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Post-lunch Drowsiness
Postprandial somnolence (colloquially known as food coma, after-meal dip, or "the itis") is a normal state of drowsiness or lassitude following a meal. Postprandial somnolence has two components: a general state of low energy related to activation of the parasympathetic nervous system in response to mass in the gastrointestinal tract, and a specific state of sleepiness. While there are numerous theories surrounding this behavior, such as decreased blood flow to the brain, neurohormonal modulation of sleep through digestive coupled signaling, or vagus nerve, vagal stimulation, very few have been explicitly tested. To date, human studies have loosely examined the behavioral characteristics of postprandial sleep, demonstrating potential shifts in Electroencephalography, EEG spectra and self-reported sleepiness. To date, the only clear animal models for examining the genetic and neuronal basis for this behavior are the fruit fly, the mouse, and the nematode ''Caenorhabditis elegans''. ...
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Acetylcholine
Acetylcholine (ACh) is an organic compound that functions in the brain and body of many types of animals (including humans) as a neurotransmitter. Its name is derived from its chemical structure: it is an ester of acetic acid and choline. Parts in the body that use or are affected by acetylcholine are referred to as cholinergic. Acetylcholine is the neurotransmitter used at the neuromuscular junction. In other words, it is the chemical that motor neurons of the nervous system release in order to activate muscles. This property means that drugs that affect cholinergic systems can have very dangerous effects ranging from paralysis to convulsions. Acetylcholine is also a neurotransmitter in the autonomic nervous system, both as an internal transmitter for both the sympathetic nervous system, sympathetic and the parasympathetic nervous system, and as the final product released by the parasympathetic nervous system. Acetylcholine is the primary neurotransmitter of the parasympathet ...
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Branched-chain Amino Acids
A branched-chain amino acid (BCAA) is an amino acid having an aliphatic side-chain with a branch (a central carbon atom bound to three or more carbon atoms). Among the proteinogenic amino acids, there are three BCAAs: leucine, isoleucine, and valine. Non-proteinogenic BCAAs include 2-aminoisobutyric acid and alloisoleucine. The three proteinogenic BCAAs are among the nine essential amino acids for humans, accounting for 35% of the essential amino acids in muscle proteins and 40% of the preformed amino acids required by mammals. Synthesis for BCAAs occurs in all locations of plants, within the plastids of the cell, as determined by presence of mRNAs which encode for enzymes in the metabolic pathway. Oxidation of BCAAs may increase fatty acid oxidation and play a role in obesity. Physiologically, BCAAs take on roles in the immune system and in brain function. BCAAs are broken down effectively by dehydrogenase and decarboxylase enzymes expressed by immune cells, and are requi ...
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Tryptophan
Tryptophan (symbol Trp or W) is an α-amino acid that is used in the biosynthesis of proteins. Tryptophan contains an α-amino group, an α-carboxylic acid group, and a side chain indole, making it a polar molecule with a non-polar aromatic beta carbon substituent. Tryptophan is also a precursor to the neurotransmitter serotonin, the hormone melatonin, and vitamin B3 (niacin). It is encoded by the codon UGG. Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (–; pKa = 9.39) and the carboxylic acid is deprotonated ( –COO−; pKa = 2.38). Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid. Tryptophan is named after the digestive enzymes trypsin, which were used in its first isolation from casein proteins. It was assigned the one-letter symbol W based on the double ring being visually suggestive to the bulky letter. Function ...
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Skeletal Muscle
Skeletal muscle (commonly referred to as muscle) is one of the three types of vertebrate muscle tissue, the others being cardiac muscle and smooth muscle. They are part of the somatic nervous system, voluntary muscular system and typically are attached by tendons to bones of a skeleton. The skeletal muscle cells are much longer than in the other types of muscle tissue, and are also known as ''muscle fibers''. The tissue of a skeletal muscle is striated muscle tissue, striated – having a striped appearance due to the arrangement of the sarcomeres. A skeletal muscle contains multiple muscle fascicle, fascicles – bundles of muscle fibers. Each individual fiber and each muscle is surrounded by a type of connective tissue layer of fascia. Muscle fibers are formed from the cell fusion, fusion of developmental myoblasts in a process known as myogenesis resulting in long multinucleated cells. In these cells, the cell nucleus, nuclei, termed ''myonuclei'', are located along the inside ...
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Isoleucine
Isoleucine (symbol Ile or I) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), an α-carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a hydrocarbon side chain with a branch (a central carbon atom bound to three other carbon atoms). It is classified as a non-polar, uncharged (at physiological pH), branched-chain, aliphatic amino acid. It is essential in humans, meaning the body cannot synthesize it. Essential amino acids are necessary in the human diet. In plants isoleucine can be synthesized from threonine and methionine. In plants and bacteria, isoleucine is synthesized from a pyruvate employing leucine biosynthesis enzymes. It is encoded by the codons AUU, AUC, and AUA. Metabolism Biosynthesis In plants and microorganisms, isoleucine is synthesized from pyruvate and alpha-ketobutyrate. This pathway ...
