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Clinical Science > Quiz 2: Iron > Flashcards

Quiz 2: Iron Flashcards

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1
Q

What part of hemoglobin binds oxygen?

A

Heme group

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2
Q

Each hemoglobin can bind to how many O2 molecules?

A

4

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3
Q

Iron deficiency is called?

A

Anemia

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4
Q

Iron overload is called?

A

Hemochromatosis

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5
Q

What is the most common cause of anemia in infants, children, and premenopausal women?

A

Iron deficiency

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6
Q

Iron studies are usually performed after what test?

A

Abnormal CBC

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7
Q

What two terms are used to describe the typical iron deficient anemia?

A

Microcytic and hypochromic

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8
Q

Should you rely on serum iron alone?

A

Nope, iron levels can vary due to time of day

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9
Q

When are iron levels usually higher?

A

Morning

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10
Q

How does stress impact iron levels?

A

Decrease iron levels

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11
Q

What medications can alter iron levels?

A

antibiotics, hormones, hypertension medications, cholesterol medications, deferoxamine

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12
Q

What does deferoxamine do?

A

Removes excess iron from the body

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13
Q

What conditions are associated with increased iron levels?

A

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

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14
Q

What is the mechanism of iron impact in alcoholic cirrhosis?

A

Ferritin, the storage form of iron, is stored in liver. When liver is damaged, iron is released to circulation.

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15
Q

What is the mechanism of iron impact in hereditary hemochromatosis?

A

HFE gene, impaired iron detection and regulation

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16
Q

What are the various CATEGORIES for decreased iron levels?

A

iron deficiency anemia, renal disease, inadequate absorption, increased loss, increased demand

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17
Q

Examples of inadequate absorption that lead to decreased iron levels?

A

antacid use, competition with other metals, bowel resection, celiac disease, inflammatory bowel disease

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18
Q

Examples of increased loss that lead to decreased iron levels?

A

From GI tract, nose with severe epistaxis, menstruation, cancer, trauma, phlebotomy

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19
Q

Examples of increased demand that lead to decreased iron levels?

A

Pregnancy

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20
Q

What does ferritin do?

A

Serves as the storage unit for iron and responds to the increased iron needs of the body by releasing it when needed

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21
Q

What is the shape of ferritin?

A

A hollow sphere with iron stored inside

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22
Q

The iron inside ferritin is stored as?

A

Fe (III) and is oxidized to Fe (II) which allows its release through the channels of the sphere when demands occur

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23
Q

When is ferritin produced?

A

When excess dietary iron is absorbed, the body responds by producing more ferritin to facilitate iron storage. Ferritin molecules store thousands of iron atoms within their mineral core.

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24
Q

Which is more valuable: serum iron or ferritin?

A

Ferritin, it doesn’t fluctuate as much

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25
Q

What percent of the body’s iron is stored within ferritin?

A

15-20%

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26
Q

Where is ferritin stored?

A

liver, spleen, skeletal muscles, and bone marrow

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27
Q

What is an acute phase reactant?

A

Something released under times of stress, infections, or cancer

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28
Q

Is serum ferritin an acute phase reactant?

A

You bet cha’

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29
Q

What is the gold standard in the diagnosis of iron deficiency anemia?

A

Serum ferritin

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30
Q

What is serum ferritin helpful in distinguishing?

A

Iron deficiency anemia (ferritin <10 ng/mL) and anemia of chronic disease (ferritin >10 ng/mL)

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31
Q

What conditions can lead to increased ferritin levels?

A

hereditary hemochromatosis, excess iron intake/poisoning, chronic hepatitis (ferritin is leaked in circulation), alcholism

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32
Q

What conditions can lead to decreased ferritin levels?

A

iron deficiency anemia

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33
Q

What is transferrins?

A

glycoproteins that are responsible for the transport of iron

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34
Q

The daily diet contains how many mg of iron?

A

10-20 mg

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35
Q

How much iron do we absorb per day?

A

1-2 mg/day

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36
Q

How much iron do we lose from desquamation of epithelia per day?

A

1-2 mg iron/day

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37
Q

What is desquamation of epithelia?

A

Skin peeling

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38
Q

How many iron molecules can transferrin bind?

A

2 iron molecules

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39
Q

What % of transferrin binding sites are normally filled

A

33%

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40
Q

Where does transferrin transport iron to and from?

A

From the site of absorption to almost all tissues of the body

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41
Q

Where is transferrin synthesized?

A

liver

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42
Q

When does transferrin synthesis increase and decrease?

