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59 Cards in this Set

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edema definition and proteins responsible
Blood proteins, such as albumins, globulins, platelets and red and white cells, are much too large to escape the blood through the pores in the capillaries. Of course, water moves through the pores easily. The force that pushes the water through the pores and into the spaces around cells (interstitial space) is called "hydrostatic pressure", the pressure exerted by the pumping action of the heart. The force that pulls water from the interstitial spaces and back into the capillaries are these same big proteins in blood. Since they are too big to pass through the pores in the capillaries, they become very concentrated at the end of the capillaries, and act as magnets drawing water back into the vessel. This action of pulling water back into the capillary is called "oncotic pressure". The important concept to remember is that the amount of water (fluid) leaving the capillary is equal to the amount of water (fluid) entering the capillary. This is one mechanism the body has for maintaining fluid balance, and it is due to a plentiful supply of blood proteins. The picture of edema above demonstrates how low blood proteins would allow fluid to accumulate in the extremities where hydrostatic pressure pushes fluid out and there are not enough proteins (oncotic pressure) to pull the fluid back in.
building blocks of proteins
Proteins are very large molecules made from an "alphabet" of about 20 different amino acids. We obtain these amino acids from food protein in our diet, and we make some of them in the cell as needed. Amino acids that we can't synthesize in the cell in sufficient amounts are known as essential or indispensable amino acids. There are 9 of them. The remaining 11 are known as nonessential or dispensable amino acids.

Like carbohydrates and lipids, amino acids are constructed from atoms of carbon, hydrogen, and oxygen. Unlike the other two fuels, amino acids contain nitrogen. There is a basic structure common to all amino acids, an amine group. This nitrogen component makes proteins unique.



Other amino acid structures are a central carbon , -C- , an acid group (COOH), and a "side chain", sometimes designated as "R". This side-chain is considered the functional group.

There are 20 different side chains, which accounts for the 20 different kinds of amino acids. These 20 amino acids have distinctive structural and chemical properties.
nitrogen makes proteins different from fat and carbs
Deamination is the removal of the amino group (NH2) from the amino acid leaving the carbon, hydrogen, and oxygen components to be converted to things like glucose or fatty acids. Of course, the skeletons can be recycled and made into new nonessential amino acids with modification of the skeleton and replacement of the nitrogen group. This process is often referred to as transamination. The point is that moving the amine group is unique to proteins (amino acids) and how our bodies handle them. By the way, you will learn in the next module that it takes vitamin B6 to move those nitrogen groups for transamination or deamination!
meaning of essential when speaking of amino acids and main characteristic of foods that would allow you suspect they are a complete protein
We are living protein. Proteins are very large molecules made from an "alphabet" of about 20 different amino acids. We obtain these amino acids from food protein in our diet, and we make some of them in the cell as needed. Amino acids that we can't synthesize in the cell in sufficient amounts are known as essential or indispensable amino acids. There are 9 of them. The remaining 11 are known as nonessential or dispensable amino acids.

Foods derived from animal products such as milk, cheese, meat, poultry, seafood and eggs contain plenty of the 9 essential amino acids. Foods derived from plant products such as grains, legumes and vegetables are missing one or more of the essential amino acids. Of all the plant foods, soybeans appear to be the best protein source. This has lead to the classification of food proteins according to quality. If a food contains all 9 essential amino acids in a pattern similar to the pattern of amino acids in humans, the protein is designated high quality and is considered a complete protein. If a food is deficient in one or more essential amino acids, the pattern is unlike the pattern of amino acids in humans and is designated poor quality (incomplete protein). As we mentioned before, we call the deficient amino acid the "limiting amino acid".
ourse of action in body if do not consume all essentials
The protein will not be made. This is an especially serious situation if the owner of the cell is a child. When protein can't be made, the child may stop growing. This is a form of undernutrition. There is an important principle to be learned here; the all-or-none principle, either all essential amino acids must be available at the time of protein synthesis or none can be used.

