the-psoriasis-treatment

You've heard that spinach has a lot of iron, right? But what you may not know is that spinach is a poor way to get iron because of its content of phytate. Some of the iron in spinach is bound to phytate. Most of the iron you get is absorbed in the small intestine's duodenum. It comes into the mucosal cell as either a free ion or as heme. If iron is attached to phytates, however, its resistant to disassociation in the gut. One way to help improve the absorption is by cooking the spinach to break down ligands attached to the iron. And by combining protein with your spinach, you can cause the stomach to release more hydrochloric acid, lowering the pH and helping free up some more iron. When people have stomach problems that inhibit their ability to release hydrochloric acid (such as when people become older), it's known that a lot of iron is not absorbed at all. In these cases, it may be important to increase the amount of iron in the diet (specifically heme iron from animal f...

Humans didn’t always have restaurants and grocery stores to visit on every corner. As part of human evolution, in fact, most of the time it’s likely our ancestors were starving quite often and got pretty good at it while foraging and hunting. It took the agricultural revolution to really make a shift to food aplenty. But starvation hasn’t gone away by any stretch. It’s a daily reality for much of the underdeveloped world. And, a bit closer to my reality, my own great grandmother often shared stories with me about how she’d go for weeks without meals as a little girl. To be able to survive from meal to meal, we depend on a starve-feed cycle. It refers to the changes in metabolism that allows variable fuel and nitrogen consumption to meet variable metabolic and anabolic demand (1). In plain English, it is what gives humans capacity to eat food well beyond caloric requirements and store it as glycogen and triacylglycerol to utilize when needed (1). This is what happens to someone biochemi...

Fat is absorbed in the intestine contained in chylomicrons and then secreted into lymphatics (1). The lymphatics drain the intestine, then lead to the thoracic duct and deliver the chylomicrons into the blood at a site of rapid blood flow (1). The rapidity is necessary to distribute the chylomicrons well preventing them from coalescing (1). Then lipoprotein lipase, which is attached to endothelial cell survaces in the lumen of capillaries, acts on the chylomicrones to liberate fatty acids via hydrolysis (1). The fatty acids are taken up by adipocytes and reesterified with glycerol 3-phosphate to form triacylglycerols and be stored as fat droplets (1). Reference 1. Devlin TM. Textbook of Biochemistry with Clinical Correlations. Philadelphia: Wiley-Liss, 2002.

When you’ve just eaten some protein, insulin, glucagon, growth hormone and glucocorticoids increase because of the presence of elevated amino acid concentration (1p232). The insulin promotes the protein synthesis and the other hormones have an opposite effect (1p232). Growth hormone is anabolic like insulin, although counterregulatory (1p232). Insulin to glucagon ratio favoring insulin stimulates protein synthesis enzymes and vice versa (1p232). The insulin is needed for uptake of amino acids across the cell membrane and antagonizing activation of amino acid oxidation by some enzymes (1p206-207). Protein synthesis is also sensitive to multiple influences including stability of mRNA, amount of rRNA, activity of ribosomes, and (most important from diet), the presence of essential and nonessential amino acids in appropriate concentration to charge the tRNA and hormone environment (1p232). When amino acids are not present or not present in sufficient quantity, amino acid oxidation increase...

I just got done working out, sort of; I did manage to break a sweat. Then I made myself a high-protein shake and was sure to include a banana for carbs. Why do I do this again? Aren’t carbs a bad thing? Well, it turns out that I need those carbs to stimulate insulin secretion to promote tissue cell uptake and use of the amino acids (1p206)(1). For this reason, it doesn’t make too much sense to take protein with some other kind of sweetener. The insulin affects movement of amino cid transporters to the membrane and their activity while also antagonizing activation of some enzymes that oxidize amino acids—very important if you’re trying to put on muscle (1p206-207)! You don’t want glucagon to dominate, leaving you with protein degradation (1p207). At least I don’t. Insulin stimulates protein synthesis and inhibits its degradation (1p207). My shake’s protein content happens to be made up of contain whey and casein. That’s a good thing for me because whey is considered a “fast” protein tha...

