mTOR forms two functional complexes, C1 and C2. The C1 complex is more significant in health and disease. mTOR responds to signals from nutrients, growth factors, and cellular energy status and controls cell growth and proliferation based on this (by regulating protein synthesis).
Historically we've considered mental health and illness as coming from either one's life experiences or coming from one's genetics or biology. We've mistakenly considered the mind separate from the brain and the brain separate from the rest of the body. We are more interconnected than those outdated views suggest. Our physical health impacts our brain health. Likewise, we experience emotions (fear, anger, sadness, and joy) not only in our brains, but in our bodies. Emotions influence our brain's biochemistry, and our biochemistry impacts our emotions and how we experience our lives.
A perfect example of this is Pyrrole Disorder - a biochemical abnormality that causes the overproduction of
pyrroles. Pyrroles are a metabolite of hemoglobin (a protein in red blood cells that carries oxygen throughout the body). Pyrroles are not a problem and do not cause disease. We all have them. They do however, bind Vitamin B6 and Zinc. When pyrroles leave the body (through urine), they take some B6 and zinc with them. This is not a problem either. The problem comes when pyrroles are being overproduced for genetic reasons or because of physical or emotional stress. This can lead to severe B6 and zinc deficiencies
Hox genes encode evolutionarily conserved transcription factors that control skeletal patterning in the developing embryo. They are expressed in regionally restricted domains and function to regulate the morphology of specific vertebral and long bone elements. Recent work has provided evidence that Hox genes continue to be regionally expressed in adult tissues. Fibroblasts cultured from adult tissues show broadly maintained Hox gene expression patterns. In the adult skeleton, Hox genes are expressed in progenitor-enriched populations of mesenchymal stem/stromal cells (MSCs), and genetic loss-of-function analyses have provided evidence that Hox genes function during the fracture healing process. This review will highlight our current understanding of Hox expression in the adult animal and its function in skeletal regeneration. Developmental Dynamics 246:310–317, 2017. © 2016 Wiley Periodicals, Inc.
PQQ (pyrroloquinoline quinone) improves energy utilization and reproductive performance when added to rodent diets devoid of PQQ. In the present paper we describe changes in gene expression patterns and transcriptional networks that respond to dietary PQQ restriction or pharmacological administration. Rats were fed diets either deficient in PQQ (PQQ−) or supplemented with PQQ (approx. 6 nmol of PQQ/g of food; PQQ+). In addition, groups of rats were either repleted by administering PQQ to PQQ− rats (1.5 mg of PQQ intraperitoneal/kg of body weight at 12 h intervals for 36 h; PQQ−/+) or partially depleted by feeding the PQQ− diet to PQQ+ rats for 48 h (PQQ+/−). RNA extracted from liver and a Codelink® UniSet Rat I Bioarray system were used to assess gene transcript expression. Of the approx. 10000 rat sequences and control probes analysed, 238 were altered at the P<0.01 level by feeding on the PQQ− diet for 10 weeks. Short-term PQQ depletion resulted in changes in 438 transcripts (P<0.01). PQQ repletion reversed the changes in transcript expression caused by PQQ deficiency and resulted in an alteration of 847 of the total transcripts examined (P<0.01). Genes important for cellular stress (e.g. thioredoxin), mitochondriogenesis, cell signalling [JAK (Janus kinase)/STAT (signal transducer and activator of transcription) and MAPK (mitogen-activated protein kinase) pathways] and transport were most affected. qRT-PCR (quantitative real-time PCR) and functional assays aided in validating such processes as principal targets. Collectively, the results provide a mechanistic basis for previous functional observations associated with PQQ deficiency or PQQ administered in pharmacological amounts.