A

increases in state of iron deficiency but can decrease in infection

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43
Q

Why does transferrin increase in a state of iron deficiency?

A

Body is trying to be more productive, get all the iron onto the seats of the bus

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44
Q

Why does transferrin decrease in infection?

A

prevents transport of iron to bacteria for use

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45
Q

In response to severe or chronic infection/disease, the amount of ferritin?

A

Increases

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46
Q

Why does ferritin increase in response to severe or chronic infection/disease?

A

Because it’s an acute phase reactant

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47
Q

What is Total Iron Binding Capacity?

A

the maximum amount of iron that serum proteins, mainly transferrin, can bind to. TIBC reflects the potential for iron binding if all of the binding sites on transferrin were filled.

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48
Q

How does the Total Iron Binding Capacity test work?

A

Radioactive iron is incubated with human serum (containing trasnferrin) and the amount of radioactive iron taken up by the transferrin in the serum is measured. The radioactive iron can only bind to iron-binding sites on transferrin that are unoccupied.

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49
Q

What is the typical % of iron-binding sites the radioactive iron can bind to?

A

66%

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50
Q

In iron deficient states would TIBC be higher or lower?

A

Increased TIBC

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51
Q

In iron overload states would TIBC be higher or lower?

A

Decreased TIBC

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52
Q

Conditions with increased TIBC?

A

iron deficiency anemia, pregnancy, oral contraceptives, viral hepatitis

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53
Q

Conditions with decreased TIBC?

A

anemia of chronic diseases, hemochromatosis, sideroblastic anemia

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54
Q

What is transferrin saturation?

A

Measurement of percentage of transferrin binding sites that are ctually bound by iron

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55
Q

An increase in the transferrin saturation represents what?

A

an increase in iron absorption

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56
Q

Normally, iron occupies what % of the iron binding sites on transferrin?

A

33%

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57
Q

What is the % saturation calculation?

A

% transferrin saturation = serum iron/ TIBC

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58
Q

Abnormalities in transferrin saturation: increased

A

iron overload states, hemochromatosis

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59
Q

Abnormalities in transferrin saturation: decreased

A

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

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60
Q

What is iron deficiency anemia?

A

a deficiency of iron and resulting anemia that usually results from blood loss, poor vitamin intake, or poor absorption of iron (in small intestine). The body makes more transferrin to compensate.

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61
Q

What are your five anemia tests?

A

CBC, serum iron, serum ferritin, TIBC, transferrin staturation

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62
Q

Lab results in iron-deficiency anemia:

A

decreased: MCV, serum iron, serum ferritin, % transferrin saturation. Increased: TIBC

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63
Q

What is anemia of chronic disease?

A

anemia that occurs in the presence of long-standing chronic disease, such as cancer, kidney disease, or severe autoimmune diseases. Usually results from decreased EPO production in kidneys and production of cytokines during disease. The body produces less transferrin to keep iron away from infections that can use it.

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64
Q

Lab results of anemia of chronic disease?

A

MCV (normal in beginning and becomes decreased over time), serum iron (decreased), serum ferritin (normal or increased), TIBC (normal or low), % transferrin saturation (decreased)

65
Q

What’s the big test to tell anemia of chronic disease from iron-deficiency anemia?

A

serum ferritin

66
Q

When blood is spun what is the largest component?

A

plasma @ 55%

67
Q

What is contained in plasma?

A

91% water, 7% blood proteins, 2% nutrients, 1% hormones and electrolytes

68
Q

Three main types of plasma proteins:

A

albumins, fibrinogen, globulins

69
Q

What % of plasma proteins is albumin?

A

50-60%

70
Q

What is albumin involved in?

A

maintenance of osmotic pressure, transportation of fatty acids, hormones, drugs, and other substances

71
Q

What % of plasma proteins is globulin?

A

36%

72
Q

What are the three types of globulins?

A

alpha, beta, and gamma

73
Q

Where are alpha and beta globulins produced?

A

liver

74
Q

What do alpha and beta globulins do?

A

involved in transportation or act as substrates

75
Q

Where are gamma globulins produced?

A

lymphoid tissue

76
Q

Where is albumin synthesized?

A

liver

77
Q

What is the most important regulator of oncotic pressure within the vascular system?

A

albumin

78
Q

How is albumin synthesis regulated?

A

nutrition (protein intake) and illness

79
Q

Albumin also serves as a transporter for:

A

hormones, lipids, drugs, and many other substances

80
Q

What disease can cause albumin to spill into urine?