Lets use an example similar to that mentioned in the text. Suppose you have been asked to make two signs saying ALABAMA. In order to make these signs you need 8 A's, 2 L's, 2 B's, and 2 M's. But in your supply of letters you come up one A short.
how is nitrogen excreted when we use protein carbon skeleton
But what about that nitrogen (NH3) in the liver from deamination? The liver converts the toxic ammonia to urea through a cycle known as the urea cycle.



Urea is the waste product of protein metabolism. It leaves the liver and is transported to the kidneys by way of the blood. The kidneys filter it out of the blood.

Urea becomes urine. Then to bathroom
calorie content of protein
High
absorption of amino acids
The free amino acids are absorbed into the blood in the villus, and directed to the portal vein, which empties into the liver.
define petitde bond
"Snapping into place" is the formation of a chemical bond between two adjacent amino acids that holds the protein together. These are called peptide bonds. Peptide bonds are only found between amino acids.



Hundreds of amino acids form a long chain with a very particular order of amino acids that makes up the primary structure of protein, the polypeptide
denaturation definition such as that when we cook an egg
The biological activity of protein can be irreversibly destroyed by all kinds of treatment. Acids such as the hydrochloric acid (HCl) in the stomach, alkaline substances such as ammonia, heat and metals are very destructive of protein. The process of destroying protein structure, denaturation, disrupts the organization of the protein, except the polypeptide chain is left intact, but the protein is no longer functional. This means that the fancy folding that took place during synthesis is ruined. All that is left is the string of amino acids.
examples of positive and negative protein balance
Protein balance is where we compare the protein intake to the protein output of our body. A positive balance indicates we are taking in more protein then we are losing. This must mean our body is growing, changing or healing in some way to keep the extra protein. When we experience positive protein balance, there is a net synthesis in body protein. This occurs during growth, pregnancy, and recovery from illness. A mature athlete in training may be producing more muscle tissue, so there is a net gain in protein, but there won't be an increase in height. Hormones such as insulin, growth hormone and testosterone are associated with protein synthesis.



Negative protein balance indicates you are losing more protein than you have consumed and inidicats some wort of breakdown process in the body. Negative protein balance occurs under a number of different circumstances. It occurs when protein intake is not adequate to meet needs for body protein synthesis. When energy intake is not adequate to meet the body's need for fuel, amino acids from dietary protein and body protein are deaminated and the carbon skeletons used to generate ATP. In such situations, the amino acids can't be used for growth, maintenance or repair. Serious injuries, infections and surgery means protein in the body is breaking down faster than it is being rebuilt. A deficiency of one or more amino acids slows down or stops protein synthesis. And, certain hormones such as the thyroid hormone and cortisol promote the breakdown of protein. Anorexia, cancer wasting and other forms of malnutrition are good examples of negative protein balance. This means we consume fewer proteins than we breakdown.
examples of positive and negative protein balance
Protein balance is where we compare the protein intake to the protein output of our body. A positive balance indicates we are taking in more protein then we are losing. This must mean our body is growing, changing or healing in some way to keep the extra protein. When we experience positive protein balance, there is a net synthesis in body protein. This occurs during growth, pregnancy, and recovery from illness. A mature athlete in training may be producing more muscle tissue, so there is a net gain in protein, but there won't be an increase in height. Hormones such as insulin, growth hormone and testosterone are associated with protein synthesis.



