FCS 361 - Exam 2 Study Guide

LIPIDS: METABOLISM IN THE TISSUES

 Describe the role of the liver, muscle, and adipose tissue in lipid metabolism and storage.

- Muscle: free FA from VLDL and hydrolyzed DAGs are oxidized for energy

o Endurance- trained muscles contain TAGs deposits

- Adipose Tissue: absorbed FA used to synthesize TAG for storage

o Absorb TAG and cholesterol from chylomicrons through LPL

o Constant re-esterification to form TAGs

o Net effect determines level of circulating FA and extent of adiposity

- Liver: hepatic synthesis of bile salts

o Synthesis of lipoproteins which endogenous lipids and apolipoproteins

o Synthesis of new lipids from non-lipid precursors (glucose and AA)

o Catabolize dietary lipids from chylomicron remnants and LDL and repackage

into HDL and VLDL

o Hepatic TAG production is accelerated when diet is rich in CHO

 Differentiate metabolism and storage of lipids in the muscle and liver in fasting and

feasting states.

- Postprandial

o Liver: glucose, AA, medium-chain FA concentrations rise in portal blood and

go directly to liver

 Glucose taken up by hepatocytes

  Excess glucose not needed for energy or glycogenesis is converted to

FA

o Adipose Tissue: adipocytes favor TAG synthesis from glucose

 Insulin accelerates entry of glucose into adipose tissues

 Increases availability of FA uptake by adipocytes via LPL

 Free glycerol returned to blood

- Fasting

o Blood glucose decreases, insulin concentration falls, lower inhibition of LPL=

increased lipolytic activity

o Accelerated lipolytic activity in adipose tissue

o Free FA and glycerol produced

 Major precursors for synthesis of endogenous VLDL triacylglycerol

 Free FA circulate in albumin are taken up by liver or muscle cells and

oxidized for energy by acetyl-CoA formation

 Some acetyl-CoA used to make ketones

o Diminished synthesis VLDL and HDL and release into circulation

o Glucose and FFA become major precursors for the synthesis of endogenous

VLDL TAG

 Atherosclerosis- symptoms, causes, steps of atherosclerosis, factors that increase risk

- Degenerative disease of vascular endothelium

- Immune system and lipid material (cholesterol and cholesterol esters)

o Cholesterol esters promote inflammatory process

 - Cytokines: protein products of monocytes and lymphocytes that mediate atherogenic

processes by attracting phagocytic cells

- Lipid hypothesis: dietary lipid intake can alter blood lipid levels, which initiate of

exacerbate atherogenesis

- Steps

o 1. Damage to arteries (caused by tobacco, LDL, diabetes, obesity, HTN)

o 2. Immune response: monocytes, T lymphocytes, cytokines attract macrophages

o 3. Lipids are (especially cholesterol and cholesterol esters) deposited in arteries

and oxidized

o 4. Macrophages engulf oxidized lipids (especially those oxidized apoB) to for

Foam Cells

o 5. Foam cells infiltrate the endothelium (muscle grows over the plaque)

o 6. The arteries become hardened due to mineralization

- Factors that increase risk

o High HDL

o Low HDL

o High saturated fat intake (increased LDL)

o Trans fat (increased LDL, decreased HDL)

o Dietary cholesterol has a minimal effect in most people

 Internal cholesterol synthesis can be regulated

o Linoleic acid lowers LDL

 Glycerol

o Where is it transported to?

 - It’s passively transported out of the adipocyte and into the bloodstream by AQP7

located in plasma membrane of adipocytes

- Passively transported into liver cells by AQP9 located in the plasma membrane of

hepatocytes

o What enzyme phosphorylates it?

- Glycerokinase (converts glycerol to glycerol phosphate)

o What is it used for?

- Can’t be metabolized by adipose tissue

- Used for energy by liver or other tissues with enzyme glycerokinase  glycolysis and

gluconeogenesis

 FA catabolism

o Describe the activation step. Where does it take place?

- Liver and Adipose tissue (intracellular TAG lipase)

o Activated by epinephrine, glucagon, etc.

o Hormone attaches to receptor on cell membrane

o cAMP phosphorylates (and activates) TAG Lipase

o Role of Carnitine Acyltransferase I and Carnitine Acyltransferase II

 Understand mechanism of Carnitine Transport system

 Carnitine acyl transferase (CAT) is the way to go in and out of carnitine

 Insulin regulation of fat and glucose metabolic rate in the skeletal muscle

 Beta Oxidation

- Beta oxidation is the breakdown of Fatty Acids and removal of 2 carbons at a time.

o Occurs in the mitochondria

- Fatty Acid synthesis is the formation of a Fatty Acid from acetyl-CoA (2C)

o Occur sin the cytosol

- Fatty acid can be elongated and desaturated to form derived lipids and eicosaonoids

- Lipid metabolism can be regulated by hormones, levels of lipids, and CHO intake

- Alcohol metabolism is similar to lipid metabolism

o Where does it occur?

- Mitochondria

o Describe in one sentence what is happening.

- Cyclic degradation with two-carbon units (acetyl co-A) from carboxyl end and then

acetyl Co-A will enter the TCA cycle for oxidation and will keep occurring until all

FA’s are completely broken down into acetyl-CoA units.

o Know enzymes, products, and substrates

- Acyl-CoA dehydrogenase

- Enoyl CoA hydratase

- Beta hydroxyacyl-CoA dehydrogenase

- Acyl-CoA acetyltransferase (thiolase)

- Yields FADH2, NADH, 4 ATP

- Products: acetyl CoA, FADH2, NADH, H+

o How many NADH and FADH2 are formed?

- 1 NADH

- 1 FADH2

o What type of reaction is at each step?

- Oxidation
 o How many acetyl CoA are formed for a certain FA? (ex. 12 C, 16 C, etc.)

- 1 acetyl CoA per 2 carbons

 Know the differences in the processes for unsaturated FA and for odd-

number FA.

- Unsaturated FA: 1 acetyl CoA for 1 C

- Odd numbered FA: 1 acetyl CoA for 3 carbons

o How many times does beta oxidation occur for a certain FA?

- 7 cycles

 How much ATP can be produced from a certain FA? Be able to do the math!

- 108 (-2 for activation step) = yields 106

 Describe how lipid breakdown is regulated.

- Leptin, insulin, and adiponectin

 Describe the basics of cholesterol catabolism. What is the purpose of this catabolism?

- Not an energy source

- Delivered via chylomicron remnants, LDL-chol, and HDL-chol

- Free cholesterol is excreted or converted to Bile acids

- Metabolic changes in bile synthesis

o Hydrocarbon side chain is added

o Carboxylic acid group is added

o Hydroxyl group is added

- Sterol solubility is enhanced, easier excretion

- If bile is not re-circulated, cholesterol catabolism is increased

 Describe the three stages of Cholesterol synthesis (3 steps listed in the slides). What is the

main enzyme that is regulated? Give two examples of how this enzyme can be inhibited.

