AN II exam 1

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1

Thiamin, vitamin ______ has both coenzyme and non-coenzyme roles

B1

2

The ___________________ role of thiamin is used for: 1) metabolism of _____________________ and ____________s

2) synthesis of __________________ for production of nucleic acid synthesis (deoxyribose for DNA and ribose for RNA) and ___________ (essential for fatty acid synthesis)

coenzyme, carbohydrates, BCAAs, pentoses, NADPH

3

The _____________________ role of thiamin is used for: ____________________ and ____________ conduction

non-coenzyme, membrane, nerve

4

The major role of TPD (thiamin) is in the pyruvate dehydrogenase complex for __________________ ________________________

oxidative decarboxylation

= removal of a carboxyl group (-COOH) from pyruvate releasing it as carbon dioxide (CO2) so acetyl coA can be made

5

what are the specific enzyme complexes that use thiamin (in its coenzyme role)? 4 complexes

1) pyruvate dehydrogenase complex (pyruvate -> acetyl coA)

2) alpha-ketogluterate dehydrogenase complex (converts alpha-ketogluterate -> succinyl coA within TCA cycle)

3) branched-chain alpha-keto acid dehydrogenase (BCKAD) complex (combination of enzymes responsible for degradation of

4) pentose phosphate pathway (TDP, thiamin, works as prothetic group of transketolase, which is needed for NADPH and pentoses)

6

What are the signs of thiamin deficiency?

"beri" means weakness; muscle wasting, nerve damage

7

this type of beriberi occurs primarily in adults with low chronic thiamin intake and high carbohydrate intake; muscle weakness and wasting occurs, especially in lower extremities

dry beriberi

8

this type of beriberi has more extensive cardiovascular involvement compared to dry beriberi - rapid heart beat; cardiomegaly (enlarged heart); edema (swelling, "pitting" edema); edema and heart disease/issues stem from heart not pumping as well as normal and fluid builds up

wet beriberi

9

this type of beriberi occurs primarily in infants from a nursing mother suffering from beriberi; symptoms include anorexia, vomiting and lactic acidosis occurs b/c thiamin is needed to convert pyruvate to acetyl coA so instead pyruvate is converted to lactic acid

acute beriberi

10

Why does a high carbohydrate diet aggravate a thiamin deficiency?

wasting

it is especially a problem with dry beriberi b/c you cannot utilize pyruvate and convert it to acetyl coA when you do not consume enough thiamin; most of the acetyl coA would not come from carbs, but come from protein, thus causing muscle wasting; decreasing carbs and increasing protein and fats would help with providing enough acetyl coA

11

thiamin deficiency in alcoholics can cause this; causes paralysis of ocular muscles (opthalmoplegia), constant, involuntary eyeball movement (nystagmus), and impaired muscle coordination (ataxia)

Wernicke-Korsakoff syndrome

12

Riboflavin is vitamin ______; "flavus" means _____________ in Latin

B2

yellow

13

FAD and NAD are similar in structure and makeup; the only thing that changes is the vitamin, either _____________ or _____________________

niacin or riboflavin

14

__________ acids enhance B2 absorption

bile

(B2 is involved in fat usage; so how much lipid is in the diet will affect riboflavin absorption; ex: if you drink a glass of skim milk, fat is not digested as well)

15

what is the major coenzyme form of riboflavin? what is the other coenzyme form?

FMN

FAD

16

How does riboflavin (B2) relate to metabolism of vitamin B6?

pyridoxine phosphate oxidase converts PMP and PNP to pyridoxal phosphate (PLP), the primary coenzyme form of vit B6

17

pyridoxine phosphate oxidase activates B6 to its main coenzyme form (PLP) through dependence on ________________ for activation

riboflavin

18

_________ is involved in all metabolisms of the three macronutrients (carbs, fat, protein)

FAD

19

you can make ____________ (B1) from tryptophan and riboflavin (B2) is required for this process

card image

niacin

20

How is riboflavin related to anabolism of iron?

riboflavin is required for the synthesis of B6 which makes PLP (the active form of B6), which is required for heme (iron) production; thus, without riboflavin, B6 cannot be made, and then heme iron cannot be made

21

what are the signs and symptoms of riboflavin deficiency (ariboflavinosis)?

