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Clinical Science > Lecture 8 "Iron and other proteins" > Flashcards

Lecture 8 "Iron and other proteins" Flashcards

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1
Q

What medications can alter iron levels?

A

antibiotics, birth control, estrogen, hypertension medicine, cholesterol medications, deferoxamine (removes excess iron from the body), gout medication, testosterone

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2
Q

What can increase iron level?

A

beta-thalassemia, alcoholic cirrhosis, high iron intake, hereditary hemochromatosis

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3
Q

What is the mechanism behind hereditary hemochromatosis increasing iron level?

A

HFE gene, impaired iron detection and regulation

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4
Q

How does alcoholic cirrhosis increase iron levels?

A

damage to liver leads to increased ferritin levels (iron storage)

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5
Q

What can decrease iron levels?

A

iron deficiency anemia, anemia of chronic disease, chronic renal failure, inadequate absorption, increased loss (from GI tract, nose bleeds, menstruation, cancer, trauma, phlebotomy), increased demand in pregnancy

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6
Q

What is the function of ferritin in the body?

A

it serves as the storage unit for iron

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7
Q

What allows the release of iron through the channels of ferritin when demands occur?

A

Iron is stored as Fe(III) and then it is oxidized to Fe(II) which allows the release

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8
Q

How much of the body’s iron is stored within ferritin?

A

15-20%

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9
Q

Where is ferritin stored?

A

liver, spleen, skeletal muscles, and bone marrow

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10
Q

What is an acute phase reactant?

A

when ferritin can increase in response to liver disease, cancer, inflammation, and infection

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11
Q

What is the gold standard in diagnosing iron deficiency anemia?

A

serum ferritin

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12
Q

What can cause increased ferritin?

A

hereditary hemochromatosis, excess iron intake/poisoning, chronic hepatitis, other chronic disease states (cancer, alcoholism)

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13
Q

What can cause decreased ferritin?

A

iron deficiency anemia

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14
Q

What are transferrin’s?

A

they are glycoproteins that are responsible for the transport of iron

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15
Q

How many iron molecules can transferrin bind?

A

2 iron molecules

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16
Q

How many transferrin binding sites are typically filled?

A

33%

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17
Q

Where is transferrin synthesized?

A

transferrin is synthesized in the liver and synthesis increase in a state of iron deficiency

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18
Q

What is total iron binding capacity?

A

The maximum amount of iron that serum proteins, mainly transferrin, can bind to. TIBC represents the potential from iron binding if ALL of the binding sites on a protein were filled.

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19
Q

What factors increase total iron binding capacity?

A

iron deficiency anemia, pregnancy, oral contraceptives, viral hepatitis

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20
Q

What factors decrease total iron binding capacity?

A

anemia of chronic disease, hemochromatosis, sideroblastic anemia

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21
Q

What is transferrin saturation a measurement of?

A

a percentage of the transferrin binding sites that are actually bound by iron

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22
Q

What causes increased transferrin saturation?

A

megaloblastic anemia, sideroblastic anemia, iron overload status, hemochromatosis

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23
Q

What causes decreased transferrin saturation?

A

iron deficiency anemia, chronic infection, malignancy, pregnancy, anemia of chronic disease

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24
Q

What are the components of plasma?

A

a large majority is water, the blood proteins (globulin, fibrinogen, albumin), nutrients (amino acids, lipids, sugars), and hormones and electrolytes

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25
Q

What are the different types of globulins?

A

alpha and beta globulins- produced by the liver and are involved in transportation or act as substrates
gamma globulins- produced by lymphoid tissue involved in immune system

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26
Q

What are some purposes Albumin serves?

A

Functions as the most important regulator of oncotic pressure within the vasculature system. Can also serve as a transporter for hormones, lipids, drugs and other substances.

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27
Q

What causes increased albumin levels?

A

dehydration

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28
Q

What causes decreased albumin levels?

A

liver disease, malabsorption, malnutrition, dilution by IV fluids, genetic variations and congenital causes, abnormal loss from renal disease, GI loss, Skin loss, severe burns

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29
Q

What is the function of alpha-1-antitrypsin?

A

It inhibits the action of many key enzymes that are released during inflammatory reactions in the lungs.

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30
Q

What is an example of an Alpha-1 globulin?

A

Alpha-1-antitrypsin

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31
Q

What are some deficient alpha-1-ntitrypsis manifestations?