Negative protein balance indicates you are losing more protein than you have consumed and inidicats some wort of breakdown process in the body. Negative protein balance occurs under a number of different circumstances. It occurs when protein intake is not adequate to meet needs for body protein synthesis. When energy intake is not adequate to meet the body's need for fuel, amino acids from dietary protein and body protein are deaminated and the carbon skeletons used to generate ATP. In such situations, the amino acids can't be used for growth, maintenance or repair. Serious injuries, infections and surgery means protein in the body is breaking down faster than it is being rebuilt. A deficiency of one or more amino acids slows down or stops protein synthesis. And, certain hormones such as the thyroid hormone and cortisol promote the breakdown of protein. Anorexia, cancer wasting and other forms of malnutrition are good examples of negative protein balance. This means we consume fewer proteins than we breakdown.
RDA for prtoein and application to a person
The RDA for protein (found on the inside front cover of your text) is based on a reference adult. Protein is the only macronutrient with an RDA. A "reference adult" is an "average" American. It is better to determine your own RDA based on the formula in the above paragraph where you find your kilograms of body weight (pounds divded by 2.2), then mulitply by 0.8 for the grams of protein you need per day. It may help you tranlate this to food by knowing that one ounce of meat usually has about 7 grams of protein and 8 ounces of milk usually has about 8 grams of protein.
RDA for prtoein and application to a person
The RDA for protein (found on the inside front cover of your text) is based on a reference adult. Protein is the only macronutrient with an RDA. A "reference adult" is an "average" American. It is better to determine your own RDA based on the formula in the above paragraph where you find your kilograms of body weight (pounds divded by 2.2), then mulitply by 0.8 for the grams of protein you need per day. It may help you tranlate this to food by knowing that one ounce of meat usually has about 7 grams of protein and 8 ounces of milk usually has about 8 grams of protein.
known harm of high protein diets
Typically, Americans consume much more protein than necessary to meet our needs. The excess intake is probably not a major health risk, unless the person has liver or kidney disease. In this case, the extra need for urea production and waste puts a strain on liver and kidney function. Another problem associated with a high protein intake is that it takes extra fluid (water) to metabolize the protein and flush away the additional urea. And finally, our favorite high-protein foods are almost always high (saturated) fat foods, contributing unneeded kcals to the diet and increasing the risk for heart disease and some cancers.
known harm of high protein diets
Typically, Americans consume much more protein than necessary to meet our needs. The excess intake is probably not a major health risk, unless the person has liver or kidney disease. In this case, the extra need for urea production and waste puts a strain on liver and kidney function. Another problem associated with a high protein intake is that it takes extra fluid (water) to metabolize the protein and flush away the additional urea. And finally, our favorite high-protein foods are almost always high (saturated) fat foods, contributing unneeded kcals to the diet and increasing the risk for heart disease and some cancers.
Vitamin A

physiological function
deficiency diseases
The best known function of vitamin A is in maintaining vision.

You will more likely see vitamin A deficiency in the Third World where there are millions of children who have lost their eye sight due to a lack of vitamin A. In fact the leading cause of blindness among children in 3rd world countries is a lack of dietary fat or the vitamin.

The production of mucus is another special function of vitamin A. Mucus is the thick substance that lubricates and protects tissues and organs. Mucus production is especially important in the eye, as it keeps the membranes moist. A vitamin A deficiency decreases mucus production so that the eye dries out, thus providing an excellent site for infections by invading bacteria. This drying of the eye is called xerophthalmia.



If untreated, xerophthalmia eventually leads to blindness. (Usually the child dies not long after blindness occurs because of so many other infections.)

Vitamin A is also required for normal growth of epithelial tissues (eyes, skin, respiratory tract, digestive tract, urogenital tract). Like the cells in the eye, many of these cells are capable of secreting mucus so that the underlying cells are kept moist and flexible. With a vitamin A deficiency, mucus production decreases and the cells begin to dry out creating a situation where microorganisms invade and cause infections, just as it occurred in the eye.

Vitamin A also maintains a healthy immune system by maintaining the specialized cells associated with immunity. Vitamin A has been known for years as the anti-infection vitamin. It promotes resistance to bacterial infections.

In order for a child to grow, vitamin A plays a role in producing the normal components of bone. Getting taller and stronger is due to the interactions of many nutrients, but vitamin A is certainly one of the key players. Caution has to be taken here because too much vitamin A can also cause problems with the bones and cause bone pain.

Vitamin A is responsible for the events that produces a normal embryo/fetus. Throughout the various stages of growth and development from the embryo forward, vitamin A plays a significant role. Vitamin A is needed for normal reproduction. This FUNDAMENTAL function of vitamin A is cell differentiation. Differentiation means that the cells mature to be a certain type of cell so a cell may differentiate into a brain cell or heart cell or some other cell. Some forms of the vitamin function by turning on and off the genetic code (gene expression). The code is responsible for producing a variety of proteins. The formation of epithelial tissue, immunity, mucus production, overall growth and development, and fetal growth all are under the influence of vitamin A. Again, this is a fine balance, if a woman gets too much vitamin A while she is pregnant, it can produce birth defects.

