, Hideo

doi:10.1083/jcb.114.4.841

Cited by 52 publications

(22 citation statements)

References 30 publications

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“…These appeared to be highly transformed cells that were unable to grow on other substrates such as type IV collagen or fibronectin. It is possible that different cell types may respond differentially to substrate molecules and that this would affect their subsequent responses to growth factors, as has been suggested for the response of embryonal carcinoma cells to activin and bFGF (41). These results focus attention on the need for studies of the responses of different types of cells to cytotactin as well as on possible differences between soluble and substratum-bound cytotactin, which have been shown to have opposite effects on neurite outgrowth (38).…”

Section: Discussionmentioning

confidence: 99%

Cytotactin binding: inhibition of stimulated proliferation and intracellular alkalinization in fibroblasts.

Crossin

1991

Proc. Natl. Acad. Sci. U.S.A.

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Cytotactin is an extracellular matrix protein that is dynamically and transiently expressed in a placedependent fashion during development by gial cells, fibroblasts, and several other cell types. In the present study, the effects of cytotactin on cell proliferation were examined in fibroblastic cells in culture. NIH 3T3 mouse cells plated on tissue culture substrata in the presence of soluble cytotactin remained rounded for longer periods than untreated control cells, similar to their response to cytotactin-coated substrates.These rounding effects could be prevented by pretreatment of the cells with nocodazole, a microtubule-disrupting agent. Cytotactin inhibited the proliferation of fibroblasts in culture in a dose-and time-dependent manner, and this inhibition occurred even after nocodazole treatment. In addition, the presence of cytotactin inhibited proliferation stimulated by growth factors or tumor promoter. These effects on cell growth were accompanied by an early inhibition of the intracellular akainization that normally occurs upon mitogenic stimulation by a number of growth-promoting agents. Together these observations suggest that cytotactin is an endogenous cell surface modulatory protein and provide a possible mechanism whereby cytotactin may contribute to pattern formation during development, regeneration, tumorigenesis, and wound healing.

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Section: Discussionmentioning

confidence: 99%

Cytotactin binding: inhibition of stimulated proliferation and intracellular alkalinization in fibroblasts.

Crossin

1991

Proc. Natl. Acad. Sci. U.S.A.

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“…bFGF, EGF, activin (Schubert et al, 1990;Schubert and Kimura, 1991;van den Eijnden-van Raaij et al, 1992), LIF and IL-6 have now each been shown to support the survival of P19 cells. In addition, insulin, a component of commonly used defined medium, appears to be necessary for prolonged cell survival.…”

Section: Identification Of Cntf Receptors On P19 Cellsmentioning

confidence: 96%

“…Laminin was not used because of its contribution to mitogenesis (Schubert and Kimura, 1991 for 10 min at 4"C, air-dried, dipped in radiosensitive emulsion (Kodak NTB2), exposed for autoradiography for 72 h at -7O"C, and developed. The percentage of cells with heavily labelled nuclei was then determined for 500-1500 cells in each of triplicate samples.…”

Section: Ph] Thymidine Labellingmentioning

confidence: 99%

Trophic Actions of Ciliary Neurotrophic Factor on Murine Embryonic Carcinoma Cells

Gupta

Haggarty

Carbonetto

et al. 1993

Eur J of Neuroscience

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Recombinant rat CNTF (ciliary neurotrophic factor) at picomolar concentration prevents the death of P19 murine embryonic carcinoma cells that usually follows upon withdrawal of serum from the culture medium. For prolonged survival of P19 cells in serum-free medium, insulin must also be present. In the presence or absence of serum, CNTF stimulates the differentiation of P19 cells, inducing the formation of neurites and synthesis of neurofilament. The results of radioautographic studies with radioiodinated CNTF indicate the presence of high-affinity binding sites on P19 cells. Equilibration of P19 cells with [125I]CNTF followed by incubation with cross-linking reagents reveals evidence for at least two putative receptors of approximately 78 and approximately 167 kDa.

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“…Indeed, in N2 medium supplemented with 1 mg/ml BSA, P19 cells grew even in the absence of activin A, and no activin activity was observed in the BSA we used (unpublished data). Schubert and Kimura recently reported that when culture dishes were precoated with laminin or fibronectin, P19 cells grew in serum-free N2 medium (25). This suggests that precoating by one of these substances prevents components in the medium necessary for P19 cell growth from binding to culture dishes.…”

Section: Discussionmentioning

confidence: 99%

The Activin A‐Dependent Proliferation of PCC3/A/1 Embryonal Carcinoma Cells in Serum‐Free Medium

Atsumi¹,

Miwa²,

Eto

et al. 1993

Dev Growth Differ

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Examination of the growth requirements of murine embryonal carcinoma cells (EC cells) or embryonic stem cells (ES cells) in serum-free medium revealed that PCC3 EC cells required activin A to grow and/or survive in such medium. In the absence of activin A, PCC3 cells began to disintegrate within 3 days under any serum-free conditions examined. P I 9 and AT805 EC cells grew even in serum-free medium without activin A but their growth rates were slightly facilitated by its addition. F9 EC cells also grew in the medium without activin A and its addition somewhat inhibited their growth rate. Three independently isolated ES cell lines and feeder-dependent PSA-1 EC cells also grew in serum-free medium without activin A if leukemia inhibitory factor (LIF) was supplemented. The addition of activin A had little effect on their growth rates. These findings suggest that PCC3 EC cells are a sort of nutritional mutant requiring activin A, thus making them useful in stidies on the growth regulatory mechanisms of EC/ES cells and/or the action of activin on EC/ ES cells.

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Substratum-growth factor collaborations are required for the mitogenic activities of activin and FGF on embryonal carcinoma cells.

Cited by 52 publications

References 30 publications

Cytotactin binding: inhibition of stimulated proliferation and intracellular alkalinization in fibroblasts.

Cytotactin binding: inhibition of stimulated proliferation and intracellular alkalinization in fibroblasts.

Trophic Actions of Ciliary Neurotrophic Factor on Murine Embryonic Carcinoma Cells

The Activin A‐Dependent Proliferation of PCC3/A/1 Embryonal Carcinoma Cells in Serum‐Free Medium

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