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Leucine
Leucine (symbol Leu or L) is an essential amino acid that is used in the biosynthesis of proteins. Leucine is an α-amino acid, meaning it contains an α-amino group (which is in the protonated −NH3+ form under biological conditions), an α-Carboxylic acid, carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain Isobutyl, isobutyl group, making it a Chemical polarity, non-polar Aliphatic compound, aliphatic amino acid. It is Essential amino acid, essential in humans, meaning the body cannot synthesize it; it must be obtained from the diet. Human dietary sources are foods that contain protein, such as meats, dairy products, soy products, and beans and other legumes. It is genetic code, encoded by the codons UUA, UUG, CUU, CUC, CUA, and CUG. Leucine is named after the Greek language, Greek word for "white": ''λευκός'' (''leukós'', "white"), after its common appearance as a white powder, a property it shares with many ...
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Valine
Valine (symbol Val or V) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated −NH3+ form under biological conditions), an α- carboxylic acid group (which is in the deprotonated −COO− form under biological conditions), and a side chain isopropyl group, making it a non-polar aliphatic amino acid. Valine is essential in humans, meaning the body cannot synthesize it; it must be obtained from dietary sources which are foods that contain proteins, such as meats, dairy products, soy products, beans and legumes. It is encoded by all codons starting with GU (GUU, GUC, GUA, and GUG). History and etymology Valine was first isolated from casein in 1901 by Hermann Emil Fischer. The name valine comes from its structural similarity to valeric acid, which in turn is named after the plant valerian due to the presence of the acid in the roots of the plant. Nomenclature According to IUPAC, carbon atoms forming v ...
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Insulin
Insulin (, from Latin ''insula'', 'island') is a peptide hormone produced by beta cells of the pancreatic islets encoded in humans by the insulin (''INS)'' gene. It is the main Anabolism, anabolic hormone of the body. It regulates the metabolism of carbohydrates, fats, and protein by promoting the absorption of glucose from the blood into cells of the liver, fat cell, fat, and skeletal muscles. In these tissues the absorbed glucose is converted into either glycogen, via glycogenesis, or Fatty acid metabolism#Glycolytic end products are used in the conversion of carbohydrates into fatty acids, fats (triglycerides), via lipogenesis; in the liver, glucose is converted into both. Glucose production and secretion by the liver are strongly inhibited by high concentrations of insulin in the blood. Circulating insulin also affects the synthesis of proteins in a wide variety of tissues. It is thus an anabolic hormone, promoting the conversion of small molecules in the blood into large ...
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Carbohydrate Metabolism
Carbohydrate metabolism is the whole of the biochemistry, biochemical processes responsible for the metabolic anabolism, formation, catabolism, breakdown, and interconversion of carbohydrates in life, living organisms. Carbohydrates are central to many essential metabolic pathways. Plants synthesize carbohydrates from carbon dioxide and water through photosynthesis, allowing them to store energy absorbed from sunlight internally. When animals and fungi consume plants, they use cellular respiration to break down these stored carbohydrates to make energy available to cells. Both animals and plants temporarily store the released energy in the form of high-energy molecules, such as adenosine triphosphate (ATP), for use in various cellular processes. While carbohydrates are essential to human biological processes, ''consuming'' them is not essential for humans. There are healthy human populations that do not consume carbohydrates. In humans, carbohydrates are available directly from co ...
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Glycemic Index
The glycemic (glycaemic) index (GI; ) is a number from 0 to 100 assigned to a food, with pure glucose arbitrarily given the value of 100, which represents the relative rise in the blood glucose level two hours after consuming that food. The GI of a specific food depends primarily on the type of carbohydrate it contains, but is also affected by the amount of entrapment of the carbohydrate molecules within the food, the fat, protein content of the food, the moisture and fiber content, the amount of organic acids (or their salts) (e.g., citric or acetic acid), and the method of cooking. GI tables, which list many types of foods and their GIs, are available. A food is considered to have a ''low GI'' if it is 55 or less; ''high GI'' if 70 or more; and ''mid-range GI'' if 56 to 69. The term was introduced in 1981 by David J. Jenkins and co-workers and was created to compare the relative effects of different foods on postprandial glucose levels. It is useful for quantifying the relati ...
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Fight-or-flight Response
The fight-or-flight or the fight-flight-freeze-or-fawn (also called hyperarousal or the acute stress response) is a physiological reaction that occurs in response to a perceived harmful event, attack, or threat to survival. It was first described by Walter Bradford Cannon in 1915. His theory states that animals react to threats with a general discharge of the sympathetic nervous system, preparing the animal for fighting or fleeing. More specifically, the adrenal medulla produces a hormonal cascade that results in the secretion of catecholamines, especially norepinephrine and epinephrine. The hormones estrogen, testosterone, and cortisol, as well as the neurotransmitters dopamine and serotonin, also affect how organisms react to stress. The hormone osteocalcin might also play a part. This response is recognised as the first stage of the general adaptation syndrome that regulates stress responses among vertebrates and other organisms. Name Originally understood as the "figh ...
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