You might realize that too much vitamin A causes birth defects becasue when women take Accutane, they are educated closely about the potential for birth defects. Most physicians will also ensure the woman is on birth control pills as well to prevent this disastrous outcome.

Becasue vitamin A has such a strong influence on the nucleus of a cell (genes), it is considered a hormone. Like many other hormones, there are receptors for vitamin A and there are transport proteins to chaperone vitamin A throughout the body.
Vitamin D

physiological function
deficiency diseases
Calcitriol regulates the absorption of the minerals calcium and phosphorus from the intestinal tract.


Along with the parathyroid hormone (PTH), it regulates the amount of calcium in the blood.


It controls how much calcium is excreted from the kidney.


Indirectly, it regulates the amount of calcium deposited in the bones.

Until the discovery of vitamin D, rickets and osteomalacia were common in areas of the northernmost latitudes, where there is little sun, and the air is heavily polluted. Rickets is a disease of children brought on by a lack of sunshine OR a lack of vitamin D in the diet. Rickets is characterized by misshapen bones, especially of the legs and pelvis, because the bones didn't have enough calcium to calcify normally. The picture of the boy was taken in Glasgow early in the last century, before the discovery of vitamin D. Oddly enough, we are seeing a resurgence of rickets in the southern states of the US where it is thought that limited time outside and physical inactivity are heavy contributors.
At birth, bones are soft and bend easily because the bone is mostly protein. As the infant matures, calcium (and other minerals) get deposited into the protein making it strong and hard or mineralized, IF there is enough vitamin D to get the job done.

Same scenario happens with teeth. If there is a vitamin D deficiency, the dentin and enamel in the teeth don't form normally.
Folate

physiological function
deficiency diseases
. It is absolutely essential for the synthesis of RNA and DNA, and thus to cell division and growth. It plays significant roles in amino acid metabolism; especially in the synthesis of the essential amino acid methionine from homocysteine. Vitamins B6 and B12 also participate in this particular reaction.
Vitamin K

physiological function
deficiency diseases
Vitamin K is critical for the blood to clot normally. In fact, there are 3 nutrients that participate in blood clotting: protein, calcium and vitamin K.





Blood clotting is an extremely complicated process that is not fully understood, but besides protein, calcium, and vitamin K, other factors are required to make it work, including the blood component, platelets.

Vitamin K also plays an important role in bone formation. The vitamin produces a special protein that allows the framework of the bone to be produced. Vitamin K also increases the calcium-binding potential of some organs such as liver, kidney and blood plasma.

Vitamin K deficiency is extremely rare. In order to produce a deficiency, the person would have to be taking antibiotics, stop eating, and not have any stores of the vitamin. Impaired fat absorption could also cause a deficiency. Prior to surgery, the physician will test a patient's blood to see how long it takes for blood to clot. If blood clotting time is slow, the surgery will be more risky.

Obviously a deficiency of vitamin K causes bleeding and bone problems.
Vitamin E

physiological function
deficiency diseases
The function of vitamin E is to protect cell membranes, DNA, and other electron dense areas in the cell from free radical damage. And, it prevents the propagation of free radicals. By donating electrons to electron-seeking compounds (oxidizing agents) antioxidants protect other molecules or parts of the cell from attack. In the process of protecting the cell membrane from oxidative damage, vitamin E gets oxidized itself. In order to rejuvenate vitamin E, another vitamin, vitamin C, comes to the rescue.