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- cheilosis (painful lesions on outside of lips and corners of mouth; aka angular stomatitis)

- glossitis (inflammation of the tongue)

- seborrheic dermatitis (associated with waxy substance found noticeably around nose)

- bloody, red and swollen oral cavity

- neuropathy

22

how can phototherapy for babies with jaundice affect B2?

phototherapy converts bilirubin to compounds that can be excreted via fecal and urine routes, but the phototherapy causes riboflavin destruction because thiamin (B2) is liable in light

23

niacin circulates in blood as __________________ b/c nicotinic acid would affect pH of blood; also, this form of niacin is the primary precursor of NAD, which is made in all cells

card image

nicotinamide

24

What are the differences in structure between nicotinic acid and nicotinamide?

nicotinic acid - has carboxyl group/carboxylic acid (COOH)

nicotinamide - has amino group (CONH2)

25

______________________ enzymes usually require NAD/NADH; this enzyme is an enzyme that catalyzes the transfer of hydrogen or electrons from a donor (oxidizing it), to an acceptor (reducing it)

dehydrogenase

NAD= nicotinamide dinucleotide

NADP= nicotinamide dinucleotide phosphate

26

when _______________ is used as a combination treatment, lipid-lowering drugs are not needed in as high of doses

niacin

27

nicotinic acid can be prescribed at large doses to treat ______________________ (up to 6/day)

hypercholesterolemia

28

1) one mechanism of action for pharmacological doses of niacin to reduce lipids is: inhibition of _________________ in adipose tissue

lipolysis

29

2) another mechanism of action for pharmacological doses of niacin to reduce lipids is: decreased __________ synthesis, and thus decreased _________ production

VLDL

LDL

30

3) another mechanism of action for pharmacological doses of niacin to reduce lipids is: inhibition of diacylglycerol _______________________

acyltransferase

31

4) another mechanism of action for pharmacological doses of niacin to reduce lipids is: increase in _________ levels

HDL

32

note that niacin is not really used anymore b/c __________ are so much more effective now and safer than they used to be

statins

niacin in large amounts can result in vasodilatory effects- flushing (burning, tingling, itching sensations accompanied by red flush on face, arms, and chest); GI symptoms; liver injury; hyperuricemia or gout; glucose intolerance; blurred vision

33

one of the consequences of niacin deficiency is _______________, meaning "rough skin"

pellagra

- the 4 D's result from pellagra are: dermatitis, dementia, diarrhea, death

34

do not forget, B6 is needed for conversion of tryptophan to niacin, but the conversion is not very efficient; only about ____% of tryptophan in the diet gets converted to niacin - very tiny amount

7%

35

biotin is found in many foods: beef, soybeans, egg yolk, cereals, nuts; also made by _______________ in large intestine

bacteria

36

___________ in raw egg whites binds to biotin, thus blocking its absorption, but this compound is heat liable so it gets destroyed in when cooked

avidin

37

this biotin-dependent carboxylase converts pyruvate into oxaloacetate; it replenishes oxaloacetate for TCA cycle/gluconeogenesis

pyruvate carboxylase

38

this biotin-dependent carboxylase makes malonyl coA from acetyl coA; it commits acetyl coA to fatty acid synthesis

card image

acetyl coA carboxylase

39

this biotin-dependent carboxylase converts propionyl coA into methylmalonyl coA; important in metabolism of amino acids and odd numbered FAs

propionyl coA carboxylase

40

this biotin-dependent carboxylase converts B-methylcrotonyl coA in B-methylglutaconyl coA; important in catabolism of leucine and isoprenoid compounds

B-methylcrotonyl coA carboxylase

41

1) one non-coenzyme role of biotin is the __________________ of proteins (histones)

biotinylation

(adds biotin to the protein group)

42

2) another non-coenzyme role of biotin is to stimulate the expression of ____________________

glucokinase

(glucokinase enzyme either phosphorylates or dephosphorylates -add/removes phosphorous- glucose molecules)

43

3) another non-coenzyme role of biotin is to inhibit expression of phosphoenolpyruvate _________________

carboxykinase

44

4) another non-coenzyme role of biotin is that it is important for normal progression of the _________ ____________

cell cycle

45
card image

what is this?

- the structure of biotin

46
card image

what is this showing?

how biotin attaches to a carboxylase through an amide linkage to form a biotinylated carboxylase

47

in pantothenic acid, "pantos" means ___________________ in Greek b/c anything that has a coA attached to the name means that it contains pantothenic acid

card image

everywhere

48

What are the two primary cofactor forms of pantothenic acid?

coA and 4-phosphopantetheine

49

coA binds to __________ groups via a thio (sulfur) ester bond with carboxylic acid and transfers the __________(same as blank above) groups as needed

acyl

acyl

50

ex: the carboxylic acid of acetyl coA is ___________ __________, to which then the coA gets attached

acetic acid

51

malocnic acid becomes ____________ _________, propionic acid becomes _____________ __________, and succinc acid becomes _____________ __________

malonyl coA

proponyl coA

succinyl coA

52

the prosthetic group for acyl carrier protein (ACP) is required in what process?