- Hydrocarbon side chain is shortened

- Carboxylic acid group is added

- Hydroxyl group is added

- 3-Hydroxy-3-methylglutarylcoenzyme A (HMG-CoA) reductase

o Inhibited by phosphorylation

 Define Ketogenesis. When does it occur? What are the consequences of ketogenesis?

- Ketogenesis occurs when you don’t have enough glucose in storage for energy. There

is insufficient glucose for glycolysis.

- Consequences:

o Less pyruvate produced

o Less OXA for acetyl CoA to combine with for TCA to continue

o Accumulation of acetyl-CoA

 Describe FA synthesis including

o Location (Describe how Acetyl-CoA gets there)

- FA synthesis takes place in the cytosol

- Acetyl CoA is transferred from mitochondria to the cytosol.

- Mitochondria: acetyl CoA + OXA = citrate

- Cytosol: citrate lyse converts citrate back to acetyl CoA + OXA

o Acetyl-CoA carboxylase (requires biotin and ATP)

 o The function of FA synthase

- Condensing enzyme (acetyl-CoA is loaded onto the condensing enzyme)

- Acyl carrier protein

o 4 steps of Biosynthesis (What type of reaction is at each step?) lengthens FA by 2

Carbons.

- 1. Condensation

- 2. 1st reduction with NADPH

- 3. Dehydration

- 4. 2nd reduction with NADPH

o How is FA synthesis regulated?

- Acetyl CoA carboxylase catalyzes the synthesis of malonyl-CoA. This is the only

enzyme that regulates it.

 Be able to compare main differences between FA synthesis and FA oxidation!

  Describe the formation of EPA, DHA, and AA. Describe the role of each

- DHA

o Photoreceptors and synaptic membranes

o Plays a role in vision, neuroprotection, successful aging, and memory

o Much is accumulated in the first year of life

o 22:6, n-6

- EPA

o 0-3 family fatty acid

o Elongates (add 2 carbons) and desaturates (forming double bond) to form 20:5,

n-3

- AA

o 0-6 family

o Elongates (adds 2 carbons) and desaturates to for 22:4, n-6

 Compare the effects of eicosanoids derived from the O-3 and O-6 FA families.

- Derived from 10-carbon polyunsaturated fats (arachidonic)

- Omega 3s are anti-inflammatory

- Omega 6s are more inflammatory and are replaced by the omega 3’s

- Essential fatty acids influence the activation of cell genes to act as a second messenger

to produce eicosanoids

ALCOHOL

 Describe properties of ethanol (including kcals/g).

- Neither a carbohydrate nor a lipid

- Structurally a carbohydrate
 - Metabolized as a fatty acid

- 7 kcal/gram

 What are the three enzyme systems involved in Alcohol metabolism? What are the results

of this metabolism?

- ADH: alcohol dehydrogenase

o Soluble enzyme in cytosol of hepatocytes

o NAD  NADH

o Electrons transferred to the ETC

 Malate: aspartate shuttle (2.5 ATP from NADH)

 Glycerol-3-phosphate shuttle (1.5 ATP from FADH2)

o Moves to using MEOS system if maxed out

- MEOS: microsomal ethanol oxidizing system

o Electron transport to ER

 Requires cytochrome P-450

o Metabolized 1/5 of alcohol + FA, retinol, steroids, drugs, etc.

o MEOS enzymes induced by alcohol

o Better tolerate (accelerated breakdown) alcohol, medications, vitamin A

 More alcohol must be consumed to reach intoxication

 Need higher doses of medications

 Vitamin A deficiency

- Catalase: in presence of hydrogen peroxide

 Main consequences of alcoholism

- Impaired gluconeogenesis via not forming alpha-ketoglutarate

 - Metabolic shift to reduction by hydrogenation

- Fatty liver

- Cirrhosis: hepatic disease

- Lactic acidosis

- Metabolic tolerance

- Third leading preventable cause of death

 What is acetaldehyde toxicity? Adverse effects?

- ADH and MEOS produce acetaldehyde

- Toxic byproduct

- Causes hangover symptoms

- Forms adduct with proteins

o Impairs activity

- Impede formation of microtubules

o Cirrhosis

 High NADH: NAD+ ratio- how does it occur? What are its effects on metabolism?

- Ethanol oxidation

o NAD is an important regulator of dehydrogenase reactions (glycolysis, TCA

cycle, beta oxidation)

o Impaired gluconeogenesis via not forming alpha-ketogutarate

o Metabolic shift to reduction by hydrogenation

o Nothing will synthesize due to alcohol in the system. Blocks reactions

 Which vitamin may need supplementation in an alcoholic? Why?

 - They need B vitamins, because alcohol blocks absorption of these vitamins and causes

a deficiency. Having B vitamin deficiencies cause neurological degradation.

 List a few benefits of Alcohol in Moderation.

- Raise HDL

- Antioxidant properties if wine

o Resveratrol

- Increased sensitivity to insulin

- Decreased risk for heart disease

PROTEIN

 Know structure, charge, and polarity of amino acids.

 Know which AA are essential and non-essential.

- Essential

o Threonine

 Polar

 Uncharged

o Tryptophan

o Histidine

o Isoleucine

o Leucine

o Lysine

 Polar

 Positive

o Methionine
 o Valine

o Phenylalanine

- Non-essential

o Alanine

o Arginine

 Polar

 Positive

o Aspartate

 polar

 Negative

o Glutamate

 polar

 negative

o Asparagine

 Polar

 uncharged

o Glutamine

 Polar

 Uncharged

o Proline

o Serine

 Polar

 Uncharged
 o Glycine

o Cysteine

o Tyrosine

 Polar

 uncharged

 What does it mean if enzymes are conditionally essential? Give two examples of situations

that may cause AA to become conditionally essential.

- we only need that when an organ fails to function properly

o disease

o prematurity

 can’t synthesize some non-essential AA

 List endogenous and exogenous sources of protein.

- Exogenous (diet)

o Animal products (meat, poultry, fish, eggs, dairy products)

o Plant products (nuts, legumes, whole grains, grains, vegetables)

- Endogenous (about 70g/day)

o Desquamated mucosal cells

o Enzymes and glycoproteins

 Know the several roles, types and functions of proteins within the body.