About the only documented example of vitamin E deficiency in humans is one that occurs in premature infants. Most of the vitamin E that an infant is born with is delivered by the mother to the fetus during the last few weeks before birth. When an infant is born prematurely, s/he has little vitamin E on board. As you can imagine, the infant is not well-protected from oxidation and the target of this action is the unsaturated fatty acids in the red blood cell membranes. Without protection from free radicals, the red blood cell membranes break apart and the contents of the cell spills out into the surrounding plasma (the fluid part of blood). The disease is called hemolytic anemia. Treatment is a formula with plenty of vitamin E to protect from the free radicals.
Thaimin

physiological function
deficiency diseases
Thiamin, in its coenzyme form , removes carbons from intermediates of energy metabolism to form carbon dioxide, which is exhaled into the air.


The classical thiamin deficiency is beri beri which translates to "I can't, I can't". Thiamin deficiency keeps us from making and having energy!
Niacin

physiological function
deficiency diseases
Niacin in coenzyme form is a hydrogen carrier that participates in hundreds of metabolic reactions in the cell. Like other B-vitamins, it is involved in all reactions transforming food energy to ATP.


Early in the 20th century, pellagra existed in the United States in epidemic proportions. It was known as the disease of the 4 D's: dermatitis, diarrhea, dementia, and eventually death. Mental hospitals were overflowing with crazy, demented pellagrans, costing taxpayers a lot of $$$.
Vitamin B6

physiological function
deficiency diseases
It can remove NH2 (amino) groups from amino acids

and it can add amino groups back to carbon skeletons to make amino acids.

A vitamin B6 deficiency due to inadequate dietary intake is extremely rare. There are a wide variety of symptoms include anemia, nausea, vomiting, depression, decreased immune function, and epileptic-like seizures, and many more.

Who might be deficient? Alcoholics and patients taking medication that interfere with the action of vitamin B6 are about the only candidates for deficiency.
Vitamin B12

physiological function
deficiency diseases
The function of vitamin B12 is to control folate metabolism. Folate is inactivated by getting trapped by a methyl group (CH3) in what is known as a "methyl trap".



Vitamin B12 reactivates the folate by releasing it from its methyl trap.
Riboflavin

physiological function'
Riboflavin in its coenzyme form participates in several steps in the transformation of energy fuels to ATP; specifically it is a hydrogen carrier.

Not only is it active in the Krebs cycle and the electron transport chain, but it is part of a large number of other coenzymes.
Vitamin C

Function
Deficiency
While vitamin C is a water-soluble vitamin, it does not function as a coenzyme. One of its major functions is to promote the synthesis of collagen, a protein that is found in connective tissues, bones, teeth, tendons, and blood vessels. Collagen is the "glue" that holds us together.

A vitamin C deficiency can occur in just 20 days and a person becomes "unglued"; the blood vessels tend to fall apart and blood begins leaking through the capillaries into surrounding tissue. A person with scurvy can bleed to death internally. Death comes quickly

Vitamin C is also is an important water-soluble antioxidant. It protects cells and cellular components from free radical attack! And it rejuvenates the oxidized (inactive) vitamin E, another powerful antioxidant. Vitamin C seems to be important in preventing certain cancers caused by nitrosamines: cancers of the stomach, esophagus, and mouth. Vitamin C is an important scavenger for free radicals.



Vitamin C aids in the body's ability to absorb dietary iron. Vitamin C keeps the immune system functioning. And much, much more.

A dietary lack of vitamin C inhibits wound healing, probably because scar tissue depends on the formation of collagen.
poor regulation of vitamin and mineral (and other dietary) supplements by the FDA
Lots of money to government
why is vitamin D unique compared to other vitamins
Most toxic of Vitamins since we cannot get rid of Vitamin D. In addition, it needs to be modified before it is able to be used
B vitamins are generally co-enzymes
Vitamin B6 in coenzyme form participates in almost all metabolic reactions involving amino acids. You might remember it from the metabolism animation as .



It can remove NH2 (amino) groups from amino acids

and it can add amino groups back to carbon skeletons to make amino acids.



Similarly, it can also remove the sulfur groups and carboxyl (COOH) groups from amino acids. Just about any reaction involving amino acids is going to require the participation of vitamin B6 . For example, when one is consuming a high protein diet, a lot of vitamin B6 is needed to dispose of extra NH2 as urea in the urine.

