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93 Cards in this Set

  • Front
  • Back

Acidosis

Increase in the acidity of the blood due to excessive loss of bicarbonate

Alkalosis

Increased in blood alkalinity due to accumulation of alkaline or reduction in acid

Allosteric

Charge which alters functioning of the organism or molecule

Amino Acid

One of a large group of organic compounds marked by the presence of both an amino group (NH3) and carboxyl group (COOH); the building protein

Complement

A group of protein which plays vital role in the bodes defenses through a series of carefully orchestrated reactions

Cyanosis

Blue tinge to the extremities -fingers, toes, lips

Hyperplasia

Excessive proliferation of normal cells in the normal tissue of an organ

Polychromasia

Blue tinge to the red cells indicating premature disease


Which of these hemoglobins is an embryonic hemoglobin?


Hgb Gower

How many total genes does a person posses for the production of alpha chains?


4 (Four)

Name one condition that may shift the OD curve to the left.

Anemia

If polychromasia is increased in the peripheral smear, the _________ should be elevated.

Reticulocyte Count

IF 2, 3-DPG increases, the hemoglobin molecule releases more oxygen. This is known as a _______OD curve.

Right - Shifted OD Curve

Which of the following statements regarding 2,3-DPG is correct?

It controls hemoglobin affinity for oxygen

When the iron in the hemoglobin molecule is in the ferric(Fe^3+) state, hemoglobin is termed??

Methemoglobin

What percent of hemoglobin is synthesized in the reticulocyte stage?

35 %

Epsilon and zeta chains are part of which of the flowing hemoglobin?

Hgb Portland

Fetal hemoglobin consist of which of the following chains?

a2E2 (a-aplha)


Hemoglobin Molecules Consist of 2 primary structures

1. Heme Portin


2. Globin Portin




Define Hemoglobin

Life giving structure of every red blood cells, the oxygen-carrying component of the red blood cells.


What is consist of the Heme portion?

- 4 iron atoms Fe2+


-Iron is surrounded by each protoporphyrin ring

What is consist of the Globin portion?

Two pairs of polypeptide chains


---Normal postnatal hemoglobin is made of


---Two alpha chains (a) and two beta (b) chains


---Two alpha chains (a) and two delta (d) chains


---Two alpha chains (a) and two gamma (y) chains


Hemoglobin Composition- Heme

* The iron is surrounded by protoporphyrin IX or the porphyrin ring
* Formed in the nucleated red blood cells
* Protoporphyrin IX results from the interaction of succinyl coenzyme A and delta-aminolevulinic acid in the mitochondria of nucleated RBC
* Several intermediate by-products are formed, which include:
* porphobilinogen, uroporphyrinogen coproporphyrin and protoporphyrinogen IX
* When iron is incorporated, it combines with protoporphyrin to form the complete heme molecule
* Defects in any of the intermediate products impairs hemoglobin function
* 65% is synthesized before the red blood cell nucleus is extrude
* An additional 35% synthesized by the reticulocyte stage

Globin portion

* Consists of amino acids linked together to form a polypeptide chain
* Most predominant chains for adult hemoglobins are the alpha and beta chains
* Alpha chains have 141 amino acids and beta chains have 146 amino
* Heme molecules lodge in the pocket of the globin chains
* 2,3-Diphosphoglycerate (2,3-DPG):
* 2,3-DPG is a substance produced via the EmbdenMeyerhof pathway during anaerobic glycolysis
* This structure plays a huge role in the oxygen affinity of hemoglobin

Hemoglobin Forms

* Each globin chain is under the influence of a specific chromosome
* Chromosome 11 contains the genes for the production of epsilon, beta, gamma, and delta chains
* Chromosome 16 is responsible for the alpha and zeta genes
* Three forms produced:
* Embryonic hemoglobin (no participation in oxygen delivery)
* Hemoglobin Gower I (ζ2, ε2)
* Hemoglobin Gower II (α2,ε2)
* Hemoglobin Portland (ζ2 δ2)
* Fetal hemoglobin (3 months fetal development–6 months post birth)
* Hemoglobin F (α2 γ2)
* High oxygen affinity

3. Adult Hemoglobin

* Hemoglobin A (α2 β2): 96%–98% (majority of adult hemoglobin)
* Hemoglobin A2 (α2 δ2): 2%–5% (normal adult hemoglobin complement)
* Hemoglobin F (α2 γ2): <1%(normal adult hemoglobin complement)