A

chronic obstructive lung disease in adults, prolonged jaundice or hepatitis in infants, live dysfunction in children, portal hypertension, chronic hepatitis, cirrhosis, hepatocellular carcinoma

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32
Q

Where is ceruloplasmin made and what is its function?

A

it is made in the liver and is involved in copper transport within the body

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33
Q

What is an example of an alpha-2 globulin?

A

ceruloplasmin –> contains 6 or seven copper atoms

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34
Q

What causes increased ceruloplasmin?

A

oral contraceptives, first trimester of pregnancy, infections

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35
Q

What is the function of haptoglobin?

A

it is produced in the liver and its function is to bind to free hemoglobin when RBCs are destroyed.

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36
Q

What happens once haptoglobin is bound to hemoglobin?

A

It transports hemoglobin back to the liver where the heme is converted to bilirubin.

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37
Q

What happens to haptoglobin when there is an increase in RBC destruction?

A

The haptoglobin becomes depleted and its levels decrease.

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38
Q

What can cause hemolytic anemia?

A

hereditary abnormalities that cause increased RBC destruction, pathogens, infection, inflammation, and toxins

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39
Q

What can cause increased haptoglobin levels?

A

infection, inflammation, neoplastic disease, pregnancy, trauma, acute MI

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40
Q

What can cause decreased haptoglobin levels?

A

hemolytic anemia, transfusion reaction, artificial heart valves

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41
Q

What is the function of complement proteins?

A

they supplement the action of antibodies to destroy and eliminate pathogens from the body

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42
Q

Which complement proteins are considered acute phase reactants?

A

C3 and C4

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43
Q

When does the complement pathway begin?

A

The cascade begins when the first protein, C1, recognizes an antibody-antigen complex or when certain components of the surface of a bacteria or virus are recognized.

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44
Q

In the complement pathway what causes inflammation and opsonization?

A

When C3 is eventually cleaved.

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45
Q

What is the ultimate goal of the complement pathway?

A

to produce a membrane attack complex (MAC) and insert itself into the membrane of the pathogen, causing lysis and destruction

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46
Q

What is opsonization?

A

it is the coating of bacterial surfaces which enhances phagocytosis

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47
Q

When may complement levels be reduced?

A

in any disease that has an increased level of circulating immune complexes or autoimmune antibodies

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48
Q

When may measurement of complement proteins be useful?

A

in autoimmune diseases such a lupus or recurrent infections.

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49
Q

What is the CH50 test used for?

A

to measure immune processes or to detect complement deficiency

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50
Q

What is needed in order to have a normal CH50 test result?

A

all nine proteins C1-C9 must be present

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51
Q

When are C3 and C4 tests primarily used?

A

used to investigate the undetectable CH50 level

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52
Q

When can C3 and C4 tests be used?

A

used to monitor some disease such as SLE(lupus). also tested in the presence of certain fungal infections, gram negative septicemia, and shock

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53
Q

When can complement testing (C3,C4) levels be decreased?

A

systemic lupus erythematosus, bacterial infections, cirrhosis, hepatitis, malnutrition

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54
Q

When can complement testing (C3,C4) levels be increased?

A

cancer, ulcerative colitis

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55
Q

What produces immunoglobulin’s?

A

B lymphocytes that then become very specific against individual infections or foreign agents

56
Q

Where is IgA typically found?

A

found in secretions along the mucosal epithelium

57
Q

How does IgA allow for clearance of pathogens?

A

allows for clearance of pathogens by cilia or of toxins in the GI tract

58
Q

Where is IgA present?

A

present in saliva, tears, colostrum, and mucus

59
Q

What can IgA deficiency cause?

A

no symptoms can present or it can cause frequent respiratory infections, inflammation of GI tract, or unexplained asthma symptoms

60
Q

What is IgD found to activate?

A

basophils and mast cells

61
Q

When can concentration of IgD increase?

A

with chronic infections

62
Q

What is IgE involved in?

A

key factor involved in allergic reactions and parasitic infections

63
Q

What is the purpose of an Immunocap?

A

it can determine specific IgE antibodies against allergens such as dog, cat, dust mites, food, etc…. can also give a total IgE count

64
Q

What is the most prevalent antibody in serum?

A

IgG… it also has the longest half life of 23 days

65
Q

What is IgG responsible for?

A

responsible for immunity to bacteria and other microorganisms

66
Q

What do IgM antibodies typically detect?

A

usually indicate recent infection

67
Q

When are IgG and IgM testing commonly used?