Another important task for vitamin B6 is to keep the body supplied with glucose when we are fasting or starving, or when we are engaged in strenuous exercise. (Gluconeogenesis is discussed in module 6!)

And, vitamin B6 puts the iron in hemoglobin.

Perhaps one of the most interesting functions of this vitamin is its role in the formation of neurotransmitters in the brain. These chemical regulators control appetite, sleep, and mood along with many other things. A severe vitamin B6 deficiency in infants leads to convulsions.
good sources of B12
Fortified cereals and all animal foods are sources of vitamin B12. If someone is taking large quantities of folate in pill form, the folate can clear up the overt symptoms of pernicious anemia, without revealing the underlying cause of the disease, a B12 deficiency. Pernicious anemia causes nerve death, and, if not diagnosed and treated in time can lead to permanent nerve damage or death. It is important that B12 deficiency be identified and corrected in a timely fashion.
disclaimer of a structure function claim relative to the FDA
Eh?
know anti-oxidant nutrients
There are any number of environmental and internal factors that damage living tissues through oxidation. Externally, cigarette smoke is one, internally x-rays are another. For protection from free radicals, the body has a defense arsenal of antioxidants ready for combat.



Some of these antioxidants are vitamins, some are minerals, and some are special molecules synthesized by cells themselves. An antioxidant is able to satisfy the unpaired electron of an oxidizing agent so that the oxidizing agent is no longer seeking to damage other molecules.

Vitamin E is a good example in the defense against free radicals within cell membranes, so we call it an anti-oxidant. It works by donating electrons to electron seeking compounds such as the electron-seeking free radicals. This keeps the free radicals from looking for electrons from other substances such as the fatty acids in the cell membrane or the DNA. Vitamin E and other anti-oxidants are protective to our tissues.



Why the big deal about free radicals? Free radicals cause oxidation and oxidation is the initiation phase of cancers.
Control of water in compartments of body by ions and which are intra and extracelular
Na is both intra and extra
K intra
Cl is both
evaporation as part of the heat regulation system
An exercising muscle produces heat, heat from exercise is transferred to the environment mostly through the skin as sweat. Through evaporation of water, some heat is removed from the body. Of course, on a cool day, we also transfer heat by convection, conduction and radiation. In hot and humid weather, evaporation is the critical heat loss pathway. To cool the body, perspiration must evaporate. If the sweat is visible on the body or it soaks into the clothes, it is not cooling.
water needs as related to energy needs of the diet
Recommended Intake: 1 ml per 1 Calorie Expended
classification of minerals to major and trace
They are divided into 2 categories: major and trace. The division is somewhat arbitrary, but if the body requires more than 100 milligrams (1/5 of a teaspoon) per day it is considered a major mineral; otherwise, it is a trace mineral. There are undoubtedly other minerals that are essential, but their function and requirements have yet to be established.
where is calcium in the body
Almost all (99%) of the calcium in the body is located in bones and teeth.
mineral bioavailability from plant vs animal products
The ability to capture minerals from foods and absorb them is known as bioavailability. A food may be very high in iron, but if the iron can't be absorbed because it is bound to a natural plant component, such as oxalic acid, it's not going to do the body much good. Such is the case with spinach, where very little iron gets into the body because the oxalic acid is chemically bound to the iron and the two can't be separated during digestion. The iron in spinach has very low bioavailability. Most minerals in animal foods are very bioavailable because animal products do not contain binders such as oxalic acid and phytic acid (a natural component of fibers). Obviously this means that plant sources tend to be less bioavailable. Here are some typical examples using calcium.
iron regulation in body via absorption and meats as best-absorbed sources
Iron is unique among nutrients in that it does not have an exit route from the body, other than from dying skin cells. The sloughing off of skin eliminates a little iron from the body every day. Therefore, the body has evolved a substantial system for blocking iron absorption. Most adults probably can't absorb more than 15% of dietary iron.

Iron enters the body on a carrier called transferrin.