 Describe protein digestion in the stomach and small intestine (including enzymes and their

respective activation).
 - HCL denatures protein and activated pepsinogen (secreted from chief cells) to pepsin

- Pepsin cleaves peptide binds near the carboxylic end of most AA

o Low specificity

- Amino peptidases

o Cleave peptide bonds at the N-terminal end

- Di-peptidases

o Cleave dipeptides into 2 free amino acids

- Tri-peptidases

o Cleave tripeptides into dipeptides and free AA

- End product: Free AA and tripeptides

- Free AA provide negative feedback and decrease activity of these enzymes

 Describe AA absorption into the enterocyte.

o Facilitated

 Most are sodium dependent

 Work in conjunction with ATPase

 Favor: peptides with high hydrocarbon mass and net electrical charge

 BCAA

 Neutral

 Essential

 Amino acids can compete for specific transporters

o Sodium-dependent

o Paracellular
  Absorption of peptides pass through tight junctions of enterocytes

 Increased likelihood of GI illness increases intestinal permeability

 Peptides are then hydrolyzed by peptidases in plasma at cell membrane or in

the tissue

 Peptides can be transported through the blood. Some AA are to unstable in

their free form. This characteristic allows for AA to be included in

parenteral nutrition formulas.

 Which of the above modes of absorption is favored? Why?

- Facilitated transport

o Peptides with high hydrocarbon mass and net electrical charge

 BCAA

 Neutral

 Essential

 Are most AA absorbed as single AA or as tripeptides?

- Tripeptides are more easily absorbed, because single/free AA are unstable. Free AA

also provide negative feedback to digestion enzymes and decrease the activity of the

enzymes.

 Describe AA absorption into extraintestinal tissues.

o Sodium-dependent N system

 Exchanges H+ for AA

o System A

 Induced by glucagon and provides amino acid substrates for

gluconeogenesis
 o System Gly

 Sodium dependent and specific for glycine and neutral AA

o Gamma Glutamyl Cycle (glutathione)

 Glutathione acts as a carrier of neutral AA

 Reacts with enzyme gamma glutamyl transpeptidase in the cell

membrane

 Forms gamma-glutamyl enzyme complex and binds neutral amino

acid

 AA is transported into the cytosol for cell use

PROTEIN: METABOLISM

 Describe Transamination and Deamination

- Transamination

o Transfer of an amine group from one amino acid to an alpha-keto acid (carbon

skeleton)

 A-keto acids

 Know the functions and locations of ALT and AST.

- Alanine amino transferase (ALT)

o Found in liver

o Pyruvate

- Aspartate amino transferase (AST)

o Found in heart

o Oxaloacetate

 Know the corresponding alpha-keto acid for alanine, glutamate, and aspartate.
 - Alanine: pyruvate

- Glutamate: alpha-ketoglutarate

- Aspartate: oxaloacetate

 List methods of, and reasons for, disposing of ammonia.

- Created for deamination, ingestion of food, bacterial breakdown of AA in intestine

- Ammonia is toxic for the body

- Disposal mechanisms:

o Form glutamate

 Gets rid of 1 ammonia

o Form glutamine

 Gets rid of 2 ammonia

o Form urea and excrete urine

- Urea is water-soluble and non-toxic

o Bodies can rid of it safely

- Formed in the liver

- Excreted in the kidneys

- Urea synthesis and excretion diminished if on low-protein diet

 Know the substrates involved in the Urea Cycle (see Urea Worksheet).

- NH3: derived from oxidative deamination of glutamate

- CO2

- Aspartate

- 3 ATP

- Urea fumarate
 - H20

 Give examples of fates of carbon skeletons/alpha-keto acids that remain after

transamination/deamination.

- Carbon skeleton and alpha ketoglutarate

o Energy generation

o Glucose production

 TCA cycle intermediates or conversion to pyruvate

 Occurs with high level of glucagon or cortisol

o Ketone body production

 Acetyl CoA or acetoacetate

o Cholesterol production

 Acetyl-CoA

 Leucine acetyl-CoAcholesterol

o Fatty acid production

 Review protein synthesis. Know the following terms: transcription, translation,

elongation, initiation, termination, ribosome, mRNA, tRNA, peptide bond

- Transcription: transcribes a gene into messenger RNA

- Translation: ribosomes move along the mRNA to synthesize proteins

- Initiation: leucine promotes the binding of initiation factors

- Elongation: tRNA brings the appropriate amino acids to form a peptide chain

- Termination: ribosome meets with a stop codon in the mRNA

- Ribosome: particle consisting of RNA

 - mRNA: RNA version of the gene that eaves the cell nucleus and moves to cytoplasm

where proteins are made

- tRNA: temporary carriers of amino acids, bringing amino acids to ribosome based on

mRNA

- peptide bond: two or more amino acids linked in a chain, carboxyl group of each acid

being joined to the amino group next by a bond of the type -OC-NH-

 Know the levels of protein structure.

- Primary structure

o AA structure

- Secondary structure

o Hydrogen bonding

 H+ and O-

o Electrostatic (ionic) attraction

 Lysine (1+) and Glutamine (1-)

- Tertiary structure

o Dictated by AA

o Clustering of hydrophobic AAs toward center

o Covalent bonding

 Disulfide bridges

- Quaternary Structure

o Interactions between two or more polypeptide chains

 Give examples of nitrogen-containing non-protein compounds.

- Glutathione
 o Antioxidant, reacts with H2O2, AA transport, conversion of prostaglandin H2

to D2 and E2

- Choline

o Methyl donor, part of acetylcholine and lecithin and sphingomyelin

- Carnitine

o FA transport

- Creatine

o Part of phosphocreatine (high-energy compound)

- Carnosine

o May be an antioxidant

 Describe intestinal amino acid metabolism.

- 90% of glutamate is metabolized in enterocyte

- 30-40% of essential AA

- Used for:

o Energy

o Structural proteins

o Nucleotides

o Apoproteins

o Digestive enzymes

 What are 2 indicators of muscle mass and protein catabolism?

- Creatine

o Existing muscle mass

- 3-methylhistidine
 o Protein degradation

o Found in actinin muscles

o Cannot be reused for protein synthesis and is excreted in urine

o Indicator of muscle breakdown

o Actin is also found in non-muscle tissues

 What influences the rate of protein synthesis? How?

- Nutrition

- Physical activity

 Where are the branched chain amino acids (BCAA) transaminated? List 3 examples of

BCAAs.

- Isoleucine

- Leucine

o Can be converted to HMB (Beta-hydroxy-methylbutyrate)

 HMB protects against muscle loss, especially those with cancer and

AIDS

 Precursor to cholesterol synthesis

- Valine

 Be able to draw the glucose/alanine cycle.

 What role does the kidney play in AA metabolism?

- Kidney play a role in the synthesis and interorgan exchange of several amino acids.

 Describe how body mass changes with age (in terms of fat and muscle composition).

- General decline of 1-2% each year after age 50

- Sarcopenia: age associated decrease in muscle mass, strength, and metabolic rate

- Influenced by:

o Reduced protein intake

o Reduced physical activity

o Loss of muscle innervation

o Oxidative damage (diminished strength)

o Decreased concentration of anabolic hormones

o Increased catabolism d/t cytokines

 Describe methods for assessing protein quality.

