ch0.1 -- misc vocabulary Flashcards
analgesia
inability to feel pain
bracketing technique
performing a sport movement with less than normal and greater than normal resistance; another form of acceleration training
dorsal
toward the posterior. from Latin dorsum, meaning ‘back’ – surface of an organism refers to the back, or upper side, of an organism. if talking about the skull, the dorsal side is the top.
ventral
toward the anterior. from Latin venter, meaning ‘belly’. surface refers to the front, or lower side, of an organism.
kyphotic
forward rounding of the back (hunchback); from ‘kyphos’ or ‘hump’ in greek. most common in older women and often related to osteoporosis.
lordotic
curving inward of lower back. some lordosis is normal, too much is referred to as swayback. lumbar lordosis makes you look like a chicken or goose.
rate coding
the rate at which the motor units are fired. as the intensity of a stimulus increases, the frequency or rate of action potentials, or “spike firing”, increases; rate coding is sometimes called frequency coding.
drag
a force acting opposite to the relative motion of any object moving with respect to a surrounding fluid. sometimes called air resistance, a type of friction, or fluid resistance.
surface drag
friction of a fluid passing along the surface of an object; in alternate words, drag caused by the friction of a fluid against the surface of an object that is moving through it.
form drag
fluid resistance from the way a fluid presses against the front or rear of an object passing through it
kinase
an enzyme that catalyzes the transfer of a phosphate group from ATP to a specified molecule
lactate vs lactic acid
Lactate is lactic acid, missing one proton. To be an acid, a substance must be able to donate a hydrogen ion; when lactic acid donates its proton, it becomes its conjugate base, or lactate.
adenylate kinase
a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides (ATP, ADP, and AMP)
adenylate kinase reaction
2ADP ATP + AMP; particularly important because AMP is a product of the adenylate kinase (myokinase) reaction, a powerful stimulant of glycolysis
hexokinase
an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate is the most important product
phosphorus
chemical element with the symbol P and atomic number 15. Elemental phosphorus exists in two major forms, white phosphorus and red phosphorus, but because it is highly reactive, phosphorus is never found as a free element on Earth. It has a concentration in the Earth’s crust of about one gram per kilogram (compare copper at about 0.06 grams). In minerals, phosphorus generally occurs as phosphate. Phosphorus is essential for life. Phosphates (compounds containing the phosphate ion, PO43−) are a component of DNA, RNA, ATP, and phospholipids. Elemental phosphorus was first isolated from human urine, and bone ash was an important early phosphate source. Phosphate mines contain fossils because phosphate is present in the fossilized deposits of animal remains and excreta. Low phosphate levels are an important limit to growth in some aquatic systems. The vast majority of phosphorus compounds mined are consumed as fertilisers. Phosphate is needed to replace the phosphorus that plants remove from the soil, and its annual demand is rising nearly twice as fast as the growth of the human population. Other applications include organophosphorus compounds in detergents, pesticides, and nerve agents.
pyruvate
Pyruvic acid (CH3COCOOH) is the simplest of the alpha-keto acids, with a carboxylic acid and a ketone functional group. Pyruvate, the conjugate base, CH3COCOO−, is a key intermediate in several metabolic pathways throughout the cell. Pyruvic acid can be made from glucose through glycolysis, converted back to carbohydrates (such as glucose) via gluconeogenesis, or to fatty acids through a reaction with acetyl-CoA. It can also be used to construct the amino acid alanine and can be converted into ethanol or lactic acid via fermentation. Pyruvic acid supplies energy to cells through the citric acid cycle (also known as the Krebs cycle) when oxygen is present (aerobic respiration), and alternatively ferments to produce lactate when oxygen is lacking (lactic acid).
allosteric
relating to or denoting the alteration of the activity of a protein through the binding of an effector molecule at a specific site.