Retinoic acid (RA) and bile acids share common roles in regulating lipid homeostasis and insulin sensitivity. In addition, the receptor for RA (retinoid x receptor) is a permissive partner of the receptor for bile acids, farnesoid x receptor (FXR/NR1H4). Thus, RA can activate the FXR-mediated pathway as well. The current study was designed to understand the effect of all-trans RA on bile acid homeostasis. Mice were fed an all-trans RA-supplemented diet and the expression of 46 genes that participate in regulating bile acid homeostasis was studied. The data showed that all-trans RA has a profound effect in regulating genes involved in synthesis and transport of bile acids. All-trans RA treatment reduced the gene expression levels of Cyp7a1, Cyp8b1, and Akr1d1, which are involved in bile acid synthesis. All-trans RA also decreased the hepatic mRNA levels of Lrh-1 (Nr5a2) and Hnf4α (Nr2a1), which positively regulate the gene expression of Cyp7a1 and Cyp8b1. Moreover, all-trans RA induced the gene expression levels of negative regulators of bile acid synthesis including hepatic Fgfr4, Fxr, and Shp (Nr0b2) as well as ileal Fgf15. All-trans RA also decreased the expression of Abcb11 and Slc51b, which have a role in bile acid transport. Consistently, all-trans RA reduced hepatic bile acid levels and the ratio of CA/CDCA, as demonstrated by liquid chromatography-mass spectrometry. The data suggest that all-trans RA-induced SHP may contribute to the inhibition of CYP7A1 and CYP8B1, which in turn reduces bile acid synthesis and affects lipid absorption in the gastrointestinal tract.
Background. While high-protein consumption—above the current recommended dietary allowance for adults (RDA: 0.8 g protein/kg body weight/day)—is increasing in popularity, there is a lack of data on its potential adverse effects. Objective. To determine the potential disease risks due to high protein/high meat intake obtained from diet and/or nutritional supplements in humans. Design. Review. Subjects. Healthy adult male and female subjects. Method. In order to identify relevant studies, the electronic databases, Medline and Google Scholar, were searched using the terms:“high protein diet,” “protein overconsumption,” “protein overuse,” and “high meat diet.” Papers not in English were excluded. Further studies were identified by citations in retrieved papers. Results. 32 studies (21 experimental human studies and 11 reviews) were identified. The adverse effects associated with long-term high protein/high meat intake in humans were (a) disorders of bone and calcium homeostasis, (b) disorders of renal function, (c) increased cancer risk, (d) disorders of liver function, and (e) precipitated progression of coronary artery disease. Conclusions. The findings of the present study suggest that there is currently no reasonable scientific basis in the literature to recommend protein consumption above the current RDA (high protein diet) for healthy adults due to its potential disease risks. Further research needs to be carried out in this area, including large randomized controlled trials.
According to endocrinologists from the VU University Medical Center in Amsterdam, two of the most important hormones to focus on for natural weight loss and energy balance are ghrelin and leptin. (1) Many experts call ghrelin and leptin the “hunger hormones” because they work to either increase or decrease our appetite. (2)
Although certain weight loss programs involving taking artificial hormones — such as those that use human chorionic gonadotropin (HCG) to increase fat-burning — can be dangerous, there are safe and effective steps we can take to manipulate our natural hunger hormones and help us reach our weight-loss goals.
ncreasing leptin sensitivity may be very important if you are trying to lose weight as obese or overweight people tend to suffer from leptin resistance (insufficient response of body cells to leptin), which results in high leptin levels in blood and poor utilization of this hormone by the body. This article features an evidence based look at 23 foods that may help you deal with leptin resistance.
The name of the satiety hormone leptin originates from the Greek word leptos meaning thin. Leptin hormone is made up of adipose cells and its function is to control energy levels by inhibiting hunger (1).
The "hunger hormone" or ghrelin opposes actions of leptin. Both of these hunger hormones exert their effect on hypothalamus through receptors in arcuate nucleus to regulate hunger to attain energy homeostasis (2).
During obesity, sensitivity to leptin is decreased, as a result satiety is not detected in spite of presence of high energy stores (3).
We identified a strong association (p=5.36×10−17) between rs492602 in FUT2 and plasma vitamin B12 levels in a genome-wide scan (n=1,658) and an independent replication sample (n=1,059) from the Nurses' Health Study. Women homozygous for the rs492602 G allele had higher B12 levels. This allele is in strong linkage disequilibrium with the FUT2 W143X nonsecretor variant, suggesting a plausible mechanism for altered B12 absorption and plasma levels.