FA synthesis

53

the sulfhydryl group in 4'-phosphopantetheine binds and transfers ___________ groups to another sulfhydryl group located in the enzyme complex

acyl

54

ex: first, malonyl coA binds binds to 4-P-pathetheine and on a second step, it is transferred to the enzyme complex via _________

card image

ACP

-this is why pantothenic acid is so important for fat metabolism

55

____________________ refers to donation of long-chain fatty acids or acetate to proteins

acetylation

56

________________: shorter chains of carbons

________________: can be longer chains of carbons

acetylation

acylation

57

What is the most common form of pantothenic acid in the body?

coenzyme A (coA)

58

what is the major form of vit B6 in the body?

PLP

59

B6 has everything to do with ________________ metabolism

protein

60

Which enzymes require vit B6 as a cofactor and what are their functions?

card image

more than 100 coenzymes require B6

61

this role of the vitamin that is thought to account for the use of more than 50% of body’s vitamin B6 (most common role in muscle)

glycogen degradation

most of the B6 found in muscle is present as PLP, which in turn is bound to glycogen phosphorylase

62

vitamin B6 is absolutely necessary for heme synthesis because it is a cofactor for ______________ synthase; without this enzyme, heme cannot be made

ALA synthase

63

without enough B6, RBCs become small and contain low levels of ________________________, which is necessary for oxygen transport throughout the body

hemoglobin

64

_____________ ______ and glycerin are the beginning of heme. B6 is necessary for heme formation, and with a deficiency, anemia can occur

card image

succinyl coA

(heme is what gives the cell its bright color because t is carry oxygen for/in the blood)

65

1) this coenzyme role of B6 plays in the transfer of an amino group (-NH2) from one amino acid to an alpha keto acid and is an important reaction for the synthesis of nonessential amino acids and for the use of amino acid carbon skeletons for energy or glucose production:

transamination

66

the two most common amino transferases for which PLP or PMP (B6) is coenzyme for are:

GOT (glutamate oxaloacetate transferase; aka aspartic amino transferase, AST) - this aminotransferase found in higher concentration in the heart

GPT (glutamate pyruvate transaminase; aka alanine aminotransferase, ALT) - this aminotransferase found in higher concentration in the liver

67

PLP (B6) is especially important in muscle so that muscle can convert glutamate to glutamine and alanine to pyruvate (remember muscle will not give up _______________, only AA)

glucose

68

PLP is also involved in ______________________, the removal of an amino group

deamination

69

2) this coenzyme role of B6 plays in the removal of the carboxyl (COO-) group from an amino acid or other compound; neurotransmitter synthesis (ex, production of serotonin):

decarboxylation

70

3) this coenzyme role of B6 plays in the irreversible break down of homocysteine to cysteine; the reactions in this process require two PLP enzymes:

transulfhydration

71

related to transulfhydration, if you have a deficiency in B6, what will there be a rise in?

homocysteine

72

4) this coenzyme role of B6 plays in the reaction in which an amino group is removed from a compound such as an amino acid and released as ammonia or ammonium ion:

deamination

73

5) this coenzyme role of B6 plays in the removal of a hydroxymethyl group from serine:

cleavage

74

the purpose of iodine is really to make ______________ hormones

thyroid

75

for the synthesis of the thyroid hormone T4 (thyroxine), how many iodide atoms are needed?

4 (T4)

76

for the synthesis of the thyroid hormone T3 (triiodothyronine), how many iodide atoms are needed?