Last week while attempting to meet a deadline at work I skipped lunch and soon enough began hearing my stomach growl. The “hunger hormone” ghrelin, I knew, had kicked in; it would react with the receptors of my hypothalamus to release certain neurotransmitters and my brain would tell me I wanted macronutrients (1p299). Carbs, fats, protein, anything would do. But I didn’t have anything to eat so I thought, “What happens if I starve?” The answer is pretty straightforward. My body’s insulin would drop while glucagon would rise (1p246). Muscle and fat tissue would also become a bit resistant to insulin (1p246). Protein synthesis would drop (1p246). Glycogen from my liver would start becoming used up and muscles would release a mix of amino acids for gluconeogenesis (stimulating the glucagon) (1p246). The liver would keep my blood sugar level stable (1p246). If I didn’t eat for awhile, then my tissues would keep using fatty acids and glucose, but also start using ketones (from the fatty a...

Raw milk and undenatured whey has been claimed to be better for you than their pasteurized and ultra-high-heat treated alternatives. Considering, however, that protein simply becomes denatured anyway in your gut (1), it would hardly make sense to care whether or not it was denatured. But a French study in the latest J Nutr and other studies explain that when milk protein is exposed to ultra-high heat (but not pasteurization), digestibility and nutritional content due can be affected (2-4). The change occurs not specifically due to denaturation, but due to Maillard reactions (reaction between amino acids and sugars) from heat, production of unusual amino acids such as furosine, and reduced availability of essential amino acids (2-4). Pasteurization resulting in partial denaturation of milk and whey has also been shown to create a biological significance on the bioavailability of nutrients such as folic acid (5). Still, I fear microbes, so suggest avoiding raw milk. Instead, try low-temp...

Deamination examples The amino acid threonine has its amino group removed by threonine dehydratase (1p209). This particular amino acid is commonly deaminated along with glutamate, histidine, serine and glycine (1p209). In the case of thronine, the reaction proceeds with loss of water, which is why the enzyme catalyzing the reaction is called a dehydratase instead of a deaminase (1p209). Vitamin B6 is important for this reaction to occur (1p209). The amino group is used by periportal hepatocytes to synthesize urea (1p209). Transamination examples The transfer of an amino groupf from one amino acid to an amino acid carbon skeleton or alpha-keto acid occurs to feed protein synthesis (1p209). The enzymes include tyrosine aminotransferase, branched-chain aminotransferases, alanine aminotransferase, and aspartate aminotransferase (1p209). The enzymes can often require vitamin B6 in a coenzyme form (1p209). The reactions are reversible and are often used to create non-essential amino acids f...

Protein denaturation is the unfolding of the secondary or tertiary structures (1). For example, heat can denature proteins in eggs by disrupting hydrogen bonds and non-polar hydrophobic interactions and as a result the egg proteins coagulate during cooking (1). Alcohol, like heat, can also disrupt hydrogen bonds, and acids, bases and heavy metal salts denature proteins by disrupting salt bridges (1). What are biochemical consequences of denaturation of insulin? In the body, protein denaturation can affect processes biochemically. Native insulin, for example, in the presence of increased, urea may be denatured because of changes in pH or, in the presence of a thiol catalyst, may be denatured due to isomerization (2). The insulin, thus, is unable to properly cause cells to take up glucose as it should (2). Reference List 1. Ophardt CE. 2003. “Denaturation of Proteins.” Virtual Chembook. Available at: http://www.elmhurst.edu/~chm/vchembook/568denaturation.html 2. Jiang C, Jui-Yoa Chang. ...

Type 1 diabetes is characterized by autoimmune destruction of beta cells in the islets of Langerhans, which results in lack of insulin secretion (1). Glucose, then cannot be taken up by cells leading to hyperglycemia and osmotic diuresis (1). The low insulin will also stimulate hepatic glycogenolysis and gluconeogenesis to produce glucose released into blood leading into accentuated hyperglycemia (1). What’s more is that gluconeogenesis becomes chronic depleting body proteins to break down into amino acids (1). Muscle,in effect, atrophes converting to glucose and lost through the diuresis (1). Weakness, fatigue and weight loss all occur (1). Insulin inhibits degradation of protein and increases protein synthesis (2). Opposite to this, lack of insulin creates an environment favoring glucagon leaving degradation of protein unchecked and protein synthesis diminished (2). The degradation occurs by action of proteases—lysosomal or proteosomal—or via the calcium-activated proteolytic degrada...

