Receptors for Epidermal Growth Factor and Steroid Hormones in Human Breast Cancer

Oncology ◽  
1988 ◽  
Vol 45 (6) ◽  
pp. 424-427 ◽  
Author(s):  
Francesco Battaglia ◽  
Giovanni Polizzi ◽  
Giovanni Scambia ◽  
Simonetta Rossi ◽  
Pierluigi Benedetti Panici ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Steroid Hormones ◽  
Human Breast Cancer ◽  
Human Breast ◽  
Epidermal Growth

Steroidal regulation of oestradiol-17β dehydrogenase activity of the human breast cancer cell line MCF-7

1988 ◽  
Vol 118 (1) ◽  
pp. 149-154 ◽  
Author(s):  
E. F. Adams ◽  
N. G. Coldham ◽  
V. H. T. James
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Human Breast Cancer ◽  
Transforming Growth Factor ◽  
Cancer Cell Line ◽  
Human Breast Cancer Cell ◽  
Human Breast ◽  
Epidermal Growth ◽  
Mcf 7

ABSTRACT We have examined the direct effects of progestins, oestrogens, peptide hormones and growth factors on oestradiol-17β dehydrogenase (OE2DH) activity of cultures of the human breast cancer cell line MCF-7. Cells were cultured in the presence of steroid or peptide for 6 days, after which the number of cells was determined and cellular OE2DH activity assessed. Progesterone, 6α-methyl-17α-hydroxyprogesterone acetate, norethisterone and d(−)-norgestrel all profoundly inhibited cell mitosis and stimulated reductive (oestrone→oestradiol-17β) and oxidative (oestradiol-17β→oestrone) OE2DH activity. Both oestrone and oestradiol-17β directly stimulated reductive OE2DH activity, but had no effect on the oxidative direction. Oestradiol-17β stimulated cell growth only in phenolred free culture medium. Ovine prolactin, LH, epidermal growth factor and transforming growth factor did not alter OE2DH activity but small stimulatory effects on the growth of MCF-7 cells were exerted by prolactin and a combination of transforming growth factor with epidermal growth factor. It is concluded that these results may explain, at least in part, the alterations in mitotic activity and tissue oestradiol-17β levels observed in breast tissue during varying physiological and pathological conditions, such as during the menstrual cycle and in breast cancers. J. Endocr. (1988) 118, 149–154

scholarly journals Activation of the Na+/H+ antiport is not required for epidermal growth factor-dependent gene expression, growth inhibition or proliferation in human breast cancer cells

1989 ◽  
Vol 257 (1) ◽  
pp. 151-157 ◽  
Author(s):  
J G Church ◽  
G B Mills ◽  
R N Buick
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cancer Cells ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Cell Types ◽  
Human Breast Cancer Cells ◽  
Human Breast ◽  
Epidermal Growth

Mitogen interaction with specific receptors in many cell types leads to activation of the Na+/H+ antiport and a resultant cytoplasmic alkalinization. Since amiloride inhibits both Na+/H+ exchange and cell proliferation, it has been hypothesized that activation of the antiport is an obligatory requirement for mitogenesis. However, concentrations of amiloride which inhibit the antiport also inhibit other cellular processes, including protein synthesis and phosphorylation. We have used an epidermal growth factor (EGF) receptor gene-amplified human breast cancer cell line, the growth of which is inhibited by high levels of EGF in culture (MDA-468) and a variant, the growth of which is stimulated by EGF (MDA-468-S4), along with two potent amiloride analogues to examine whether activation of the Na+/H+ antiport and cytoplasmic alkalinization is necessary for both EGF-dependent effects to occur. At concentrations of the amiloride analogues which block Na+/H+ exchange in both cell types by 76-98%, the EGF-dependent alterations in [3H]thymidine incorporation or induction in c-myc or c-fos gene transcription were unaltered. These results were confirmed by a lack of effect of the amiloride analogues on both the growth-stimulatory and growth-inhibitory effects on EGF in an anchorage-independent growth assay. Similarly, in pH-altered media that prevented normal cytoplasmic alkalinization, the response of both MDA-468 and MDA-468-S4 to EGF activation was unaltered. In addition, activation of the Na+/H+ antiport alone was not sufficient to induce c-myc and c-fos transcription in either cell type. Taken together, these data suggest that neither the Na+/H+ antiport nor cytoplasmic alkalinization are necessary or sufficient for either EGF-dependent growth stimulation or growth inhibition in MDA-468 human breast cancer cells.

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