3 (T3)

77

this is the hormone that regulates thyroid hormone synthesis and secretion

TSH (thyroid stimulating hormone)

secreted from pituitary, then sends signal to thyroid to produce more T3 or T4

78

true/false

the thyroid makes more T4 than T3

true! (50-100x's more)

79

how are thyroid hormones formed?

step 1) iodide is ______________ transported into the cell

card image

actively

80

how are thyroid hormones formed?

step 2) iodide gets attached to a _______________________ and forms Thg-MIT

card image

thyroglobulin

81

how are thyroid hormones formed?

step 3/4) Thg-MIT is iodinated to form Thg-DIT, which condenses with another Thg-DIT in the colloid to form _____________

card image

Thg-T4

82

how are thyroid hormones formed?

step 5) Thg-DIT also can condense with ____________ to form Thg-T3 and reverse (r)T3

card image

Thg-MIT

83

how are thyroid hormones formed?

step 6) T4 and T3, now active thyroid hormones, are released into the blood following ______________________ of Thg-T3 and Thg-T4 back into the thyroid cell and hydrolysis of the Thg by proteases

card image

endocytosis

(engulfing the whole thing)

84

thyroid hormones play a vital role in expending energy. what does this mean?

oxygen consumption

85

_______ is the most biologically active thyroid hormone

T3

86

the function of thyroid hormone is mediated through effects in the ______________ of cells

nucleus

87

thyroid hormones bind to __________ or interact with it via zinc fingers to increase mRNA expression and _______________ synthesis to:

- stimulate _____________ consumption

- increase __________ ________________ __________

- increase body __________ production

DNA

protein

oxygen

basal metabolic rate (BMR)

heat

88

in adipose tissue, thyroid hormones do what?

enhance lipolysis

89

in muscles, thyroid hormones do what?

enhance contraction

90

in the bone, thyroid hormones do what?

promote anabolism (growth and development)

(anabolism expends energy)

91

in the cardiovascular system thyroid hormone does what?

increases heart rate

92

in the gastrointestinal tract, thyroid hormone does what?

stimulates nutrient digestion and absorption

93

for metabolism, thyroid hormone does what?

stimulates metabolic rate and cellular oxygen consumption in metabolically active tissue

94

this vitamin has the second highest intracellular concentration

magnesium (Mg)

(the first is K)

95

magnesium is protein-bound primary to this protein: _______________

albumin

96

magnesium is mostly found associated with ____________

what percentage?

bone

50-60%

97

magnesium is associated with phosphorus and calcium to form the ________________ ________________ during bone formation

crystal lattice

98

magnesium is also important on the ________________ of bone; it is thought to contribute to an exchangeable pool to maintain blood levels

surface

99

magnesium is also found in _____________________ fluids, primarily skeletal muscle

extracellular

100

magnesium is bound to ______________________ in cell membranes for stabilization

phospholipids

101

* Mg allows smooth and and cardiac muscle ______________________ (Ca ions exchange)

contractility

- ratio affects muscle contraction

102

Mg is associated with DNA and proteins how? (2 ways)

nucleic acid synthesis

AA activation

103

Mg is also a cofactor in over ________ enzyme reactions, two of which are:

300

cAMP

insulin cascade

104

* Mg is also associated with ATP in which pathways? (4)

glycolysis, TCA, HMP shunt, beta-oxidation

105

Mg is part of the tyrosine kinase activity at the ______________ receptor

insulin

106

the major form of choline in foods is as the ______________________ ______________

phospholipid lecithin

107

Choline is primarily found in the body in the form of ________________

lecithin

108

in the brain, kidneys, and liver, lecithin gets cleaved by phospholipase C yielding a __________________ and _________________________

diglyceride

phosphorylcholine

109

alkaline phosphatase cleaves the phosphate yielding free ______________

card image

choline

110

how does choline help decrease homocysteine levels?

free choline can be oxidized to betaine which serves as a methyl donor to homocysteine to generate methionine

111

which two enzymes work in oxidizing betaine?

card image

choline dehydrogenase

betaine aldehyde dehydrogenase

112

free choline also has 2 other functions:

phosphorylation

acetylation

113

remember, choline can be synthesized in the body by methylation of _______________ by SAM

serine

114

what does the K in vitamin K mean?

koagulation (coagulation)

115

true/false

vit K is one of the few vitamins that is more bio-available in plant sources than animal

true!

116

since vitamin K is a fat-soluble vitamin, where do you think most of our vit K is found?

cell membranes

117

what is the primary function of vitamin K?

blood clotting cascade!

118

all glutamic acid residues must be carboxylated for the protein to function. which K-dependent protein does this?