Arginine is used for synthesis of protein, agmatine, polyamines and creatine [1]. Because kidneys synthesize arginine usually in sufficient amounts in the urea cycle(releasing 2-4g daily), it's normally not necessary to attain it from the diet [1p196;229]. At times, however, arginine can become conditionally essential [1p229]. Such times would include protein malnutrition, excessive ammonia production, excessive lysine intake, burns, infections, peritoneal dialysis, rapid growth, urea synthesis disorders, or in the inflammatory state of sepsis [2]. A deficiency could result in fatty liver, poor wound healing, hair loss, skin rash and constipation [2]. Arginine is changed into nitric oxide causing blood vessel relaxation [2], which can lower blood pressure. Thus, should not be used by a patient with low blood pressure [3]. If suffering of sickle cell disease, arginine can worsen symptoms [3]. One should exercise caution if supplementing with arginine because the amino acid is known ...

Urea cycle regulation is dependent on dietary factors and hormone concentrations (1). A feed-forward regulation exists in that available ammonia causes more urea to be created (1). This can also mean that higher protein can also act as a feed-forward regulation since it increases urea enzyme levels (1-2). Ammonia can come from diet, from deamination, or bacteria in the GI tract inducing formation of carbamoyl phosphate by mitochondrial carbamoyl phosphate synthetase (1). Other regulation also exists. First, synthesis of n-acetyl glutamate, which is the allosteric activator of the carbamoyl phosphate synthetase (2). The activator is made in the liver and intestine when stimulated by available arginine (1-2). Second, arginase is inhibited by ornithine and lysine making it able to become rate limiting (1). Reference List 1. Gropper SS, Smith JL, Groff JL. Advanced Nutrition and Human Metabolism. Belmont, CA: Thomson Wadsworth, 2009. 2. Lieberman M, Marks A, Smith CM, Marks DB. Marks’ basi...

While Dietary Reference Intakes for protein are 0.8g protein per kg for adults, data suggest athletes may need more depending on their sport, particularly strength-training athletes (1). Research also indicates that even non-athletes who weight train may benefit from the added protein (2). Endurance exercise sports such as cycling and running increase protein turnover, including a lot more oxidation amino acids, so it is suggested that extra protein would also be wise (3;4). However, many athletes often exceed intake required (5). While the positive balance may not affect competitiveness, excessiveness does not encourage further muscle growth or strength gain (5). It should also be noted that strength-training itself also encourages improved utilization of dietary protein possibly reducing need of added protein (5). When consumed with carbohydrate, net protein balance during and after endurance exercise is improved, but there is little evidence of actual improved performance due to the...

It's clear that carbohydrates with protein affects insulin, thereby inducing glycogen synthesis. However, I was left thinking, “But what kind of carbohydrate is best?” And I found a study that suited my curiosity. One published in 2007 in J Int Soc Sports Nutr showed that 40 subjects who weight trained taking 40g of whey protein were also given 120g of sucrose, honey or maltodextrin (1). After 30 minutes, the honey group showed greatest glucose concentration and best degree of blood glucose maintenance; however, there was really no significant difference and either can be used (1). Reference List 1. Tipton KD, Elliott TA, Cree MG, Aarsland AA, Sanford AP, Wolfe RR. Stimulation of net muscle protein synthesis by whey protein ingestion before and after exercise. Am J Physiol Endocrinol Metab 2007;292:E71-E76.

Arginine is a precursor for nitric oxide, which relaxes vascular smooth muscle leading to improved blood flow and, thus, the flow of nutrients to muscles (1;2). Oral arginine appears to also stimulate growth hormone release, especially when taken with exercise (3). Supplementation with arginine didn’t increase body mass significantly in a study in 2008; although, when taken with creatine, arginine did improve endurance and power of muscle (2). Reference List 1. Gropper SS, Smith JL, Groff JL. Advanced Nutrition and Human Metabolism. Belmont, CA: Thomson Wadsworth, 2009. 2. Little JP, Forbes SC, Candow DG, Cornish SM, Chilibeck PD. Creatine, arginine alpha-ketoglutarate, amino acids, and medium-chain triglycerides and endurance and performance. Int J Sport Nutr Exerc Metab 2008;18:493-508. 3. Kanaley JA. Growth hormone, arginine and exercise. Curr Opin Clin Nutr Metab Care 2008;11:50-4.