A

Epstein Barr Virus, Cytomegalovirus, Herpes I/II testing, Varicella, measles, mumps, rubella

68
Q

What is multiple myeloma?

A

a neoplastic disorder which causes proliferation of a monoclonal immunoglobulin, typically IgG and IgA

69
Q

What parameters of the CMP measure electrolyte function and abnormalities?

A

sodium, potassium, chloride, CO2, anion gap, calcium

70
Q

What parameters of the CMP measure renal function?

A

BUN and creatinine

71
Q

What CMP parameters measure liver function?

A

bilirubin, alkaline phosphate, AST, ALP

72
Q

What are some reasons why someone would order a CMP?

A

with abdominal pain to check for elevated liver enzymes and renal dysfunction… to evaluate abnormalities of glucose in diabetes… to evaluate potassium and renal function in the treatment of hypertension… to evaluate for liver dysfunction or liver toxicities with medication

73
Q

What is the ICF predominantly comprised of?

A

potassium

74
Q

What is the ECF predominantly comprised of?

A

sodium

75
Q

How does the body maintain sodium homeostasis?

A

by regulating water intake and excretion in the kidneys

76
Q

What hormones regulate sodium?

A

mainly antidiuretic hormone (ADH), aldosterone, naturietic hormone

77
Q

What detects a increase in osmotic pressure?

A

Osmoreceptors

78
Q

What detects a decrease in blood pressure?

A

baroreceptors (aortic arch, carotid sinus)

79
Q

How can hypernatremia occur?

A

can result from increased sodium intake or increased water loss… but the body releases ADH and thirst in response

80
Q

What is the intracellular concentration of potassium?

A

150 mEq/L

81
Q

What is the concentration of serum potassium?

A

4MEq/L

82
Q

What factors can increase potassium levels?

A

increased dietary or IV intake, crush injuries or infection, acidotic states

83
Q

What factors decrease potassium levels?

A

deficient dietary or IV intake, fluid and electrolyte loss, alkalotic states, diuretics

84
Q

What controls glucose levels?

A

glucagon and insulin

85
Q

What hormones influence glucose levels?

A

adrenocorticosteroids, ACTH, epinephrine, growth hormone, thyroxine

86
Q

What factors affect glucose levels on a CMP?

A

stress, pregnancy, glucose-containing IV fluids, some medications

87
Q

What factors can increase glucose levels?

A

diabetes, acute stress response, pancreatitis, certain diuretics, corticosteroid therapy

88
Q

What factors can decrease glucose levels?

A

insulinoma (insulin secreting tumor), insulin overdose, starvation, hypothyroidism

89
Q

What is the main filtering structure in the kidney?

A

glomerulus

90
Q

Where does Urea formation occur?

A

occurs in the liver as a result of the catabolism of protein into amino acids -> free ammonia is formed in the process

91
Q

What does BUN overall represent?

A

the metabolic functioning of the liver and excretory function of the kidneys

92
Q

When can there be an increase in blood urea nitrogen?

A

high protein diets, gastrointestinal bleeding, dehydration, certain medications, sepsis

93
Q

When can there be a decrease in blood urea nitrogen levels?

A

primary liver disease/failure, low protein diets, over hydration

94
Q

What is creatinine?

A

a byproduct of catabolism of creatine phosphate which is involved in the contraction of skeletal muscles

95
Q

Where is creatinine filtered?

A

filtered by the glomerulus of the kidney

96
Q

What is creatinine values typically used for?

A

used with the BUN to obtain information about functioning of kidneys and the GFR

97
Q

What is creatinine production dependent on?

A

muscle mass

98
Q

What can increase creatinine levels?

A

disorders of renal function, urinary tract obstruction, diabetic nephropathy, rhabdomyolysis, gigantism, acromegaly

99
Q

What can decrease creatinine levels?

A

debilitation, decreased muscle mass

100
Q

Where is calcium more abundant?

A

more abundant in the ECF than the ICF

101
Q

What is calcium most involved in?

A

muscle contraction, cardiac function, neural transmission, clotting cascade

102
Q

What are the three forms of calcium in the body?

A

protein bound 40%, complexed 12%, and ionized 48%

103
Q

What are the protein bound types of calcium?

A

mostly albumin, but also to alpha, beta 1&2, gamma globin

104
Q

What are the complexed types of calcium?

A

w/ phosphate, citrate, bicarbonate, sulfate

105
Q

What are the ionized types of calcium?

A

free calcium in its active form

106
Q

What regulates calcium?