- High quality/complete (contains all essential AA)

- Low quality/incomplete

- Protein Digestibility corrected AA score (PCAAS)

o Compare amount of limiting amino acid to reference food (usually egg or milk)

o Take digestibility into consideration

- Protein efficiency ratio

o Body weight gained on a test protein divided by the grams of protein consumed

- Chemical or AA score= mg of AA in 1.0 g of test prot/ mg of AA in 1.0 g of ref. prot

 Explain nitrogen balance.

o Nitrogen balance= (protein intake (g) / 6.25) – (Urinary nitrogen + 2g + 2g)

 Accounts for nitrogen lost in feces and nitrogen lost in urine that is not

incorporated into urea

 Give examples of protein recommendations.

- Plant proteins

o Incomplete

 Except soy

o 70-90% digestibility

- Animal proteins

o Complete

 Except gelatin

- 10-15% of kcals

- RDA= 0.8 grams/kg of body weight per day

o Healthy adults

- Calorie and CHO intake must be adequate for optimal protein use

- AI is used for infants 0-6 months

o Based on amount in breast milk

- Adequate protein for elderly adults is important for maintaining bone mass

 Describe the difference between kwashiorkor and marasmus and characteristics of each.

o Kwashiorkor

 Adequate energy

 Inadequate protein
  Low serum proteins results in ascites and edema

o Marasmus

 Extreme muscle wasting

 Prolonged protein/energy deficiency

 Visceral proteins within normal limits (WNL)

Ch. 9 – Water-Soluble Vitamins

 Clinical Application: Give an example of how pharmacological doses of a water-soluble

vitamin may improve symptoms of an inborn error in metabolism.
- Folic acid supplements during pregnancy can reduce certain birth defects
 Vitamin C
o What is the main type of reaction that vitamin C is required for?
- Reduction (e- donor) and oxidizes Iron (Fe3+  Fe2+)
- Hydroxylation of proline and lysine require vitamin C
- Adds rigidity to collagen
o Prolyl hydroxylase
o Lysyl hydroxylase
- How is vitamin C Absorbed?
o Absorption across the brush border occurs in the small intestine by sodium
dependent transporters or SVCT1 and SVCT2 (active transport)
o Simple diffusion in stomach and small intestine– helps with absorption when
intakes are higher
o Anion channels may mediate vitamin C diffusion faster than transporters
o Give examples of neurotransmitters and other compounds that are synthesized by
vitamin C dependent peptide amidation.
- Norepinephrine
- Serotonin
o How is vitamin C Absorbed into the intestinal cell?
- Active transport
- Simple diffusion
- Carrier mediated transport (SVCT1)
o How is vitamin C absorbed into extraintestinal cells?
- Facilitated diffusion using sodium dependent transporters
o Where is the highest concentration of vitamin C in the body?
- Adrenal gland
- Pituitary gland
- Retina
o How is vitamin C excreted?
- Tissue>plasma
- Re-absorbed by the tubules
- Renal reabsorption threshold
 - Excreted in the urine as ascorbic acid or oxalate
o What is the RDA for men, women, smokers?
- Men: 90 mg/day
- Women: 75mg/day
- Smokers: an additional 35 mg
o What are food sources of vitamin C?
- Yellow peppers
- Kiwi
- Potato
- Broccoli
- Tomato
- Orange
- Papaya
- Strawberries
o Explain the mechanism by which scurvy symptoms such as bleeding gums and
pinpoint hemorrhages occur due to vitamin C deficiency.
- Plasma levels <2.0 mg/dL
- Leukocytes <10mg/108 WBC- deficient
o What are some methods for assessing vitamin C nurtriture?
- Possible medication interactions
- GI distress
- Absorb too much iron
- Kidney stones
o Urine acidification
o Too much oxylate
 Thiamin
o What are roles of Thiamin within the body?
- Energy metabolism (decarboxylation reactions)
- Synthesis of NADPH and pentoses
- Nerve cells and muscle cells (mechanism unclear)
o What is the main type of reaction that thiamin is involved with? Give examples of
some of those reactions.
- Reducing
- Decarboxylation
o What vitamins are required for the pyruvate dehydrogenase reaction?
- Thiamin
- Pantothenic acid
- Riboflavin
- niacin
o What are some food sources of Thiamin?
- Enriched pasta
- Pork chop
- Green peas
- Waffle
- Wheat bagel
- Enriched cereal
 - Sunflower seeds baked potato
- Black beans
o Describe the mechanism for Thiamin absorption.
- TDP (aka TPP) is hydrolyzed by phosphates  absorbed as free thiamin
- Jejunum (passive or active via THTR1)
- Uptake by liver and phosphorylated to TDP (active co-enzyme form)
- Found in brain, heart, liver, muscles, kidney
o What may decrease absorption of thiamin?
- Thiaminases
o Raw fish
- Polyhydroxyphenols
o Coffee, tea, blueberries, black currants, brussels sprouts, red cabbage
- Alcohol
o Why is the RDA higher for men than for women?
- Men have an overall larger body
o Describe the mechanism by which lactic acidosis may occur due to thiamin
deficiency.
-
o What is the coenzyme form of Thiamin?
o **Know the symptoms for wet and dry beriberi, and Wernicke-Korsakoff
syndrome.
- Dry beriberi
o Muscle weakness
o Peripheral neuropathy
o Foot drop
o Tenderness of calf muscles
- Wet beriberi
o Cardiomegaly
o Tachycardia
o Edema
- Acute
o Lactic acidosis
o Occurs mostly in infants
- Wernike-korsakoff
o Common among those who abuse alcohol
 Displace nutrients
 Impair thiamin absorption
 Decreased activation of thiamin to coenzyme form
 Increases excretion of thiamin in the kidney
o Develops suddenly
o Medical emergency
o Caused by acute lesion in brain
o Paralysis or weakness or eye movements, ataxia, mental disturbances
o Brain damage if not treated
 Riboflavin
 o What are the coenzyme forms of riboflavin?
- FAD (Flavin Mononucleotide)
o Why is milk stored in opaque containers?
- Killed by UV light
o Give 3 examples of flavoprotein functions.
- Oxidative decarboxyltion of pyruvate and keto glutarate
- Synthesis of folate
- Choline catabolism
o How is the RDA for riboflavin established?
- Men: 1.3 mg/day
- Women: 1.1 mg/day
o What is the deficiency of riboflavin called? What are some of the symptoms of this
deficiency?
- Aribinoflavinosis
o Sore throat
o Cracked skin
o Enlarged tongue
o What effect does alcohol have on riboflavin status?
- Can’t be absorbed
 Niacin
o What are food sources of niacin?
- Bound in corn, wheat, and cereal products
o What are the main differences between the functions of NAD and NADPH?
(Recall that niacin is a component of both of these coenzymes.)
- NAD and NADP are hydrolyzed to free nicotinamide
o What AA can be converted to niacin?
- Tryptophan
o What are niacin equivalents? Know how to calculate the amount of niacin
equivalents from 3 oz of meat.
- 1 mg of niacin = 60 mg tryptophan
o What is the name of the condition that results when a person is niacin deficient?
- Pellagra
o What are the symptoms?
- Diarrhea
- Dermatitis
- Dementia
- Death
o What are symptoms of niacin toxicity?
- Niacin flush
- Tingling
- Vision distortion
 Pantothenic acid
o What does pantos mean? What foods contain pantothenic acid?
- Everywhere
- Chicken, beef, potatoes, broccoli, egg yolks, whole grains
 o Which coenzyme is pantothenic acid a part of? Give examples of reactions in
which this enzyme is important.
- Co-Enzyme A
- Glycolysis, TCA cycle
o Describe the signs of deficiency in Pantothenic Acid.
- Fatigue
- GI stress
- Neurological distrbances
- Burning feet
o What is the AI for Pantothenic Acid?
- 5 mg/day
 Biotin
o Describe the digestion and absorption of biotin.
- Bound to protein
- Digestion by proteolytic enzymes
- Free biotin absorbed in jejunum
o Sodium dependent transport protein
o Passive diffusion
o What are some function of biotin as a coenzyme? As a non-co-enzyme?
- Energy metabolism
o Pyruvate carboxylases
 Replenishes oxaloacetate
 Needed for gluconeogenesis
o Acetyl CoA carboxylase
 Acetyl CoA  malonyl CoA (FA synthesis)
- DNA repair
o What are some symptoms of biotin deficiency? List some common causes of
deficiency.
- Hair loss
- Depression
- Eating raw eggs
- impaired absorption
o GI illness
o Alcohol
- Anticonvulsant drug therapy
 Folate
o What are the 3 distinct parts of folate?
- Pteridine
- PABA
- Glutamic acid
o List some food sources of folate?
- Fortified foods
- Naturally occurring
o Describe folate digestion and absorption.
- Removes glutamate residues
- Absorbed into enterocyte in mono glutamate form
 o Compare and contrast folate and folic acid (including food sources).
- Folate: naturally occurring, destroyed by heat, reduced form
- Folic acid: fortified foods, supplements, oxidized form, heat stable
o Be prepared for an essay on folate deficiency and anemia, birth defects, cancer,
CVD.
- Methotrexate
o Cancers and rheumatoid arthritis treatment
o Similar structure to folate
o Can cause severe folate deficiencies
o Inhibits dihydrofolate reductase
- Birth defects
o Brain and spinal cord develop during first days and weeks of pregnancy
o What methods are used to assess folate levels?
 Plasma, serum, RBS
 N-formininoglutamate excretion

