RBC Structure and Function Flashcards

1
Q

Blood is

A

Connective Tissue

Derived from mesoderm

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2
Q

Function of Circulating Blood

A

Deliver Oxygen
Control Infection
Requirement for hemostasis

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3
Q

Most Sensitive Organs to O2

A

Brain
Heart
Kidney

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4
Q

What is Hematocrit?

A

the volume percentage of RBC in blood
Males 44%
Females 40%
Infants 50%

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5
Q

RBC size and shape

A

7-8 microns
biconcave disc
stain acidophillic (red)
Anucleated

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6
Q

Young Red Blood Cell

A

Reticulocyte

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7
Q

Anisocytosis

A

Variation in size

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8
Q

Poikilocytosis

A

Variation in shape

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9
Q

Chromicity

A

RBC color

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10
Q

Mean Cell Volume

A

Average volume of RBC

80-100fl

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11
Q

Mean cell hemoglobin

A

Average amount of hemoglobin per RBC

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12
Q

Mean Cell hemoglobin concentration

A

measures amount of hemoglobin in the cell relative to its size
If you just measured hemoglobin one could have very macrocytic RBCs that indicate high hemoglobin
MCHC factors in size of RBC

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13
Q

Red Cell distribution width

A

Make sure cells have tight distribution

i.e. all the cells fall within the same size

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14
Q

Hemoglobin

A

Oxygen and binding delivery
Tetrameric: 4 subunits (globin + heme)
2 alpha -globin
2 beta - globin

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15
Q

Hemoglobin vs. Myoglobin

A

Hemoglobin shows cooperativity and has a sigmoidal curve
Myoglobin, found in muscle, does not show cooperativity and has a hyperbolic curve
NB: myoglobin has a higher binding affinity for O2

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16
Q

Right Shift

A

Decrease affinity for oxygen

17
Q

What causes Right shift?

A

Increase Temp
Increase CO2
Increase 2,3 DPG
Low pH

18
Q

Left Shift

A

Increase affinity for oxygen

19
Q

What causes Left Shift?

A

Decrease Temp
Decrease CO2
Decrease 2,3 DPG
High pH

20
Q

2,3 Diphosphoglycerate

2,3DPG

A

derived from glycolytic intermediate
regulates the affinity of Hgb for O2
Increase shifts curve to the right
2,3DPG is competitive inhibitor for O2 and makes O2 dissociate more easily

21
Q

R State

A

Relaxed binds oxygen more easily

22
Q

T state

A

Tense state binds oxygen less readily

23
Q

What amino acid does heme interact with

24
Q

CO poisoning

A

Binds to heme iron
240 fold higher affinity than O2
Shifts O2 dissociation curve to the LEFT

25
Major and Minor genes for Adult Hemoglobin
Major: alpha 2; beta 2 Minor alpha 2; delta 2
26
Fetal Hemoglobin composition
alpha 2; gamma 2 fetal hemoglobin is resistant to 2,3DPG HbF has higher O2 affinity than adult
27
Sickle Cell Anemia
Glu 6 Val Valine substitution for glutamine Hb becomes insoluble when DEOXYGENATED
28
Methemoglobin
Iron in Hb: Ferrous Fe2+ Oxidative Stress causes transition to Fe3+ Ferric Methemoglobin has Fe3+ Methemoglobin cannot transport O2!!!!
29
Methemoglobin Reaction
Cyt b5ox + NADH --> Cyt b5red + NAD Cyt b5red + Hb-Fe3+ --> Cyt b5ox + Hb-Fe2+ occurs via methmoglobin reductase
30
Superoxide Dismutase
O2 Radical -->H2O2 + H2O
31
Catalase
H2O2 --> H2O + O2 | gets rid of hydrogen peroxide
32
Glutathione
2GSH + H2O2 --> GSSG + 2H2O GSSG + NADPH --> 2GSH + NADP gets rid of hydrogen peroxide
33
Hemoglobin A1C
Glycated Hb Non-enzymatic Proportional to blood glucose levels Integrated measure of glucose control over prolonged period
34
Spectrin
Gives RBC rubber like flexability
35
Ankyrin and Band 4.1
Anchor spectrin to the membrane
36
Band 3
anion exchanger important for moving bicarbonate in and out of cell
37
Cytoskeletal Organization of RBC
Band 3 is found in the membrane Ankyrin binds to band 3 Ankyrin/ Band 3 complex can bind to sepctrin Spectrin forms hexagonal lattice beneath plasma membrane
38
Heriditary Elliptocytosis
Caused by mutation in spectrin