A

diabetes, long term high blood pressure

81
Q

Conditions leading to increased albumin levels?

A

dehydration

82
Q

Conditions leading to decreased albumin levels?

A

liver disease, malabsorption/malnutrition, abnormal loss (renal disease, GI loss, skin loss, severe burns), dilution by IV fluids

83
Q

Where is prealbumin synthesized?

A

liver

84
Q

What does prealbumin do?

A

functions as a transport protein for thyroxine and vitamin A

85
Q

Is prealbumin or albumin better at assessing a patient’s nutritional status? Why?

A

Prealbumin because it has a shorter half life and is more sensitive to rapid changes in nutrition

86
Q

Prealbumin may not be an accurate assessment of nutrition in patients with:

A

inflammation, infection, or trauma

87
Q

Prealbumin is increased in what conditions?

A

pregnancy, Hodkin’s lymphoma

88
Q

Prealbumin is decreased in what conditions?

A

renal/liver disease, malabsorption/malnutrition, eating disorders, Crohn’s disease, low protein diet, severe illness/inflammation/infection

89
Q

Alpha-1-antitrypsin is what type of globulin?

A

alpha-1-globulin

90
Q

What is the function of alpha-1-antitrypsin?

A

to inhibit the action of many key enzymes that are released during inflammatory reactions in the lungs

91
Q

Deficient or abnormal alpha-1-antitrypsin can lead to?

A

early onset COPD (damage of lung parenchyma), can also cause liver disease due to toxic accumulation of mutant alpha-1-antitrypsin in the cells of the liver

92
Q

Conditions leading to decreased/deficient alpha-1-antitrypsin?

A

COPD (often before age 40), prolonged jaundice or hepatitis in infants, liver dysfunction in children, chronic hepatitis, cirrhosis, hepatocellular carcinoma

93
Q

Where is haptoglobin produced?

A

in the liver

94
Q

What is the function of haptoglobin?

A

to bind to free hemoglobin when RBCs are destroyed

95
Q

What happens once haptoglobin is bound to hemoglobin?

A

it transports hemoglobin back to the liver where the heme is converted to bilirubin

96
Q

If there is RBC destruction, the haptoglobin becomes?

A

depleted and its levels decrease

97
Q

Haptoglobin is very useful when looking for signs of?

A

hemolytic anemia

98
Q

Hemolytic anemia can be caused by a variety of factors including:

A

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

99
Q

Conditions resulting in increased haptoglobin

A

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

100
Q

Conditions resulting in decreased haptoglobin

A

hemolytic anemia, transfusion reaction, artificial heart valves

101
Q

Is haptoglobin an acute phase reactant?

A

Duh

102
Q

What are complement proteins?

A

supplement or “complement” the action of antibodies to destroy and eliminate pathogens from the body

103
Q

The complement pathway involves how many proteins?

A

9 (C1-9)

104
Q

Generally, where are complement proteins synthesized?

A

liver

105
Q

Which complement proteins are considered acute phase reactants?

A

C3 and C4

106
Q

What is the primary function of the complement cascade?

A

to facilitate oponization of pathogens, making them “tastier” for neutrophils and allow phagocytosis

107
Q

When does the complement pathway begin?

A

When the first protein, C1, recognizes the antibody-antigen complex or when certain components of the surface of a bacteria or virus are recognized

108
Q

What happens to C3?

A

It’s cleaved, which causes inflammation and opsonization

109
Q

What is the ultimate goal of the complement pathway?

A

produce a membrane attack complex (MAC) through this pathway and insert itself into the membrane of the pathogen, causing its lysis and destruction

110
Q

The most commonly measured complement proteins are?

A

C3 and C4

111
Q

Complement levels rise by as much as ?% with many infectious and inflammatory conditions.

A

50%

112
Q

Another test used to measure complements is?

A

CH50

113
Q

Measurements of complement proteins may be useful in what conditions?

A

autoimmune diseases, recurrent infections

114
Q

CH50 is used to measure?

A

immune processes or screen for reduced complement (frequent infections)

115
Q

What does CH50 measure?

A

quantitatively mesaure the ability of human serum to lyse sheep RBCs that have been coated with antibody (when 50% of cells lysed). Measures the amount of hemolysis that occurs.

116
Q

What must be present for a normal CH50 result?

A

All nine proteins, C1 through C9

117
Q

Decreased CH50 indicate?

A

decreased complement activity

118
Q

CH50 = zero, indicates?

A

one of pathway components is totally absent

119
Q

What are C3 and C4 tests used for?

