[Lotus]

Foods that reduce breast growth turn hormones into their sulfur forms. The sulfur form of estrogen is more than 100 times weaker than the normal form. Therefore, eating foods with these sulfur properties can reverse breast growth.

Hi Jhalem,
Do you have any science (papers) that supports your claim?

Estrogen sulfates are quantitatively the most important form of circulating estrogens during the menstrual cycle and in the post-menopausal period. Huge quantities of estrone sulfate and estradiol sulfate are found in the breast tissues of patients with mammary carcinoma.

Estrone sulfate is converted in a very high percentage to estradiol (E2) in different hormone-dependent mammary cancer cell lines (MCF-7, R-27, T-47D)

http://www.sciencedirect.com/science/article/pii/0022473189900770

Celery inhibits 5 alpha reductase , black pepper improves bioavailability of P450-cyp34 enzyme and helps lower cholesterol (both postive for NBE). Zinc inhibits 5 alpha reductase:

5 alpha reductase inhibitor FOOD LIST
http://www.breastnexus.com/showthread.php?tid=17436&pid=159358&highlight=Black+pepper#pid159358

NBE food list
http://www.breastnexus.com/showthread.php?tid=23292&pid=148145&highlight=Black+pepper#pid148145

Black pepper and piperine reduce cholesterol uptake and enhance translocation of cholesterol transporter proteins.
http://www.ncbi.nlm.nih.gov/m/pubmed/22736065/?i=6&from=/21434835/related

Thanks POM, sorry Ella.

Here's an example of what how interactions can happen, multiplying its effects. Say you drink green tea (a CYP17 inhibitor of testosterone). Now because you add piperine (in certain supplements, or added by supplementing) it increases the EGCG (polyphenols) in green tea by 1.3 fold.



J Nutr. 2004 Aug;134(8):1948-52.
Piperine enhances the bioavailability of the tea polyphenol (-)-epigallocatechin-3-gallate in mice.
Lambert JD1, Hong J, Kim DH, Mishin VM, Yang CS.
Author information
Abstract
(-)-Epigallocatechin-3-gallate (EGCG), from green tea (Camellia sinensis), has demonstrated chemopreventive activity in animal models of carcinogenesis. Previously, we reported the bioavailability of EGCG in rats (1.6%) and mice (26.5%). Here, we report that cotreatment with a second dietary component, piperine (from black pepper), enhanced the bioavailability of EGCG in mice. Intragastric coadministration of 163.8 micromol/kg EGCG and 70.2 micromol/kg piperine to male CF-1 mice increased the plasma C(max) and area under the curve (AUC) by 1.3-fold compared to mice treated with EGCG only. Piperine appeared to increase EGCG bioavailability by inhibiting glucuronidation and gastrointestinal transit. Piperine (100 micromol/L) inhibited EGCG glucuronidation in mouse small intestine (by 40%) but not in hepatic microsomes. Piperine (20 micromol/L) also inhibited production of EGCG-3"-glucuronide in human HT-29 colon adenocarcinoma cells. Small intestinal EGCG levels in CF-1 mice following treatment with EGCG alone had a C(max) = 37.50 +/- 22.50 nmol/g at 60 min that then decreased to 5.14 +/- 1.65 nmol/g at 90 min; however, cotreatment with piperine resulted in a C(max) = 31.60 +/- 15.08 nmol/g at 90 min, and levels were maintained above 20 nmol/g until 180 min. This resulted in a significant increase in the small intestine EGCG AUC (4621.80 +/- 1958.72 vs. 1686.50 +/- 757.07 (nmol/g.min)). EGCG appearance in the colon and the feces of piperine-cotreated mice was slower than in mice treated with EGCG alone. The present study demonstrates the modulation of the EGCG bioavailablity by a second dietary component and illustrates a mechanism for interactions between dietary chemicals.

http://www.ncbi.nlm.nih.gov/pubmed?filters=&orig_db=PubMed&cmd=Search&term=134%2A%5Bvolume%5D%20AND%201948%5Bpage%5D%20AND%202004%5Bpdat%5D%20AND%20Lambert%20JD%5Bauth%5D

Inhibition of 5 alpha-reductase activity in human skin by zinc and azelaic acid.
https://www.ncbi.nlm.nih.gov/m/pubmed/3207614/

concentrations of 3 or 9 mmol/l, zinc was a potent inhibitor of 5 alpha-reductase activity. At high concentrations, zinc could completely inhibit the enzyme activity