Group for 'hormonally driven' C's http://health.groups.yahoo.com/group/FitCare

[Guest guest]

Well, here it is folks.

The reincarnation / reinvention / regurgitation of PC-ACT. Before that it was

PC-SPES (2001) and before that EPCEL (1998), with other groups in between.

One thing they had in common was prostate cancer. Now it has changed.

After much research there came the realisation (for me and a few others at

least) that prostate cancer and other 'hormonally driven' cancers had a common

natural cause in fetal estrogen imprinting. [Prins et al.]

I hope by debating this aspect [ championed by Gustafsson et al. who

investigated the estrogen receptors alpha and beta] we will be able to arrive at

(maybe even discover) routes of prevention and cure[e.g. 1,2] for all these

diseases that until now have been hidden away. It is a long shot, but without

debating it out in the open we will never get closer to the truth.

Feel free to join whatever your background, just remember the usual rules of

etiquette when entering into correspondence. No spam.

Oh yes, and feel free to pass on the link to anyone who may be interested.

http://groups.yahoo.com/group/FitCare

Or,

FitCare-subscribe

Cheers,

Sammy.

1. 1. J Steroid Biochem Mol Biol. 2010 Feb 13. Vitamin D and breast cancer:

Inhibition of estrogen synthesis and signaling. Krishnan AV, Swami S, Feldman D.

Division of Endocrinology, Department of Medicine, Stanford University School of

Medicine, Stanford, CA 94305, United States.

Calcitriol (1,25-dihydroxyvitamin D(3)), the hormonally active metabolite of

vitamin D, inhibits the growth and induces the differentiation of many

malignantcells including breast cancer (BCa) cells. Calcitriol exerts its

anti-proliferative activity in BCa cells by inducing cell cycle arrest

andstimulating apoptosis. Calcitriol also inhibits invasion, metastasis and

tumorangiogenesis in experimental models of BCa. Our recent studies show

additionalnewly discovered pathways of calcitriol action to inhibit the growth

of BCacells. Calcitriol suppresses COX-2 expression and increases that of

15-PGDHthereby reducing the levels and biological activity of prostaglandins

(PGs).Calcitriol decreases the expression of aromatase, the enzyme that

catalyzesestrogen synthesis selectively in BCa cells and the breast adipose

tissuesurrounding BCa, by a direct repression of aromatase transcription via

promoterII as well as an indirect effect due to the reduction in the levels

andbiological activity of PGE(2), which is a major stimulator of

aromatasetranscription through promoter II in BCa. Calcitriol down-regulates

theexpression of estrogen receptor alpha and thereby attenuates estrogen

signalingin BCa cells including the proliferative stimulus provided by

estrogens. Wehypothesize that the inhibition of estrogen synthesis and signaling

by calcitrioland its anti-inflammatory actions will play an important role in

the use ofcalcitriol for the prevention and/or treatment of BCa. Copyright ©

2010 Elsevier Ltd. All rights reserved.PMID: 20156557

2. J Steroid Biochem Mol Biol. 2007 Feb;103(2):189-95. Regulation of human

estrogen

receptor alpha-mediated gene transactivation in Saccharomyces cerevisiae by

human coactivator and corepressor proteins. Bitter GA. BitTech, Inc., Westlake

Village, CA 91361, USA. gab@...

Human estrogen receptor alpha (ERalpha)-mediated transcription activation was

evaluated in the yeast Saccharomyces cerevisiae using both the native ERalpha

and a G400V variant. A previous study demonstrated that coexpression of human

SRC-1, a potent stimulator of ERalpha function in mammalian cells, potentiated

ERalpha-mediated gene expression in yeast over five-fold in an E(2)-dependent

manner. In the present study, two additional human coactivator proteins were

shown to potentiate ERalpha-mediated gene expression in yeast. SRC2 potentiated

transactivation two- to three-fold while SRC3 potentiated transactivation

five-to eight-fold. Both human coactivators potentiated both the native ERalpha

and the G400V variant in an E(2)-dependent manner. The effect of a human

corepressor protein was also evaluated in yeast. Repressor of estrogen receptor

activity (REA) did not affect E(2)-induced transactivation by ERalpha (either

isoform). However, in a strain that coexpressed human SRC1, REA reduced

E(2)-induced transactivation to that observed with ERalpha alone. Furthermore,

repression of SRC1 potentiation was specific for the native ERalpha since REA

had no effect on SRC1 potentiation of the G400V variant. Additionally, REA

repression was specific for SRC1 since potentiation of ERalpha (either isoform)

transactivation by SRC2and SRC3 was unaffected by coexpression of REA. These

results support previousobservations in mammalian cells that REA does not

prevent ERalpha from bindingtoDNA but does inhibit potentiation of

ERalpha-mediated transactivation by SRC1.The results in the present study

further characterize REA-mediated repression,and demonstrate the utility of this

yeast system for dissecting molecularmechanisms involved in regulating gene

transactivation by human ERalpha. PMID: 17194583