A

to investigate the undetectable CH50 level and to monitor some diseases like SLE (lupus), funcgal infections, gram negative septicemia, and shock.

120
Q

Why are C3 and C4 tests used in response to an overwhelming fungal infection?

A

Most of us don’t get fungal infections, maybe immunocompromized

121
Q

Conditions with decreased complement testing (C3,C4) ?

A

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

122
Q

Conditions with increased complement testing (C3,C4)?

A

cancer, ulcerative colitis

123
Q

What is the most significant gamma globulin?

A

Immunoglobulins (antibodies)

124
Q

What produces immunoglobulins?

A

B lymphocytes

125
Q

Are immunoglobulins specific or general?

A

Specific

126
Q

The type of immunoglobulin is determined by?

A

variation of the heavy chain

127
Q

What are the different types of immunoglobulins?

A

IgG, IgE, IgD, IgA, IgM

128
Q

Where is IgA usually found?

A

saliva, tears, colostrum, mucus

129
Q

What is IgA the defender of?

A

mucosal or epithelial surfaces against pathogens and allows for clearance of pathogens by cilia or of toxins in GI tract

130
Q

IgA deficiency can cause what symptoms?

A

None or it can cause frequent respiratory infections, inflammation of GI tract, unexplained asthma symptoms

131
Q

IgD represents ?% of circulating immunoglobulins?

A

0.25%

132
Q

IgD is found to activate?

A

basophils and mast cells

133
Q

IgD increases with?

A

chronic infections and multiple infections

134
Q

IgE is the key factor involved in:

A

allergic reactions and parasitic infections (Helminth infections)

135
Q

IgE binds to:

A

mast cells and this initiates a chain of immune responses

136
Q

What does Immunocap do?

A

It’s an allergy test which determines specific IgE antibodies against allergens

137
Q

What is the major antibody produced when an antigen is encountered?

A

IgG

138
Q

What is the most prevalent antibody in serum?

A

IgG

139
Q

Which antibody has the longest half life?

A

IgG

140
Q

The half life of IgG is?

A

23 days

141
Q

What is an example of an illness where IgG could persist and be detected for life in some cases?

A

Mononucleosis

142
Q

Which antibody can cross the placenta?

A

IgG, so that the fetus can be protected from infection

143
Q

What is the initial antibody secreted after an immune challenge with half-life of 10 days?

A

IgM

144
Q

IgM antibodies indicate?

A

Recent infection

145
Q

How to interpret IgG and IgM

A

IgM shows up first (I get Meds = I’m sick now), IgG comes in later (I already got Germs = I’m over it now)

146
Q

IgG and IgM levels are usefully for determining if?

A

someone has an active infection currently or has already had the infection in the past, but may not have realized it

147
Q

Multiple myeloma represents ?% of all hematologic cancer?

A

10%

148
Q

Neoplastic disorder usually causes proliferation of:

A

IgG and IgA

149
Q

In multiple myeloma clones of a single structurally-identical antibody multiples rapidly and now becomes labelled the:

A

M protein (monoclonal proteins)

150
Q

What is serum protein electrophoresis useful in?

A

identifying patients with multiple myeloma and other potentially malignant disorders

151
Q

Serum protein electrophoresis can be done on?

A

serum or urine

152
Q

How to interpret a protein electrophoresis:

A

albumin is the largest component of serum and represents the largest peak-closest to the positive electrode, globulins are smaller proportion (alpha1, alpha2, beta, gamma) think hang-loose with right hand

153
Q

What’s the biggest a2 component on a serum protein electrophoresis?

A

haptoglobin

154
Q

What’s the biggest B1/2 component on a serum protein electrophoresis?

A

Transferin

155
Q

What makes up the gamma component on serum protein electrophoresis?

A

IgM, IgA, IgG

156
Q

How would a serum protein electrophoresis look in multiple myeloma?

A

Big spike in gamma called M (monoclonal) protein, which usually occurs in gamma region, but can occur in the alpha-2 or beta range.

157
Q

Conditions associated with M protein on protein electrophoresis:

A

multiple myeloma, smouldering myeloma

158
Q

What does a polyclonal gammopathy look like on an electrophoresis?

A

broader based peak in the gamma region

159
Q

What conditions are associated with polyclonal gammopathy?

A

liver disease (cirrhosis or hepatitis), autoimmune disease, infection (HIV, hepatitis), hematologic disorders or malignancies (Non-Hodgkin’s lymphoma, sickle cell anemia, thalassemia), non-hematologic malignancies

Clinical Science (7 decks)

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