STOP
 Vitamin B-12
o Maintains myelin sheaths that protect nerve fibers
o Helps folate build blood cells
o Homocysteine  methionine
o Be prepared for an essay on B-12 digestion and absorption.
 Vitamin B12 is released from proteins, pepsin and HCL
 Binds to an R protein in stomach or duodenum
 R protein is digested, B12 gets released
 B12 binds with intrinsic factor
 IF is a glycoprotein that is produced by parietal cells but escapes
enzymatic catabolism
 B12-IF travels to ileum binds to a receptor on the intestinal cell
 Gets internalized by endocytosis
 B12 binds to transcobalamin II for transport into portal blood
o List examples of sources of B-12
 Animal foods and some fermented products
 Destroyed by cooking
 RDA: 2.4 mcg/day
o Be prepared for an essay about causes for deficiency/who is at risk for
deficiency/treatment.
 Inadequate intake (vegans)
 Absorption defects
 Ileal resection, celiac disease, ileitis
 Intrinsic Factor Deficiency
 Pernicious anemia
 Gastrectomy
 Zollinger-Ellison Syndrome
 Tumor secretes gastrin
 Pancreatic insufficiency
 o Low pH
 B12 is not released from R-protein
o How is B-12 nutriture assessed?
 Serum can look normal, but tissue concentration may be low
 Schilling test
 Low urine B12 suggests poor absorption