allosteric activation
occurs when an “activator” binds with the enzyme and increases its turnover rate
allosteric inhibition
occurs when an end product binds to the regulatory enzyme and decreases its turnover rate and slows product formation
docosahexaenoic acid (DHA)
an omega-3 fatty acid. a primary structural component of the human brain, cerebral cortex, skin, and retina. can be synthesized from alpha-linolenic acid or obtained directly from maternal milk (breast milk), fish oil, or algae oil. fish sources: cooked salmon contain 500-1500 mg DHA and 300-1000 mg EPA per 100 grams. other sources: DHA include caviar (3400 mg per 100 grams), anchovies (1292 mg per 100 grams), mackerel (1195 mg per 100 grams), and cooked herring (1105 mg per 100 grams). brains from mammals are also a good direct source, with beef brain, for example, containing approximately 855 mg of DHA per 100 grams in a serving.
eicosapentaenoic acid (EPA)
an omega-3 fatty acid. obtained in the human diet by eating oily fish or fish oil, e.g. cod liver, herring, mackerel, salmon, menhaden and sardine, and various types of edible algae. also found in human breast milk. a precursor to docosahexaenoic acid (DHA). converted from ALA, but medical conditions like diabetes or certain allergies may significantly limit the human body’s capacity for metabolization of EPA from ALA.
beta oxidation
the catabolic process by which fatty acid molecules are broken down in the cytosol in prokaryotes and in the mitochondria in eukaryotes to generate acetyl-CoA, which enters the citric acid cycle, and NADH and FADH2, which are co-enzymes used in the electron transport chain. It is named as such because the beta carbon of the fatty acid undergoes oxidation to a carbonyl group.
calcium ATPase
Ca2+ ATPase (PMCA) is a transport protein in the plasma membrane of cells that serves to remove calcium (Ca2+) from the cell. it is vital for regulating the amount of Ca2+ within cells. uses hydrolysis of ATP.
combination training
cross-training to enhance recovery, because it is postulated that recovery relies primarily on aerobic mechanisms. several studies have demonstrated that recovery in power output is related to endurance fitness. bogdanis and colleagues reported relationships in power recovery in the first 10 seconds of a cycling sprint, the resynthesis of PCr, and endurance fitness (VO2Max).
glycogenolysis
breakdown of the molecule glycogen into glucose
inorganic phosphate
a chemical derivative of phosphoric acid. the phosphate ion is an inorganic chemical, the conjugate base that can form many different salts. inorganic phosphates occur naturally in many forms and are usually combined with other elements (e.g., metals such as sodium, potassium, calcium and aluminum). inorganic phosphates are present in all living organisms and are required to support life.
law of mass action
also known as mass action effect. concentrations of reactants – substances that start reactions – or products – substances that are produced – or both in solution will drive the direction of the reactions. (with enzyme-mediated reactions, such as the reactions of the phosphagen system, the rate of product formation is greatly influenced by the concentrations of the reactants)
metabolic acidosis
exercise induced decrease in ph – blood becomes more acidic, which inhibits glycolytic reactions, interferes with excitation-contraction coupling, and inhibits enzymatic turnover rate of cell energy systems
metabolic specificity
training that results in the use of a specific bioenergetic pathway
near-equilibrium reactions
reactions that proceed in a direction dictated by the concentrations of the reactants due to the law of mass action
nicotinamide adenine dinucleotide (NADH)
A cofactor that is central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH respectively. In metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The cofactor is, therefore, found in two forms in cells: NAD+ is an oxidizing agent - it accepts electrons from other molecules and becomes reduced. This reaction forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the main function of NAD. However, it is also used in other cellular processes, most notably a substrate of enzymes that add or remove chemical groups from proteins, in posttranslational modifications. In organisms, NAD can be synthesized from simple building-blocks (de novo) from the amino acids tryptophan or aspartic acid. In an alternative fashion, more complex components of the coenzymes are taken up from food as niacin. Similar compounds are released by reactions that break down the structure of NAD. These preformed components then pass through a salvage pathway that recycles them back into the active form. Some NAD is converted into the coenzyme nicotinamide adenine dinucleotide phosphate (NADP). The chemistry of NADP is similar to that of NAD, but it has different role, being predominantly a cofactor in anabolic metabolism. NAD+ is written with a superscript plus (+) sign because of the formal charge on one of its nitrogen atoms; however, it is actually predominantly a singly charged anion (charge of minus 1) at physiological pH. NADH, on the other hand, is a doubly charged anion because of its two bridging phosphate groups.
