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HB2 > RBC Structure and Function > Flashcards

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

A

Histadine

24
Q

CO poisoning

A

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

25
Q

Major and Minor genes for Adult Hemoglobin

A

Major:
alpha 2; beta 2

Minor
alpha 2; delta 2

26
Q

Fetal Hemoglobin composition

A

alpha 2; gamma 2
fetal hemoglobin is resistant to 2,3DPG
HbF has higher O2 affinity than adult

27
Q

Sickle Cell Anemia

A

Glu 6 Val
Valine substitution for glutamine
Hb becomes insoluble when DEOXYGENATED

28
Q

Methemoglobin

A

Iron in Hb: Ferrous Fe2+
Oxidative Stress causes transition to Fe3+ Ferric
Methemoglobin has Fe3+
Methemoglobin cannot transport O2!!!!

29
Q

Methemoglobin Reaction

A

Cyt b5ox + NADH –> Cyt b5red + NAD
Cyt b5red + Hb-Fe3+ –> Cyt b5ox + Hb-Fe2+
occurs via methmoglobin reductase

30
Q

Superoxide Dismutase

A

O2 Radical –>H2O2 + H2O

31
Q

Catalase

A

H2O2 –> H2O + O2

gets rid of hydrogen peroxide

32
Q

Glutathione

A

2GSH + H2O2 –> GSSG + 2H2O
GSSG + NADPH –> 2GSH + NADP
gets rid of hydrogen peroxide

33
Q

Hemoglobin A1C

A

Glycated Hb
Non-enzymatic
Proportional to blood glucose levels
Integrated measure of glucose control over prolonged period

34
Q

Spectrin

A

Gives RBC rubber like flexability

35
Q

Ankyrin and Band 4.1

A

Anchor spectrin to the membrane

36
Q

Band 3

A

anion exchanger important for moving bicarbonate in and out of cell

37
Q

Cytoskeletal Organization of RBC

A

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
Q

Heriditary Elliptocytosis

A

Caused by mutation in spectrin

HB2 (14 decks)

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