A

parathyroid hormone (PTH), which is secreted by the parathyroid glands which are located on the thyroid gland

107
Q

What happens as calcium levels decrease?

A

PTH is released and calcium is reabsorbed by the kidneys, released from bone and absorption from GI tract is increased

108
Q

What other test should be ordered if a person had elevated calcium levels?

A

Ionized calcium (unaffected by albumin protein levels), PTH, check albumin level

109
Q

What factors can increase calcium levels?

A

hyperparathyroidism, vitamin D intoxication, tumors, acromegaly

110
Q

What factors can decrease calcium levels?

A

hyperparathyroidism, vitamin D deficiency, hypoalbuminemia, malabsorption

111
Q

What is bilirubin a component of?

A

bile

112
Q

Where is bilirubin typically formed?

A

typically the spleen and reticuloendothelial system

113
Q

What is unconjugated bilirubin?

A

when heme is catabolized and forms biliverdin which then becomes bilirubin… before in the liver

114
Q

What is conjugated bilirubin?

A

once in the liver the bilirubin is conjugated with glycuronide

115
Q

What is indirect bilirubin?

A

unconjugated

116
Q

What is direct bilirubin?

A

conjugated

117
Q

What occurs when bilirubin levels are too high?

A

jaundice can occur when total serum bilirubin levels exceed 2.5 mg/dL

118
Q

What is a negative effect of unconjugated bilirubin?

A

it can pass through the blood brain barrier so if levels are too high and stay high mental retardation and encephalopathy can occur ( >15 mg/dL is critical)

119
Q

What are some causes of indirect hyperbilirubinemia?

A

hepatocellular dysfunction (hepatitis, cirrhosis, neonatal hyperbilirubinemia), any disease that increases RBC destruction (transfusion reactions, sickle cell anemia, hemolytic anemia), many medications

120
Q

What are some causes of direct hyperbilirubinemia?

A

gallstones, obstruction of extra hepatic ducts by tumor or other cause, liver metastases (obstruction)

121
Q

What are the main components of serum protein?

A

albumin: most abundant

globulins

122
Q

How does renal disease affect serum protein levels?

A

the glomerulus becomes less able to filter proteins and overwhelms the ability of the renal tubules to reabsorb protein -> leads to loss of protein in urine

123
Q

What factors cause hyperproteinemia?

A

dehydration, malignancy, infection

124
Q

What factors cause hyperproteinemia?

A

hepatic failure or disease, malnutrition states, malabsorption states, renal failure of disease

125
Q

What are the functions of albumin?

A

important regulator of osmotic balance between intravascular and interstitial spaces (albumin pulls water into circulatory system)… act as transporter for drugs, bilirubin, thyroid hormones, and other hormones or enzymes

126
Q

Why is albumin a poor indicator of nutrition status?

A

because it has a long half life… pre-albumin is better

127
Q

What factors can increase albumin levels?

A

dehydration due to concentration of albumin

128
Q

What factors can decrease albumin levels?

A

malnutrition, pregnancy, hepatic disease or failure, protein-losing nephropathies

129
Q

What enzymes are included in a CMP to test liver function?

A

alkaline phosphate ALP, aspartate aminotransferase AST, alanine aminotransferase ALT

130
Q

When can liver function tests have abnormalities?

A

when there is injury to hepatocytes from alcohol, metabolic disorders, or medications

131
Q

What is the function of Alkaline Phosphotase?

A

functions in growth and development of bones, teeth and many other tissues -> essential for bone mineralization

132
Q

Where are the highest concentrations of ALP?

A

liver, biliary tract, bone

133
Q

When is ALP increased? pertaining to liver disorders

A

cirrhosis of the liver, obstruction of the biliary tract, live tumors, drugs that are toxic to liver

134
Q

When is ALP elevated? pertaining to bond disorders

A

cancers that metastasize to the bone, primary cancer of the bone, post-fracture, hyperparathyroidism, growing children

135
Q

Where is aspartate aminotransferase found in the body?

A

in metabolic tissue such as heart, liver, skeletal muscle -> if damage occurs in an of these tissues AST is released into circulation and its level increases

136
Q

When is AST elevated?

A

liver disease, tumors involving the liver, infectious mononucleosis, skeletal muscle disease or trauma (burns, myositis, muscular dystrophy)

137
Q

When is Alanine aminotransferase increased?

A

myositis, myocardial infarction, hepatotoxic drugs, cirrhosis, hepatitis

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