 Ch. 10 - Fat-Soluble Vitamins

o Compare and contrast digestion, absorption, transport, and storage of fat-soluble
and water-soluble vitamins.
o Vitamin A
 Be prepared for an essay regarding vitamin A deficiency
 Night blindness
o Failure or delayed recovery of vision in the dark following a
flash of light may be caused by a vitamin A deficiency
 Keratin accumulation
o Skin, GI, urinary tract, respiratory tract, eyes
 Xeropthlamia
o #1 cause of blindness worldwide
 Deterioration of mucous membranes
 Bone growth: stimulates osteoclasts
o Too much mineral deposition
 Hematopoiesis
o Decreased incorporation of iron into RBC
o Decreased mobilization of iron stores
 Toxicity
 Vitamin A: UL 2.5
o Nausea/vomiting
o Blurred vision
o Headaches
o Bone abnormalities
o Liver damage
o Birth defects
 Nutriture Assessment
 Levels of rhodopsin in the eye
 Histological tests of morphological changes in the epithelial cells of
the conjunctive
o Large and flat= deficiency
 Dose response test:
o >20%=deficiency
 5 hr. plasma retinol – initial plasma retinol / 5-hour retinol
concentration x100
o Vitamin D
o Know sources of vitamin D, including the form (D2 vs D3).
  D3: liver, eggs, salmon, herring, tuna, sardines, cheese, fortified dairy
products, supplements
 D2: shitake mushrooms, fortified foods
 Sunlight
o Be prepared for an essay regarding vitamin D conversions to the active form and
calcium homeostasis
 Leaves enterocyte via chylomicrons
 Leaves the liver via vitamin D binding protein (DBP)
 Vitamin D formed in the skin in transported though the blood via DBP
 D3 (food/sunlight)
 Liver  25-OH cholecalciferol (calcidiol)
 Kidney  1,25 dihydroxy cholecalciferol (calcitriol)
 D2
 Can also be converted to the active from via the same 1 and 25
hydrolases
 Less efficient
 1. In blood there is a decrease in Ca2+ and goes to the parathyroid gland
 2. The Ca2+ signals the parathyroid gland to release parathyroid hormone
(PTH) then the elevated PTH levels can go two different places
 3. Increase PTH in the blood goes to the kidney
 4. Stimulates kidneys to increase in Ca2+ reabsorption
 5. Increase blood Ca2+
 6. Stimulates renal-hydroxylase to convert 25-OH D to 1,25-(OH)2 D
(calcitriol)
 7. Increase blood calcitriol and dietary Ca2+ in lumen through intestines
 8. Increase in calcitriol Ca2+ absorption in intestine by increasing calbindin
D9K synthesis, calcium channel transporter synthesis, Ca2+ ATPase
exporters, and claudin protein synthesis, among other means
 9. Increase blood Ca2+ travels from intestine back through blood
 10. Bone: increase PTH, increase calcitriol travels to bone
 11. Increase PTH and calcitriol stimulate resorption of Ca2+ and P from
bone
 12. Result is an increase in blood Ca2+
 When blood calcium is low
 Parathyroid glands release PTH
o Stimulates conversion to calcitriol (active form)
 Increased active form of vitamin D
o Increased absorption of calcium in the intestines
o Increased reabsorption of calcium in the kidneys
o Increased bone turnover (calcium is released from the bones)
o Describe the role of vitamin D in gene expression.
 Vitamin D Response element (VDRE) interacts with DNA
 1. VDR binds with calcitriol
 2. Changes in gene transcription
 3. Changes in protein synthesis
 o Describe vitamin D deficiency and mechanisms that may lead to vitamin D
deficiency. Who is at risk?
 Metabolites are excreted via the bile
 Assuming minimal sun exposure: 600-800IU
 Higher end for elderly and pregnant women
 8 oz. of fortified milk contains 100IU
 Vitamin D is affected by
 Season of the year
 Location
 Organ dysfunction
 Dark skin
 Sunscreen
 Rickets (children)
 Osteoporosis (adults)
 Decreased calcium absorption
 Decreased osteoblast action
 At risk populations
 Elderly
 Fat malabsorption
 Tropical sprue
 Crohn’s disease
 Parathyroid, liver, and/or kidney disease
 Anticonvulsant drug therapy
 Breast fed infants
 Little exposure to sunlight
o Assessment of Nutriture
 Serum 25-OH concentrations
 75-100 nmol/L needed for bone health
 Vitamin E
o Know forms of vitamin E. Which one is most active?
 Tocopherols
 Have saturated side chains with 16C
 RRR alpha tocopherol is the most biologically active form (d-alpha-
tocopherol)
 Tocotrienols
 Trienols
 Have unsaturated side chains with 16C
 Supplements use a mix of sterioisomers
 Not as active as the naturally occurring RRR isomer
o What are food sources of vitamin E?
 Wheat germ oil (20 mg/oz)
 Wheat germ (4.5g/oz)
 Almonds (7mg/oz)
 Mayonnaise (0.1mg/Tbsp.)
 Spinach (1.9mg/0.05cup)
  Destroyed at high temperatures
o Be able to describe the mechanism by which vitamin E protects red blood cells.
 Low dietary intake associated with development of cataracts and macular
degeneration
 Tocotrienols suppress the activity of HMG-CoA reductase  decreased
blood cholesterol
o What are symptoms of vitamin E deficiency? Who is at risk?
 Skeletal muscle pain weakness
 Hemolytic anemia
 Degenerative neurological problems
 At risk
 Fat malabsorption disorders
 Genetic defects in transfer protein
o What are concerns with vitamin E deficiency?
 Toxicity is rare
 Symptoms
 GI distress
 Increased risk for bleeding (interferes with blood clotting)
 Increased mortality with supplementation
o Assessment of Nutriture
 Plasma levels <5 mcg/mL
 Erythrocyte hemolysis test
 In vitro lysis of ed blood cells when incubated with hydrogen
peroxide
 Vitamin K
o Know sources of each form of vitamin K.
 Phylloquinone
 Green leafy vegetables
 Oils and margarines
 Some supplements
 Menaquinone
 Formed by bacteria in the colon
 Liver, fermented cheeses
 Menadione
 Synthetic for found in animal feeds
o Be prepared for an essay regarding vitamin K, the vitamin K cycle, blood clotting,
and anti-coagulation medications.
 Transported from enterocyte via chylomicrons and from liver via VLDL
 Stored in cell membranes of lungs, kidneys, bone marrow, adrenal. Glands,
etc.
 The liver rapidly metabolizes the vitamin but retains little in storage
 Blood clotting= Vitamin K (koagulation)
 Prothombin and other protein must become carboxylated to be functional
 This process is vitamin K-dependent
 Carboxylation
 Vitamin K-dependent proteins
  Prothrombin (factor II)
 Factor VII
 Factor IX
 Factor X
o Allows conversion to fibrinogen to fibrin
 Vitamin K-dependent carboxylation of Osteocalcin and matrix Gia protein
 Facilitate binding of calcium to the bone matrix
 Vitamin K Cycle
 Vitamin K is rapidly depleted without dietary intake
 Recycle (reduces) via vitamin K cycle to insure blood count
 Vitamin K must be in reduced form to be functional
 Warfarin
 Anticoagulant medication
 Prevents recycling of vitamin K
 Large quantities (1 lb. of broccoli) can override the anticoagulant
effects
 Keep vitamin K intake consistent
o Describe the interactions vitamin K has with vitamins A and E.
 Vitamin K interacts with large amounts of vitamins A and E interfere with
absorption of vitamin K
 Vitamin E interferes with vitamin K metabolism

o Be able to describe why infants are at risk for vitamin K deficiency and most adults
are not.
 Babies have very little vitamin K in their bodies because vitamin k doesn’t
pass through the placenta
o How is vitamin K nutriture assessed?
 Serum levels
 Prothrombin time
 >25 seconds = deficiency
 Under-carboxylated prothrombin or osteocalcin

Ch. 11 – Major Minerals

CALCIUM:

 What are some good sources of calcium (beside milk and dairy)?
o Dairy products
o Vegetables
o Nuts
o Tofu
o Supplements
 Describe the two processes of calcium absorption.
o Active transport is duodenum and jejunum
  Saturable
 Transport protein: TRPV6 (transient receptor potential vanilloid 6)
 Calbindin (cytosolic binding protein; stimulated by vitamin D), shuttles
calcium across the cytosol
 TRPV6 and Calbindin decline with age
o Paracellular absorption
 What role does calbindin play in calcium absorption?
o Decreases blood calcium
 List the factors that influence calcium absorption.
o Increase
 Vitamin D
 Protein
 Sugar
 Low calcium intake
 Pregnancy and lactation
 Gastric acid
o Decrease
 Phytates
 Oxylates
 Unabsorbed dietary fats
 Divalent cations
 Magnesium and zinc
 Deficiency of gastric acid d/t GERD treatments or advancing age
 Name and describe the three hormones that are involved with regulation of extracellular
calcium?
o PTH
 Promotes synthesis if calbindin
 Secreted when calcium is low
o Calcitriol
 Promotes synthesis of calbindin
 Increases TRPV6 and ATPases
o Calcitonin
 Secreted by the thyroid gland
 Inhibits osteoclasts
 Suppresses PTH formation and synthesis
 Decreases blood calcium
 Compare cortical and trabecular bone. Which type is more sensitive to changes in calcium
intake?
o Cortical bone
 Outer, hand, 75-80% of bone
 o Trabecular
 Inner (vertebrae, shaft of long bones, pelvis, etc), spongy
 Sensitive to changes in nutrients, hormones, etc.
 What other roles does calcium play that are not associated with bone?
o 1% Ca not associated with bone
o 50% is ionized (active)
o Alone or with calmodulin, it affects enzymes that regulate
 Blood clotting
 Nerve conduction
 Muscle contraction
 Enzyme regulation
 Membrane permeability
 How does phosphorus, fat, and bile, protein, sodium, caffeine and alcohol interact with
calcium?
o Phosphorus
 Absorption inhibited by calcium
 Historically used in treatment of kidney disease
o Fat and Bile
 Calcium binds and forms soaps  decreased absorption of fat and bile
o Protein, sodium, caffeine, alcohol
 Promote calcium loss
 Be prepared for an essay on calcium homeostasis (be sure to describe how PTH,
calicitonin, calcitriol, and calbindin are involved)
 What is the RDA for men and women? What about for individuals 51 or older?
o 1,000mg for men and women
o 51+ yrs. Old: 1,200mg
o Adolescents: 1,300mg
 What are the symptoms of toxicity? Deficiency?
o Deficiency
 Rickets
 Hypocalcemia
 Results in tetany
 Osteoporosis
 Colon cancer
 Obesity
o Toxicity
 UL: 2500 mg
 Symptoms
 GI distress
 Metabolic alkalosis
 o Lethargy
o Anorexia
o n/v
o heart arrythmias
 loss of kidney function
 See the Grandma Francesca Case Study.
 Assessment of Nutriture
o Serum calcium levels adjusted for protein status
o DXA-bone density

