The effect of fetal calf serum on growth arrest caused by activators of protein kinase C

T. D. Bradshaw, A. Gescher, George Pettit

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The growth of human-derived A549 lung carcinoma cells is inhibited by activators of protein kinase C (PKC) such as 12-O-tetradecanoylphorbol- 13-acetate (TPA). In this study, the effect of serum deprivation on TPA-induced growth retardation has been investigated. Cells cultured with 10% FCS and TPA (10-8M) stopped growing for 6 days, whereas inhibition of DNA synthesis caused by TPA in cells which were grown in medium containing the serum substitute ultraser lasted for less than 48 hr. The ability of cells to respond to the growth-inhibitory potential of TPA decreased with decreasing amounts of FCS in the cellular medium. Addition of fetuin or epidermal growth factor (EGF) to incubates with serum-deprived cells increased the ability of TPA to affect growth, but addition of platelet-derived growth factor (PDGF), transforming growth factor beta (TGF-β) or retinoic acid (RA) was without effect. Growth arrest caused by byostatin I, another PKC activator, was equally transitory in serum-supplemented and serum-deprived cells. Cytosol of serum-deprived cells contained only 32% of specific phorbol ester binding sites compared to cells grown with FCS; PKC enzyme activity and immunodetectable protein were similarly reduced in cells grown without FCS. There was no difference in rate of TPA-induced down-regulation of PKC activity and cytosolic phorbol ester receptor sites between cells grown with or without serum.

Original languageEnglish (US)
Pages (from-to)929-932
Number of pages4
JournalInternational Journal of Cancer
Volume47
Issue number6
StatePublished - 1991
Externally publishedYes

Fingerprint

Protein Kinase C
Tetradecanoylphorbol Acetate
Growth
Serum
Fetuins
Platelet-Derived Growth Factor
Phorbol Esters
Tretinoin
Epidermal Growth Factor
Transforming Growth Factor beta
Cytosol
Cultured Cells
Down-Regulation
Binding Sites
Carcinoma
Lung
DNA
Enzymes

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

Cite this

The effect of fetal calf serum on growth arrest caused by activators of protein kinase C. / Bradshaw, T. D.; Gescher, A.; Pettit, George.

In: International Journal of Cancer, Vol. 47, No. 6, 1991, p. 929-932.

Research output: Contribution to journalArticle

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abstract = "The growth of human-derived A549 lung carcinoma cells is inhibited by activators of protein kinase C (PKC) such as 12-O-tetradecanoylphorbol- 13-acetate (TPA). In this study, the effect of serum deprivation on TPA-induced growth retardation has been investigated. Cells cultured with 10{\%} FCS and TPA (10-8M) stopped growing for 6 days, whereas inhibition of DNA synthesis caused by TPA in cells which were grown in medium containing the serum substitute ultraser lasted for less than 48 hr. The ability of cells to respond to the growth-inhibitory potential of TPA decreased with decreasing amounts of FCS in the cellular medium. Addition of fetuin or epidermal growth factor (EGF) to incubates with serum-deprived cells increased the ability of TPA to affect growth, but addition of platelet-derived growth factor (PDGF), transforming growth factor beta (TGF-β) or retinoic acid (RA) was without effect. Growth arrest caused by byostatin I, another PKC activator, was equally transitory in serum-supplemented and serum-deprived cells. Cytosol of serum-deprived cells contained only 32{\%} of specific phorbol ester binding sites compared to cells grown with FCS; PKC enzyme activity and immunodetectable protein were similarly reduced in cells grown without FCS. There was no difference in rate of TPA-induced down-regulation of PKC activity and cytosolic phorbol ester receptor sites between cells grown with or without serum.",
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