Gla γ-carboxyglutamate

119

vitamin K really just allows _____________ to be able to attach to proteins to be used for bone mineralization and blood clotting

card image

calcium

120

_____________________________ residues on major proteins for the blood clotting cascade; includes prothrombin (factor II), factor VII, IX, and X-formation of fibrin clot

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y-carboxyglutamate

121

calcium in needed for the blood clot; vit K allows for the ________-________ to form, so then calcium can "fit" in this and be utilized

COO-COO

122

1) in the vitamin K cycle, vitamin K is first present in blood in its ________________ form (vit K quinone)

oxidized

123

2) in the vit K cycle, vitamin K quinone (oxidized) must be reduced by _________________ __________________ to work in carboxylation (dihydroquinone, KH2)

quinone reductase

124

3) in the vit K cycle, ______________________ of proteins leads to formation of vitamin K 2,3-epoxide

γ-carboxylation

125

4) in the vit K cycle, vitamin K quinone is reformed by ________________ _________________

epoxide reductase

126

the whole purpose of the vitamin K cycle is so that other proteins involved in blood clotting and bone mineralization can be _______________________

carboxylated

127

what is the mechanism of action of warfarin?

warfarin affects all of the vit K-dependent clotting factors

this means that warfarin inhibits blood clots (it is an anticoagulant); useful for decreasing death for those who are at risk for recurrent myocardial infarction, thromboembolic events (stroke, systemic embolization), or artificial heart valve replacement

128

folate must have all three of these parts to be folate

card image

1) pterin

2) PABA

3) glutamic acid (can be more than 1)

-aka THF when it is reduced

129

what are the different cofactors of folate and what are their functions?

1)

B12 - needed so the methyl from 5-methyl THF can donate its methyl to cobalamin (B12) to make methylcobalamin, which is the methyl donator to Hcy (homocysteine)

130

what are the different cofactors of folate and what are their functions?

2)

riboflavin (B2) - cofactor for methylene THF reductase (accepts reducing equivalents from NADPH)

131

what is the methyl folate trap?

the methyl-folate trap is when there is not enough B12 to keep regenerating THF in the cells; essentially, the "trap" occurs when there is not enough cobalamin (B12) to take the methyls off of the 5-methyl THFs , and thus a buildup of 5-methyl THF occurs and cannot be converted to THF

132

how can an excess of folic acid mask a vitamin B12 deficiency?

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excess folate/folic acid can mask a vitamin B12 deficiency by correcting megaloblastic macrocytic anemia, but neurological damage form lack of B12 still occurs and is irreversible; when there are large amounts of folate in the diet, the body does not need B12 to regenerate THF; thus, the high folate consumption can still produce DNA and correct macrocytic anemia, but there is still that B12 deficiency being masked

133

what is the role of the enzyme methylene tetrahydrofolate (THF) reductase (MTHFR)?

converts 5,10 methylene to 5 methyl THF, which requires FAD

this enzyme is necessary for remethylation of Hcy

134

what would happen if there were a defect in MTHFR?

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high homocysteine!; cannot methylate homocysteine to methionine

135

what does methotrexate do?

inhibits dihydrofolate reductase (DHFR) which keeps DNA from being divided; thus, methotrexate inhibits the whole step of utilizing THF

136

related to the article about folate, what types of supplements would be indicated for patients taking methotrexate and why?

card image

5-MTHF would be a good supplement because

1) the DHFR-catalyzed reaction would reach saturation easily (this run allows DNA to be divided) and

2) 5-MTHF does not mask a vitamin B12 deficiency like folic acid supplements might

137

what kind of anemia can result from a folate deficiency?

megaloblastic macrocytic anemia

(megaloblastic = odd oval shape with distorted nuclei; macrocytic = large; high mean cell volume (MCV))

* cells divide later, and when that happens they have more time to become larger (so what you see is a macrocytic -large- RBCs); these larger cells are a key clue to folate or B12 deficiency; this is for CELL DIVISION (not color - that’s heme)

138

why is B12 called methylcobalamin?

the Co (cobalamin) in the middle of the molecule

139

what changes in the different forms of B12?

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CN group

140

synthetic B12 in fortified foods in fortified foods is not bound to _________________

protein

141

digestion: naturally occurring B12 in food is bound to ________________, and must be released from this for absorption

protein

142

_______________ acid (HCl) is essential for breaking B12 off of protein

gastric

143

absorption: ______________ helps with HCl to break down the protein to release the B12, then it is attached to another protein called "______" protein

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pepsin

R

144

in the duodenum, R protein is hydrolyzed and free _________________ results

cobalamin

145

cobalamin binds to ________________ factor (IF) after release from R protein thus forming IF-B12 complex

intrinsic

146

______________ complex traverses entire length of small intestine

IF-B12 complex

147

in the ilium, IF-B12 is absorbed via binding with receptors known as ________________

cubilins

(these are the proteins that cabolamin binds to once in the ileum)

148

finally, ________________ ________________ occurs equally throughout GI

only about 1-2% of oral dose is absorbed of cobalamin

passive diffusion

149

this is a picture of cobalamin digestion/absorption

card image

nice

150

how does vitamin B12 work with folate?