You might think so. In theory, glutamine supplementation appears to make sense. Supplementation increases plasma glutamine in the plasma (1), which is thought to support the immune system (2;3) because the immune system uses glutamine for energy production (4). Plus, because exercise causes muscles to increase use of glutamine, stores are depleted (4). However, according to a 2001 study showed glutamine does not have any “significant effect on muscle performance, body composition or muscle protein degradation” (5). Reference List 1. Maughan RJ. Nutritional ergogenic aids and exercise performance. Nutr Res Rev 1999;12:255-80. 2. Williams MH. Facts and fallacies of purported ergogenic amino acid supplements. Clin Sports Med 1999;18:633-49. 3. Nieman DC. Exercise and resistance to infection. Can J Physiol Pharmacol 1998;76:573-80. 4. Gropper SS, Smith JL, Groff JL. Advanced Nutrition and Human Metabolism. Belmont, CA: Thomson Wadsworth, 2009. 5. Candow DG, Chilibeck PD, Burke DG, Davison ...

Saturated fats including trans fat can lead to a increased risk of cardiovascular disease mainly by raising cholesterol and causing a poor LDL:HDL ratio (1). Trans fat is thought to be more atherogenic because it has also been found to lower HDL cholesterol in studies (1-3). But what about diabetes risk? In 2006 a review on the literature of trans fats versus saturated fats in insulin resistance noted that while high intake of saturated fats may promote insulin resistance, it is too early to determine if trans fats create increased risk(3). However, a 2008 rat study published in Asia Pac J Clin Nutr (2) showed that rats fed a diet higher in saturated fats had decreased peripheral insulin sensitivity, but that if trans fat was included the effect was greater. Biochemically the reason for the effects on insulin sensitivity from dietary trans fat may have to do with its potential interference with cell membrane functions and decreasing insulin concentration (3-5). Ultimately both saturate...

The presence of ovomucin, a natural trypsin inhibitor in eggs, can help block some of egg cholesterol absorption and bile acid reabsorption through enterohepatic circulation (1). Despite ovomucin, however, there does appear to be enough dietary cholesterol in eggs absorbed that can potentially cause increased cholesterol levels (2;3). Reference List 1. Nagaoka S, Masaoka M, Zhang Q, Hasegawa M, Watanabe K. Egg ovomucin attenuates hypercholesterolemia in rats and inhibits cholesterol absorption in Caco-2 cells. Lipids 2002;37:267-72. 2. Levy Y, Maor I, Presser D, Aviram M. Consumption of eggs with meals increases the susceptibility of human plasma and low-density lipoprotein to lipid peroxidation. Ann Nutr Metab 1996;40:243-51. 3. Applebaum-Bowden D, Hazzard WR, Cain J, Cheung MC, Kushwaha RS, Albers JJ. Short-term egg yolk feeding in humans. Increase in apolipoprotein B and low density lipoprotein cholesterol. Atherosclerosis 1979;33:385-96.

Raw egg white contains avidin. As dietary protein is digested, the presence of avidin can bind to biotin tightly preventing its absorption into the body (1). Because biotin is used as a prosthetic group in acetyl CoA carboxylase, a biotin deficiency can then inhibit the carboxylation reaction catalyzed by acetyl CoA carboxylase that converts malonyl CoA from acetyl CoA and CO2 (2). The conversion to malonyl CoA is ultimately the reaction by which carbons of a fatty acid are contributed to by acetyl CoA (2). Cooking destroys the avidin, which is a good thing. But wait, an article in the latest Journal of Nutrition explains that Maillard reaction products (result of heating proteins and sugars) may alter amino acid availability and reduce digestibility of certain proteins (3). It would lead to believe that you'd want your protein raw or microfiltered versus fried or treated with ultra-high temperatures. Sure enough, you'll get more protein from a raw egg, plus enzymes and vitami...

Along with the recommendation of exercise and a healthy diet (including a bit of red wine daily), both lovastatin and cholestyramine can be used in the treatment of familial hypercholesterolemia (1;2). While lovastatin works as a HMG CoA reductase inhibitor to reduce cholesterol synthesis in the liver, cholestyramine acts as a bile acid-binding resin that increases fecal removal of cholesterol (1p152;3-4). Reference List 1. Gropper SS, Smith JL, Groff JL. Advanced Nutrition and Human Metabolism. Belmont, CA: Thomson Wadsworth, 2009. 2. Netdoctor.co.uk. Familial hypercholesterolemia. Available at: http://www.netdoctor.co.uk/diseases/facts/familialhypercholesterolaemia.htm . 3. Netdoctor.co.uk. Questran (colestyramine). Available at: http://www.netdoctor.co.uk/medicines/100002209.html . 4. Medicine.net. Lovastatin (oral). Available at: http://www.medicinenet.com/lovastatin-oral/article.htm .