Hemoglobin function

* Oxygen delivery is the principal purpose of the hemoglobin
* Hemoglobin also transports C02 away from the tissues
* The hemoglobin molecule loads oxygen on a one-to- one basis
* one molecule of oxygen to one molecule of heme in the oxygen-rich environment of the lungs
* As hemoglobin goes through the loading and unloading process, changes occur in the molecule
* allosteric changes

Hemoglobin function

* The hemoglobin molecule takes a tense and a relaxed form
* When tensed
* hemoglobin is not oxygenated
* 2,3-DPG is at the center of the molecule
* salt bridges between the globin chains are in place
* When relaxed
* hemoglobin is oxygenated
* 2,3-DPG is expelled
* salt bridges are broken
* molecule is capable of fully loading oxygen

Oxygen Dissociation (OD) Curve

* Hemoglobin delivers oxygen in exchange for CO2
* OD curve represents oxygen release from hemoglobin to the tissues
* Sigmoid shape
* Increase bound oxygen when Increase PO2
* Lungs: PO2 is 100 mm Hg = 97% Hgb saturation
* Circulation: PO2 is 40 mm Hg = 25% Hgb saturation

Oxygen Dissociation (OD) Curve

* In the normal curve (blue) at 40 mm Hg, 75% of the hemoglobin molecule is saturated with oxygen, leaving 25% capable of being released to tissue (7.4)
* For the right shifted curve (red), at 40 mm Hg, hemoglobin is 50% saturated but willing to give up 50% of its oxygen to the tissues (7.2)
* For the left shifted curve (green), at 40 mm Hg, hemoglobin is 85% saturated but willing to release only 12% to the tissues. (7.6)

OD Curve Changes Shift to the Right

* Shift to right
* More likely to release oxygen to tissue
* Lower affinity
* Anemia
* Acidosis (Decreased pH)
* Increased 2,3-DPG
* Elevated body temperature (fever)

OD Curve Changes Shift to the Left

* Shift to left
* Less likely to release oxygen to tissue
* Higher affinity
* Abnormal hemoglobin
* Alkalosis (Increased pH)
* Decrease 2,3-DPG, body temp, and abnormal Hgb (CO)

Abnormal Hemoglobin


* Hemoglobins that are physiologically abnormal have a higher oxygen affinity
* produce conditions that are usually toxic to the human body
* Results from the following:
* ingestion or absorption of harmful substances
* Inherited defects
* Three abnormal hemoglobins are:
* Methemoglobin
* Iron in Fe3+ state
* no longer capable of binding oxygen
* level >10%, individuals appear cyanotic

Abnormal Hemoglobin

* 2. Sulfhemoglobin
* Exposure to sulfonamides
* sulfemoglobin cannot carry oxygen
* It may be toxic at low levels
* 3. Carboxyhemoglobin
* High affinity for carbon monoxide
* Affinity is 200 times greater than its affinity for oxygen;
* no oxygen is delivered to the tissues

Hemolysis

* Red blood cell death is a natural process after 120-days
* The contents of the RBC are released and recycled for RBC regeneration
* If premature cell death or hemolysis occurs, a series of events begin to cascade providing laboratory evidence that cells are dying earlier than 120-day life cycle
* The bone marrow shows erythroid hyperplasia
* increase in red blood cell precursors
* premature release of reticulocytes and other immature cells
* The peripheral smear provides visual clues of hemolysis
* increase in polychromasia
* presence of nucleated red blood cells
* spherocytes

Hemolysis

* Extravascular 90%
* RES system: spleen, liver, lymph nodes, bone marrow
* Releases heme and globin contents to be recycled
* Iron is transported via transferrin to the bone marrow or storage sites to be used in erythropoiesis
* Rest of hemoglobin molecule reacts with hemoxygenase, yielding- biliverdin
* biliverdin is reduced to unconjugated bilirubin
* This bilirubin product attaches to albumin and is transported to the liver
* Intravascular
* Lysed directly in blood vessels
* Table 4.2 p. 55
* Extravascular hemolysis: increased
* bilirubin, decreased haptoglobin

Hemolytic Anemia: Intravascular

* Decrease Hgb, HCT, RBC count
* Increase Serum bilirubin
* Decrease Serum haptoglobin
* Hemoglobinemia (free Hgb)
* Hemoglobinuria
* Possible Increase retic
* Increase LDH
* Schistocytes