oxidative phosphorylation
the process in which ATP is formed as a result of the transfer of electrons from NADH or FADH2 to O2 by a series of electron carriers. This process, which takes place in mitochondria, is the major source of ATP in aerobic organisms
rate-limiting step
the mechanism step with the greatest activation energy and therefore the slowest step in a chemical reaction, which is therefore the rate at which the reaction is determined. phosphofructokinase is the most important regulator of glycolysis because it is the rate-limiting step.
repletion
the restoration of energy substrates, such as phosphagen and glycogen
sodium-potassium ATPase
also abbreviated Na⁺/K⁺-ATPase, an enzyme that uses ATP molecules to pump sodium and potassium ions via hydrolysis. a similar enzyme is calcium ATPase.
slow glycolysis
when pyruvate is shuttled into the mitochondria to undergo the krebs cycle (cycle of reactions to produce energy); slower resynthesis rate due to the number of reactions, but this can be kept up for longer durations if the exercise is low enough
hormone vs enzyme
The enzyme is a catalyst which enhances the rate of reaction in the body whereas hormones are chemical messenger which provides the signal to the cell for performing various functions. Secondly, enzymes act on the site where they are produced while hormones act distantly from the cell where they are produced and travel through body fluid.
allosteric
relating to or denoting the alteration of the activity of a protein through the binding of an effector molecule at a specific site
allosteric binding site
a site at which substances other than hormones can enhance or reduce the cellular response to the primary hormone. it’s binding an enzyme at a site other than the active site; allows molecules to either activate or inhibit, or turn off, enzyme activity – by binding these molecules change the confirmation, or shape, of the enzyme
cross-reactivity
when a given receptor partially interacts with other hormones (i.e., allosteric binding or blocking of the primary binding site)
proteolytic enzyme
enzymes that break down proteins into shorter fragments (peptides) and eventually into their components, amino acids; also called protease, proteinase, or peptidase. cortisol increases the level of these. proteolysis occurs by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. proteases are involved in many biological functions, including digestion of eaten proteins, protein catabolism (breakdown of old proteins), and cell signalling. one example is enzymes that use glutamate carboxylic acid for proteolysis.
anaerobic alactic system
the part of the anaerobic energy system that makes energy anaerobically without lactate. also known as the phosphagen or creatine phosphate system. the anaerobic lactic system makes energy through glycolysis and is known as the glycolytic system.
hyaline cartilage
articular cartilage found on the articulating surfaces of bones; glass-like (hyaline) but translucent; found on many joint surfaces. it is also most commonly found in the ribs, nose, larynx, and trachea. firm, has a considerable amount of collagen.
fibrous cartilage
very tough form of cartilage found in the intervertebral disks of the spine and at the junctions where tendons attach to bone. the only type of cartilage that contains Type I collagen in addition to the normal type II.
tendon
fibrous connective tissue which attaches muscle to bone, tendons may also attach muscles to structures such as the eyeball. a tendon serves to move the bone or structure
ligament
fibrous connective tissue which attaches bone to bone, and usually serves to hold structures together and keep them stable.
function of ligaments vs tendons?
Ligaments appear as crisscross bands that attach bone to bone and help stabilize joints. For example, the anterior cruciate ligament (ACL) attaches the thighbone to the shinbone, stabilizing the knee joint. Tendons, located at each end of a muscle, attach muscle to bone. Tendons are found throughout the body, from the head and neck all the way down to the feet. The Achilles tendon is the largest tendon in the body. It attaches the calf muscle to the heel bone. The rotator cuff tendons help your shoulder rotate forward and backward. You can think of ligaments as rope, with a series of tough, intertwined cords that bind bones. Ligaments also have some elastic fibers that allow the joint to move, but not so much that it moves beyond its capacity. The knee joint, for instance, has four major ligaments, one on each side of the knee and two that run diagonally across the front and back of the kneecap. These ligaments help stabilize the knee and keep it from moving too far to the left or right, forward or backward. Tendons are also tough cords, but they have a little more give than ligaments. As a muscle contracts, the attached tendon pulls the bone into movement. Think of what happens to your bicep when you bend your elbow. Tendons also help absorb some of the impact muscles take as they spring into action.
