22-02-2017, 08:09 AM
Also shared at BreastNexus:
(22-02-2017, 08:00 AM)Lotus Wrote: Proline-, glutamic acid-, and leucine-rich protein-1 (PELP1/MNAR) are estrogen receptor (ER) co-regulators, egg whites are an example of Leucine. Proline is an imino acid (technically), but can be made by glutamic acid........who knew it's an estrogen receptor co-regulator?......lol we do now.
Vitamin A (retinol) is pro-aromatase, castor oil is one example of vitamin A, (some Aloe Vera burn gel
have vitamin A...hint hint?).
I see soy has some limiting collagen effects, but honestly I'd stay away from soy considering how it destroys the thyroid.....it's weak at stimulating estrogen receptors (which is why you need so much of it to have some benefit). I also wouldn't take soy if your estrogen production is near normal....which has a reverse effect to lowering estrogen, while peploe with low estrogen production might see some (albeit cyclical results) raising estrogen.
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Review of Retinoid Biology: Part 2 (Increases production of hyaluronic acid and fibronectin)
Mariana Phillips, MD. (Updated July 2015*)
https://www.aad.org/File%20Library/Unass...logy-2.pdf
L-proline
http://aminoacidstudies.org/l-proline/
Slow peptide bond formation by proline and other N-alkylamino acids in translation.
Pavlov MY1, Watts RE, Tan Z, Cornish VW, Ehrenberg M, Forster AC.
Author information
Abstract
Proteins are made from 19 aa and, curiously, one N-alkylamino acid ("imino acid"), proline (Pro). Pro is thought to be incorporated by the translation apparatus at the same rate as the 19 aa, even though the alkyl group in Pro resides directly on the nitrogen nucleophile involved in peptide bond formation. Here, by combining quench-flow kinetics and charging of tRNAs with cognate and noncognate amino acids, we find that Pro incorporates in translation significantly more slowly than Phe or Ala and that other N-alkylamino acids incorporate much more slowly. Our results show that the slowest step in incorporation of N-alkylamino acids is accommodation/peptidyl transfer after GTP hydrolysis on EF-Tu. The relative incorporation rates correlate with expectations from organic chemistry, suggesting that amino acid sterics and basicities affect translation rates at the peptidyl transfer step. Cognate isoacceptor tRNAs speed Pro incorporation to rates compatible with in vivo, although still 3-6 times slower than Phe incorporation from Phe-tRNA(Phe) depending on the Pro codon. Results suggest that Pro is the only N-alkylamino acid in the genetic code because it has a privileged cyclic structure that is more reactive than other N-alkylamino acids. Our data on the variation of the rate of incorporation of Pro from native Pro-tRNA(Pro) isoacceptors at 4 different Pro codons help explain codon bias not accounted for by the "tRNA abundance" hypothesis.
https://www.ncbi.nlm.nih.gov/pmc/article.../zpq50.pdf
Proline P (Pro)
http://www.biology.arizona.edu/biochemis...oline.html
Newest Research on Why You Should Avoid Soy
https://www.mercola.com/article/soy/avoid_soy.htm
SEX HORMONE SYNTHESIS, REGULATION, AND FUNCTION
http://www.pathophys.org/sexhormones/
Retinoid acids promote the action of aromatase and 17 -hydroxysteroid dehydrogenase type 1 on the biosynthesis of 17 -estradiol in placental cells
Abstract
The biosynthesis of 17 -estradiol (E2) in human placenta involves the actions of aromatase and 17 -hydroxysteroid dehydrogenase type 1 (17HSD1). Aromatase, an enzyme complex comprised of P450aromatase (P450arom) and NADH-cytochrome P450 reductase, converts androgens to estrogens, whereas 17HSD1 catalyzes the reduction of estrone to E2. In the present study, the effects of retinoic acids (RAs) on P450arom and 17HSD1 expression in placental cells were investigated. Treatment with all-trans-RA (at-RA) or 9cis-RA increased E2 production in JEG-3 chorio- carcinoma cells and cytotrophoblast (CTB) cells isolated from normal early placentas. Meanwhile, the activity of aromatase and expression of P450arom mRNA were induced by at-RA in JEG-3 cells. Northern blot analysis showed that the effect on P450arom mRNA expression occurs in a dose- and time-dependent fashion. Similar to at-RA and 9cis-RA, Ro40–6055, the retinoic acid receptor (RAR )-selective activator, increased the expression.
http://joe.endocrinology-journals.org/co...1.full.pdf
Mol Cell Endocrinol. 2008 Aug 13;290(1-2):2-7. doi: 10.1016/j.mce.2008.04.019. Epub 2008 May 13.
PELP1--a novel estrogen receptor-interacting protein.
Brann DW1, Zhang QG, Wang RM, Mahesh VB, Vadlamudi RK.
Author information
Abstract
PELP1 (proline-, glutamic acid-, and leucine-rich protein-1) is a novel estrogen receptor (ER)-interacting protein that has been implicated to be important for mediation of both the genomic and nongenomic signaling of 17beta-estradiol (E2). PELP1 contains ten nuclear receptor-interacting boxes (LXXLL motifs), which allow it to interact with ER and other nuclear hormone receptors, a zinc finger, a glutamic acid-rich domain, and two proline-rich domains. The proline-rich regions contain several consensus PXXP motifs, which allow PELP1 to couple the ER with SH3 domain-containing kinase signaling proteins, such as Src and PI3K P85 regulatory subunit. PELP1 is expressed in many different brain regions, including the hippocampus, hypothalamus, and cerebral cortex. Further work has demonstrated that PELP1 is colocalized with ER-alpha in neurons in various brain regions. PELP1 is primarily expressed in neurons, with some expression also observed in glia. Subcellular localization studies revealed that PELP1 is highly localized in the cell nucleus of neurons, with some cytoplasm localization as well, and PELP1 is also localized at synaptic sites. Work in other tissues has demonstrated that PELP1 is critical for nongenomic and genomic signaling by E2, as PELP1 knockdown studies significantly attenuates E2-induced activation of ERK and Akt signaling pathways, and inhibits E2 genomic transcriptional effects on gene expression in breast cancer cells. Preliminary studies in the brain, suggests that similar roles may exist for PELP1 in the brain, but this remains to be established, and further work to characterize the precise roles and functions of PELP1 in the brain are needed.
PMID: 18571832 PMCID: PMC2578818 DOI: 10.1016/j.mce.2008.04.019