PHOSPHORUS:

 What are food sources of phosphorus?

o Widely distributed in foods
o Meat, fish, dairy
o Whole grains
o Beans
 Phytic acid form
 Does Phosphorus use facilitated or passive diffusion?
o Digestion
 Cleaved from protein, sugars, lipids
o Absorption
 Saturable- carrier mediated active transport
 Concentration- dependent facilitated diffusion
 What are some factors affecting absorption?
o Increase
 Vitamin D
o Decrease
 Phytates
 Magnesium
 Aluminum
 Calcium
 Where is phosphorus stored?
o Intestine to blood
 Organic 70% (lipoproteins, phospholipids)
 Inorganic forms 30%
o Storage
  Circulating is in equilibrium with skeletal and cellular
 Found in all cells, especially bone and muscle
 Describe the roles of Phosphorus in the body, especially related to nucleotide phosphates.
o Nucleotide phophates
 Structural roles (DNA&RNA)
 Energy Storage (ATP)
 Intracellular 2nd messenger (cAMP)
o Structural Roles
 Phospholipids
o Acid-Base Balance
 Buffer
o Oxygen availability
 2,3-diphosphoglycerate required for oxygen release from hemoglobin
o Bone mineralization
 85% as hydroxyapatite
 Calcitonin- promotes ossification of phosphorus onto matrix
 PTH- promotes resorption of phosphorus from bone and excretion in urine
 Calcitriol- promotes increased phosphorus absorption in the intestine
 How is the majority of Phosphorus excreted from the body?
o Urine- inorganic form 67-90%
o Feces—10-33%
o High diet, high serum, high urine (renal regulation)
 What is the RDA for Phosphorus?
o 700 mg/day
o Deficiency is rare
 People with renal disease taking phosphate binders
o Toxicity is rare

MAGNESIUM:

 List some good dietary sources of magnesium.

o Nuts
o Legumes
o Whole grains
o Seafood
o Leafy greens
o Beans
o Peas
o Chocolate
o The less processed, the better
 List a few factors influencing magnesium uptake.
o Increase
 Vitamin D in pharmalogical doses
 Fructose and oligosaccharides
 Protein
o Decrease
 Phytates
 Steatorrhea (forms soap)
 Nonfermentable fibers
 Calcium
 What are some of the functions of magnesium in the body?
o Bone- part of crystal lattice and surface
 Hydroxylation of vitamin D
o Part of phospholipids (cell memebranes)
o Stabilizes nucleic acids
o Muscle contraction
o Enzymes
o Roles in metabolism
 Beta oxidation, TCA, glycolysis, hexose monophosphate shunt, protein
synthesis, etc.
 Compare and contrast the effect of PTH on calcium and magnesium.
o Hormonal control via PTH
 Increased intestinal absorption
 Decreased renal excretion
 Enhanced bone magnesium resorption
o PTH affects magnesium in the same ways as Ca
 When would an individual be susceptible to magnesium deficiency?
o Older adults, 31+
 Males: 420mg
 Females: 320mg
o Osteoporosis
o Exacerbates inflammation and contributes to diseases such as heart diseases, HTN,
DM, and cancer

SODIUM:

 Be familiar with the following terms, relating to sodium:

o Free, light, reduced, low, very low
 What percent of sodium is generally absorbed?
 Describe the three pathways of sodium absorption.
  How are concentrations of sodium regulated in the blood?
 Which hormones promote the reabsorption of sodium?
 Which hormones promote the secretion of sodium?
 What are the symptoms of sodium deficiency?
 What is the UL for sodium? What is the average intake?

POTASSIUM:

 What are some main dietary sources of potassium?

 How much is absorbed? What is the mechanism for absorption?
 How is potassium transported?
 What is the function of potassium?
 How does potassium affect calcium excretion?
 What are the signs of deficiency and toxicity from potassium?

CHLORIDE:

 How is chloride transported into the body?

 What are the functions of chloride?

Ch. 12 – Fluid Balance and Acid/Base Balance

 Define the following terms: intracellular fluid, extracellular fluid, interstitial fluid,
intravascular fluid.
o Intracellular: inside cells
o Extracellular: outside of cells
 Interstitial (between cells)
 Intravascular: inside blood vessels
 Name the main intracellular and extracellular cations.
o Intracellular
 Cations
 Potassium
 Magnesium
 Anions
 Phosphate
 Sulfate
o Extracellular
 Cations
 Sodium
 Anions
  Chloride
 What is the main extracellular anion?
o Chloride
 Describe how filtration forces and osmotic pressure influence fluid balance. Describe
the effect of low albumin levels on fluid balance.
o Hydrostatic pressure from the pumping of the heart
o Plasma
o Stronger FF at the arteries than veins
 What does GFR stand for? What does it mean if someone has a low GFR?
o Glomerular Filtration rate
o Decreased or severe kidney failure
 Be prepared for an essay question about fluid balance and the RAAS system.
 Describe the action and outcome of an ACE inhibitor medication.
 What is ANP? Describe the overall effect of ANP.
 Be prepared for an essay question similar to the Acid/Base case studies.

