Chapter 2 - Erythropoiesis And Hemoglobin synthesis Flashcards

1
Q

What is a erythropoieses?

A

Production of red blood cells

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2
Q

What is the primary function of red blood cells?

A

To carry hemoglobin which is responsible for the transportation of oxygen and carbon dioxide within the body
Red blood cells maintain hemoglobin and it’s functional Ferrous state by a series of metabolic reactions

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3
Q

What is erythropoietin?

A

A hormone which initiates the production of red blood cells in the bone marrow it is produced in the kidney.

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4
Q

Where are red blood cells formed?

A

Bone marrow

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5
Q

What are the stages of maturation in the red blood cell?

A
Rubriblast (pronormoblast)
Prorubricyte (basophilic normoblast)
Rubricyte (polychromatic normoblast)
Metarubricyte (orthochromic normoblast)
Reticulocyte
Mature erythrocyte
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6
Q

What are some characteristics of a Rubriblast (pronormoblast)

A

18 to 20 µm
N:C ratio of 6 to 1
Dark marine blue cytoplasm
Beginning to accumulate components necessary for hemoglobin production

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7
Q

What are some characteristics of a Prorubricyte (basophilic normoblast)

A

16 µm
N:C Ratio of 6 to 1
No nucleoli red to purple chromatin

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8
Q

What are some characteristics of a Rubricyte (polychromatic normoblast)

A
13 µm 
N:C of 4 to 1 
nuclear chromatin is condensed and compacted 
hemoglobin begins to be synthesized 
last stage capable of mitosis
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9
Q

What are some characteristics of a Metarubricyte (orthochromic normoblast?

A

8 µm N:C ratio of 1 to 1

nuclear chromatin is homogeneous (pyknotic)

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10
Q

What are some characteristics of a Reticulocyte?

A

8 µm
no nucleus
remnants of RNA visualized as reticulum RNA remnants will continue to form Heme
Hemoglobin production is completed here
slightly larger than mature red blood cell when it’s released in peripheral blood called Polychromatophilic

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11
Q

What are some characteristics of an erythrocyte?

A
6 to 8 µm 
no nucleus 
biconcave disc shape 
does not produce hemoglobin 
lives approximately 120 days
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12
Q

If there is an increased demand for oxygen carrying capacity what is released into the blood?

A

Reticulocytes

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13
Q

When does hemoglobin synthesis start and end?

A

it starts in the polychromatophilic normoblast (rubricyte)stage and ends in the reticulocyte stage

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14
Q

True or false hemoglobin is a complex protein?

A

True it is composed of a heme portion and a protein globin portion

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15
Q

Where does the synthesis of heme take place?

A

In the mitochondria of an immature red cell

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16
Q

Where does the synthesis of globin take place?

A

In the ribosomes of an immature red cell

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17
Q

What does a hemoglobin molecule consist of

A

Four gene groups and four polypeptide chains

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18
Q

What Percent of the dry weight of the red cell is hemoglobin?

A

90%

19
Q

Hemoglobin a
hemoglobin F
hemoglobin A2 consist of what?

A

2 Alpha, 2beta chains
2 Alpha, 2 gamma chains
2alpha, 2 Delta chains

20
Q

Where do red blood cells get their energy from?

A

The breakdown of glucose (glycolysis)

21
Q

The M den-Mayerhoff pathway provides 90% of what?

A

ATP

22
Q

The phosphogluconate pathway produces how much ATP?

A

5 to 10%

23
Q

The methemoglobin reductase pathway As a responsible for what?

A

Maintaining iron in the reduced ferrous state so O2 can be delivered to the tissues

24
Q

What does the heme portion contain?

A

Four iron atoms in the Ferrous state

25
Q

True or false iron in the ferric state can bind to O2

A

False

26
Q

What does the globin portion consist of?

A

Amino acids linked together to form a polypeptide chain there are four polypeptide chains

27
Q

What determines the hemoglobin type?

A

The different globin chains

28
Q

What are the types of hemoglobin in non-adults?

A

Hgb gower 1
Hgb Portland
Hgb F (fetal hgb)

29
Q

What is the primary function of hemoglobin?

A

Oxygen delivery but it also pulls CO2 away from the tissues keeping the blood in a balanced PH

30
Q

The ability of hemoglobin to accept or release oxygen is?

A

Oxygen affinity. Binding requires high oxygen affinity releasing requires a low oxygen affinity

31
Q

The binding and releasing of oxygen from the hemoglobin molecule is called?

A

Oxygen dissociation curve.

32
Q

A shift to the right In an oxygen dissociation curve means what?

A

Hemoglobin has less attraction for oxygen and is more willing to release oxygen to the tissues
causes Anemia, decreased pH, fever
“Red line”

33
Q

A shift to the left “blue line” in an oxygen dissociation curve means what?

A

Hemoglobin has more of an attraction for oxygen and is less willing to release it to the tissues
causes reduce the body temp,abnormal hemoglobin’s, increased pH

34
Q

Abnormal hemoglobin’s have a reduced ability for what?

A

Carrying oxygen

35
Q

High amounts of abnormal hemoglobin’s can cause what?

A

Cyanosis, hypoxia, and death

36
Q

Once iron has been oxidized into the ferric state is the red cell capable of reducing the iron back to the Ferrous state?

A

Yes

37
Q

When hemoglobin combined with carbon monoxide instead of oxygen what is formed?

A

Carboxyhemoglobin
It is reversible if caught in time.
10 to 15% of people experience dizziness and headaches 40% experience comas and convulsions

38
Q

What causes sulfhemoglobin and can it be reversed?

A

Hemoglobin oxidizes due to chemicals or drugs and it cannot be reversed

39
Q

What abnormal hemoglobin is the only one that cannot be measured by the cyanmethemoglobin?

A

Sulfhemoglobin

40
Q

Hemoglobinometry Is the measurement of what

A

Hemoglobin in the blood.

41
Q

The most popular form of hemoglobinometry is?

A

Colorimetric

42
Q

Cyanmethemoglobin causes the hemoglobin to be oxidized to what?

A

Methemoglobin

43
Q

Sources of error in Cyanmethemoglobin?

A

Highwhite blood cell counts causing turbidity fix this by centrifuging to test solution lipemic samples
abnormal hemoglobin proteins

44
Q

Normal hemoglobin reference ranges

A

Male: 14.0 to 18.0 g/dL
Female: 12.0 to 16.0 g/dL