When the transferrin carrier is full, the rest of the dietary iron is loaded into short term storage in intestinal cells. The short term storage is ferritin, which holds the iron until an empty transferrin carrier can return to the intestine to pick it up. Iron is stored principally in the liver, spleen, and bone marrow, and when iron stores are full the iron-binding sites on transferrin will be full. As a consequence, iron transfer from intestinal cells to the blood transferrin is inhibited.




The iron-containing ferritin in the intestinal cells is excreted in the feces when intestinal cells die and are sloughed off.
Sometimes this is referred to as the "mucosal block" because it keeps us from absorbing too much iron!

Iron in food can exist in three different forms. Heme iron is the form found in the animal proteins hemoglobin and myoglobin. It is found only in animal tissues and is the most absorbable form of iron. About 40% of the iron in meat and other animal products is heme iron. The remainder of iron in meat and animal products is called nonheme iron. Nonheme iron is the iron form found in plant foods (and some in other animal tissues). Nonheme iron is not very well absorbed. The third type of iron is elemental iron, the iron derived from foods cooked in cast iron cookware and supplements.
Ethanol
By now in this course, it shouldn't surprise you that we want you to see that alcohol is an organic chemical with the formula C2H5OH. Ethanol, the alcohol in beverages, is found in wine, beer, mixed drinks, or distilled spirits. These are examples of the alcohol content of various drinks. They do not always represent a "serving" of alcohol.
kcal content of alcohol
Alcohol provides 7 kcals/gram but it is not considered a nutrient because our body does not require it for function and it does not perform any structural role for the body.
first organ to be exposed to alcohol with absorption
Liver
chief site of alcohol metabolism
Liver
first area of absorption
Alcohol is such a small molecule (two carbons long) that it does not require digestion, so it can be absorbed by simple diffusion throughout the gastrointestinal tract. About 20% of the alcohol is absorbed through the stomach walls. The small intestine is a rapid absorption area so if you want to slow down the absorption of alcohol, you have to slow it down in getting to the small intestine. Obviously, consuming alcohol more slowly will slow down absorption and eating foods that will slowly empty from the stomach will slow down absorption. Slowing down the absorption is why many folks don't want to drink on an empty stomach.
male vs female metabolism of alcohol
Women can produce enough ADH in the stomach to metabolize only 10% of the alcohol consumed. Thus, women develop alcohol-related health problems more rapidly then men do with the same alcohol consumption habits
alcohol dehydrogenase
The oxidation (metabolism) of alcohol involves 2 important enzyme systems.

alcohol dehydrogenase (ADH). (Don't confuse these initials with the ADH from the brain, the Anti-Diuretic Hormone. )
The ability to synthesize the enzyme ADH is the key to alcohol metabolism. ADH is produced by cells that line the stomach, so that a person absorbs less alcohol than consumed. However, there is a difference in the amount of ADH produced. Me are able to produce enough ADH in the stomach to metabolize about 30% of the alcohol they have consumed. Women can produce enough ADH in the stomach to metabolize only 10% of the alcohol consumed. Thus, women develop alcohol-related health problems more rapidly then men do with the same alcohol consumption habits. Certain drugs, such as those used to treat ulcers and heartburn, inhibit ADH activity. Aging and alcohol abuse also decrease ADH production in the stomach.

Keep in mind that majority of the alcohol gets absorbed as alcohol so the liver is the chief site for alcohol metabolism. The liver produces the most ADH.
guidelines for consuming alcohol in moderation for men and women
No more than one drink for women, 2 drinks for men.
name for scarring and fatty infiltration of the liver caused by alcohol overuse
The liver normally metabolizes fatty acids as its preferred fuel. However, alcohol must be oxidized before any other fuel, forcing the liver to convert more and more fatty acids into triglycerides. This eventually leads to a buildup of fat in liver tissue. Liver cells begin to die when niacin is used up processing (metabolizing) alcohol. These dead cells form scar tissue, which in turn causes fibrosis.

Liver tissues have a remarkable ability to regenerate themselves, but only if the owner of the liver avoids alcohol and has a good diet. Otherwise, the fibrosis advances to cirrhosis.