Ch. 13 – Microminerals

IRON:

 What are some of the main heme sources of iron? Nonheme sources?
a. Heme
i. Animal products
b. Nonheme
i. Plant sources and dairy products
 Be prepared for an essay regarding iron digestion, absorption, exit from enterocyte,
and transport through the body.
a. Iron digestion
i. Heme is hydrolyzed from globin portion of hemoglobin and myoglobin
ii. Non-heme is enzymatically freed in GI tract and gets secreted by gastric
b. Absorption
i. Heme and nonheme iron get absorbed in the duodenum and jejunum.
Inhibitors and enhancers of iron. Protein hepcidin regulator
c. Hepcidin
i. Hepatocyte
1. Binds and gets transported into the blood srum
ii. Blood serum
1. Fe-11 binds to TfR
iii. Enterocyte
1. TfR enter enterocyte
 iv. Non-heme
1. Enters enterocyte binds to DCYT8 and DMT1 as a facilitated
transporter
 What are some enhancers of iron absorption? Inhibitors?
a. Enhancers
i. Vitamin C
ii. Meat
iii. Poultry
iv. Fish
v. Alcohol
b. Inhibitors
i. Tannins (tea and coffee)
ii. Calcium
iii. Dairy products
 What are functions of iron?
a. Essential element for blood production
b. Found in hemoglobin and myoglobin
c. Hemoglobin is essential for transferring oxygen in your blood
 Be able to describe the mechanism behind, and symptoms of, hemochromatosis.
a. Too much iron in the body builds up (iron overload)
b. Symptoms are arthritis
c. Body can’t get rid of the iron
 What factor determines the amount of iron taken up by tissues?
a. This depends on the amount of iron stored in the body
b. Transferrin saturation and iron will bind to transferrin and is transferred to the
organs
 What role does iron have in the transport of oxygen?
a. Every red blood cell contains iron in hemoglobin which is the protein that carries
oxygen to the body’s tissues from the lungs
 What are some of the neurological effectors that require iron for synthesis?
a. Oxygen transportation
b. DNA synthesis
c. Mitochondrial respiration
d. Myelin synthesis
e. Neurotransmitter synthesis in metabolism
 Know the general interactions that iron has with the following nutrients:
a. Copper
i. Elevated copper levels in mucosa, liver, and blood
b. Zinc
i. Competitive during intestinal absorption
c. Lead
 i. Taken up by iron absorption but inhibit iron by blocking it
d. Selenium
i.
e. vitamin C
i. increases solubility of iron in small intestine
f. vitamin A
i. helps with absorption rate
 How is iron excreted?
a. Iron doesn’t get excreted; it goes through uptake and recycling in the body
 What is the RDA for men? Women? During pregnancy?
a. males: 8mg
b. females: 18mg
c. 27mg
 What populations are most vulnerable to iron deficiency?
a. Pregnant women and women in childbearing years
 Describe the three stages of deficiency.
a. Stage 1- storage depletion
b. Stage 2- mild deficiency
c. Stage 3- iron deficiency anemia

ZINC:

 What are good food sources of zinc?

a. Shellfish
b. Beef
c. Poultry
d. Pork
e. Legumes
f. Nuts, seed
g. Whole grains
h. Fortified breakfast cereals
 Describe zinc absorption.
a. Mouth, stomach, and small intestine
b. Needs to be hydrolyzed from Amino Acids and nucleic acids before it can be
absorbed
c. Protein digested in GI tract and degraded into amino acids
d. Zinc released from food during consumption
i. Acidic environment of the stomach and upper duodenum
ii. Proteases an nucleases in the stomach and small intestine
e. 20-30% of zinc from typical US diet, the human contains about 1.5-3.0g of zinc
f. Absorbed into small intestine
 g. Carrier mediated transport and diffusion
 List some nutrients that are inhibitors of zinc absorption.
a. Casein
b. Some other protein sources may inhibit
 What are some exogenous ligands that are enhancers of zinc absorption? Endogenous?
a. Histidine
b. Methionine
c. Citrate
 Zinc is part of several metalloenzymes. Name a few. Which enzyme is responsible for
nucleic acid synthesis?
a. Histone deacetylases
b. Carbonic anhydrases
c. Matrix metalloproteinases
 Describe how zinc is involved in the acute phase response.
a. Regulates the acute phase response and serum amyloid A production in response to
sepsis through JAK-STAT3 signaling
 Describe the relationship between metallothionein, zinc, and copper.
a. Metallothionein; Increases zinc absorption
b. When cadmium or copper is bound into it as well, the degradation rate is decreased
 How is zinc involved with protein synthesis?
a. Regulates thymidine kinase mRNa through zinc-dependent protein bind to
promoter region of the gene
b. Required for DNA synthesis, cell division, and growth
 How does zinc affect CHO metabolism?
a. Reduces oxidative stress by participating in synthesis of antioxidant enzymes and
acts as a catalyzer of enzymes
 Zinc affects taste through its interaction with which protein?
a.
 What is the RDA for zinc?
 What are some symptoms of Zinc deficiency?

COPPER

 Describe the digestion and absorption of copper.

 What factors enhance copper absorption? Inhibits?
 Know the following terms in relation to transport:
o Metallothionein, Cerulplasmin, apocerulopla smin (enzyme), ascorbic acid
 What are the main functions of copper?
 How is copper involved with enzymatic reactions?
 Copper acts as a cofactor for which enzymes?
 Describe the following features of Wilson’s disease and Menke’s disease:
o What causes the decease?
o What are the symptoms?
o What are the treatments?
 What are the causes and symptoms of copper toxicity?

SELENIUM:

 What are the organic and inorganic forms of selenium?

 What factors enhance and inhibit absorption?
 Describe transportation of selenium.
 Name three enzymes in which selenium is a cofactor.
 List the causes and signs of Keshan’s disease and Kashin-Beck disease.
 What are the major symptoms of selenium deficiency?
 What are the symptoms of toxicity?
 What populations have shown toxicity of selenium?

CHROMIUM:

 What are the general functions of chromium?

 How does chromium affect nucleic acid metabolism?
 In what populations is there potentially an increased need for chromium?

IODINE:

 What are three forms of iodine?

 How is iodine absorbed? How is the thyroid gland involved?
 What are the functions of thyroid hormones?
 Describe the hormones that are involved in the synthesis of thyroid hormones.
 How is iodine involved with the synthesis of thyroid hormones?
 What is organification? Where does it occur?
 How is thyroxine transported in the blood?
 Define goitrogens.
 What is the result of iodine deficiency? What are the symptoms of cretinism?
 What are the symptoms of a hypothyroid state?
 Describe the signs of exophthalmic goiter.
 What is Grave’s disease?
o Is it genetic?
o Do men or women get it more commonly?
 o What are the symptoms?

FLUORIDE:

 About what percentage of water in the US is fluoridated?

 How much of the fluorine is absorbed? What is the mechanism for absorption?
 What are the major functions of fluorine?
 List some nutrients that increase or decrease fluorine absorption.
 What are the signs of deficiency? What about toxicity?