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vitamin B12 accepts the methyl group from 5-methyl THF

151

what is the role of the enterohepatic circulation in maintaining vitamin B12 status?

B12 gets reabsorbed with bile; so B12 can be secreted with bile and then be re-absorbed again

-this is the reason that a B12 deficiency develops more rapidly in individuals who malabsorb (pernicious anemia) vs those who consume vegetarian diet

152

What kind of anemia can result from a B12 deficiency?

1)

pernicious anemia - caused by lack of functional IF in stomach; can't absorb B12 b/c do not have intrinsic factor (autoimmune destruction of gastric parietal cells)

153

another anemia resulting from B12 deficiency

2)

megaloblastic macrocytic anemia

- when not enough B12 to accept methyl from 5-methyl THF, causes RBCs to divide later, which allows RBCs to have more time to become larger in size, resulting in the above anemia

154

which enzymes require zinc (Zn) as a cofactor?

component of metalloenzymes

includes carbonic anhydrase, alcohol dehydrogenase (alcohols to aldehydes, ex: retinol-> retinal), carboxypeptidases (protein digestion), superoxide dismutase (free radical terminator)

155

how does zinc affect gene expression?

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zinc fingers stabilize the folds in genes

156

what is the function of chromium (Cr)?

potentiation of the action of insulin via chromodulin

157

____________________ is produced in response to insulin secretion which stimulates Cr uptake by beta cells

chromodulin

158

chromodulin binds to the cytosolic beta subunits of the insulin receptor and stimulates ____________ activity

kinase

159

chromium is mostly bound to ___________________, but if transferrin is not available because of binding to iron, it may bind to other proteins

transferrin

160

what are the enzymes that require iron as a cofactor?

cytochromes

monooxygenases

deoxygenases

thyroperoxidase

catalase

myeloperoxidase

161

this iron protein absorbs intact heme in the duodenum

Hep1

162

this iron protein is the transporter for ferrous iron; located everywhere in the body

DMT1

synthesis of DMT1 is affected by iron status (increased synthesis with low status, decreased expression with increased enterocyte iron concentration)

163

this iron protein transports iron to the basalateral membrane and out of the intestinal cell

ferroportin

164

this iron protein oxidizes ferrous iron to ferric iron when transport out of intestinal cells occurs

hephaestin

165

this iron protein is critical for iron transport by transferrin (transferrin transfers oxidized state of iron); works as an antioxidant to eliminate free radicals produced by phagocytosis of invading organisms by WBCs; also called acute phase protein b/c its concentration increases in blood during inflammatory response; 6 copper atoms get attached to this protein (it is the primary form of circulating Cu, 60-70%); this protein delivers Cu to tissues after binding to specific membrane receptors

ceruloplasmin

166

transports the ferric iron (oxidized iron) that was converted by hepaestin; most of the iron transported by this enzyme comes from degradation of hemoglobin

transferrin

167

this is an iron storage protein, specifically stores broken-down iron; predominates over ferritin under high iron concentrations

hemosiderin

168

this iron protein binds up to 3 iron atoms in the intestinal cell so that the iron is prevented from oxidative damage; chaperone for iron

PCB1

169

this iron protein travels through blood to target intestinal cells and macrophages; binds to ferroportin leading to degradation; "deletes" extra iron when too much intracellular iron

hepcidin

170

these (two of them) iron protein remove free hemoglobin and heme from blood and transport them to the liver

haptoglobin and hemopexin

171

this iron protein is the major storage protein; stores iron in ferric ion state (Fe3+)

ferritin

172

this iron protein is another chaperone for iron

steap3

173

what are the characteristics of iron deficiency anemia?

Iron-deficient anemia causes serum iron and serum ferritin to plummet and serum transferrin to raise dramatically. Without enough iron and stores of iron (ferritin), transferrin (the major transporter of iron) raises because it is so desperately searching for iron to transport around in the body.

174

what are the early signs of iron deficiency as compared to late signs?

1) decrease in iron stores

2) decrease in circulation iron

3) free protoporphyrin concentrations in RBC and transferrin receptors rise

4) anemia

175

helpful chart

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okay. praise Jesus, we are complete finally