Cirrhosis is a progressive disease of the liver characterized by enlargement and diffuse damage and scarring that chokes off the blood supply to much of the liver. Without oxygen and nutrients, the liver begins to die. The overt symptoms are jaundice (the whites of the eyes and skin turn yellow), high blood pressure in the portal vein (nutrients from the digestive tract have trouble getting into the liver), ascites (fluid produced by the liver accumulates in the abdomen) , and finally liver failure. Most of the deaths from alcohol cirrhosis occur in people of middle age. Cirrhosis develops in about 12 to 35% of cases of alcoholism. And again, genetic factors determine the risk for the disease.
risks of alcohol consumption with pregnancy
The results: fetal alcohol syndrome (FAS), the most preventable birth defect in the United States.

The symptoms of FAS include mental and physical retardation, abnormalities of the face and skull and small size. There is no treatment for the condition and the newborn is damaged for life.
phytonutrients in red wine
The phenols in wine may help to protect against heart disease by acting as antioxidant nutrients decreasing LDL (bad) cholesterol or they may increase the HDL (good) cholesterol levels in the blood. We have talked about phytochemicals in the course and these phenols are just another fine example.
Define basal metabolism and factors associated with increased
Basal metabolism is defined as the minimum amount of energy expenditure needed to maintain the involuntary (vital) activities of life.

Question: What kind of functions are involuntary?

To measure the basal metabolic rate (BMR), oxygen uptake is determined in a fasting individual at physiological and psychological rest. The subject is in a warm room, early in the morning, resting quietly. The person is relaxed and awake.

It is easier to determine resting metabolic rate (RMR) because the measurement can be taken any time of the day with only a 3 to 4 hour fast, rather than overnight. The difference in the two measurements is about 10%.

The amount of energy required for BMR depends largely on lean body mass.
thermic effect of food and approximate use of overall energy
It "costs" energy to digest, absorb, and metabolize food. About an hour after eating, thermogenesis reaches its maximum. It accounts for about 5 to 10% of total energy expenditure. When we are trying to predict a person's energy needs, it is very easy to use 10% for the thermic effect of food (TEF).
direct and indirect calorimetry
A human calorimeter is an example of direct calorimetry. Its an air-tight chamber with an oxygen supply, allowing an individual to live and work in a tightly controlled environment. Heat produced and radiated by that individual can be measured, and by applying the definition of a "calorie", the energy expenditure is determined. There are only a limited number of human calorimeters available because they are impractical to use, and they are very expensive to maintain and operate.



Indirect calorimetry is easy to use. Energy expenditure is measured by oxygen utilization.
define body mass index
Body Mass Index is calculated by:

Dividing body weight (in kilograms) by height in meters squared

Or

Weight in pounds divided by height in inches squared times 703.1
methods of estimating body fat and accuracy
Skinfold thickness

Underwater weighing

Bioelectrical impedance assessment (BIA) is yet another established technique to measure total body fat. A very low energy current of electricity is passed through the body from electrode to electrode (patches on one hand and same side foot). It is based on the premise that fat tissue resists the electrical flow, lean tissues (lots of water and electrolytes) promote electrical flow.

Near Infrared Assessment (NIR)

Another method for measuring body fat is to employ short wavelengths of infrared light delivered to the biceps in the arm or other body sites. In theory, the amount of fat can be estimated by the refraction (or bending) of the light waves. The device is very small and portable but the research shows there is no predictable relationship of the NIR prediction with underwater weighing or DXA predictions.
android obesity and diseases associated
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major goals of weight loss programs and rate of weight loss
The key to successful weight control is exercise. By controlling energy intake and expending an extra 200 to 300 kcals per day, it is possible to achieve a weight loss of half a pound of fat per week.
interpretation of BMIs and categories
BMI 19-25 is considered appropriate for optimal health.

With BMI over 25 , weight-related health risks begin: signifies overweight

With BMI exceeding 30, greater health risks: signifies obesity

BMI over 40 signifies severe obesity. May qualify subject for gastroplasty