Hemolytic Anemia: Extravascular

* Decrease Hgb, HCT, RBC count
* Increase Serum bilirubin
* DecreaseHaptoglobin
* Hepatosplenomegaly possible
* -sequestered damaged red blood
* Increase LDH
* Spherocytes

Intrinsic Red Cell Defects leading to hemolysis (anemia)

* Hemoglobinopathies
* Structural and synthesis
* Red cell membrane defects
* Red cell enzyme defects
* Stem cell defects

Extrinsic Red Cell Defects

* Autoimmune hemolytic anemia (AIHA)
* Parasitic infections
* Microangiopathic hemolytic anemia (MHA)
* caused by factors in the small blood vessels
* Environmental agents
* Venoms
* Chemical agents

Amino Acids

Alpha Chains -141 Amino Acids in a unique arrangement.


Beta Chains - 146 Amino Acids in a unique arrangement.

2,3-DPG

A substance produced via the Embden Meyerhof pathway during anaerobic glycolysis. This structure relates to oxygen affinity of hemoglobin.

Synthesis of Hemoglobin

Hemoglobin synthesis begins at Polychromatic normoblast stage of RBC development. this synthesis is seen by the change in cytoplasmic color from a deep blue to lavender cytoplasmic color. Hemoglobin, 65% is synthesized before the RBC nucleus is extruded, with an additional 35% synthesis by reticulocyte stage.

Normal Mature RBC

Full complement of hemoglobin which occupies a little less than one-half of the surface area of the RBC.

Epsilon and Zeta Chains reserved for the what production?

Production of Embryonic Hemoglobin

Embryo Develops

Hgb Gower 1 (a2, E2) (Alpha 2, Epsilon 2)

Synthesized and remain in Embryo for 3 months

Hgb Portland (y2$2) These hemoglobin do not participate in oxygen delivery

Fetal Hemoglobin

Hgb F (a2y2)(alpha2,gamma2) Being to synthesized at 3 months of Fetal development and remains as the majority hemoglobin at birth

3 to 6 months after delivery

Hgb A (alpha2, beta 2) The amount of gamma chains declines and the amount of beta chains increases. Hgb A, the majority of adult hemoglobin (95-98%)

Hemoglobin consist of ?

Iron and Protoporhyrin Ring

Globin consist of?

Amino acid chains of specific lengths and specific amino acidosis. Alpha and Beta are the two most significant amino acid chains.

What are the 2 Embryonic Hemoglobin?

Hgb Gower and Hgb Portland

What is the Fetal Hemoglobin?

Hgb F

Adult Hemoglobin?

Hgb A - Primary


Hgb A2 and Hgb F - Complement

Oxygen Delivery?

Primary purpose of Hemoglobin molecule

2,3-DPG

Related to oxygen affinity of hemoglobin

OD Curve Represents?

The saturation of hemoglobin with oxygen and the release of oxygen from the hemoglobin molecule under normal and abnormal physiologic conditions.


Hemolysis

Is the premature destruction of the RBC before 120 day life cycle

Hemolysis Classified as?

Intravascular or Extravascular , which relates to the site of hemolysis

Intravascular Hemolysis

Occurs inside the body vessels

Extravascular Hemolysis

Occurs outside the body vessels, primarily in the reticuloendothelial system

Hemolyic Anemias

Classified by intrinsic defects of RBC or extrinsic defects that affects the RBCs.

Name 4 microcytic anemias:

1. Iron deficiency anemia (IDA)
2. Thalessemia
3. Iron overload disorders
4. Anemia of chronic disorders

Two ways that IDA (iron deficient anemia) can develop

1. deficient iron intake
2. defective iron absorption

What causes thalassemia

1. Caused by missing or diminished alpha or beta globin chains
2. Results in formation of hypochromic microcytes due to rapid cell divisions searching for iron
3. Normal adult hemoglobin cannot be synthesized

Describe iron overload disorders

1. Ex: hereditary hemochromatosis
2. Patients will show dimorphic smear (some microcytes with macrocytes) (some normal hemoglobin and some hypochromic)

What causes anemia of chronic disorders

1. arises from renal failure or thyroid dysfunction
2. Iron delivery to the reticuloendothelial system is impaired

Conditions that cause macrocytes:

1. liver disease of alcoholism
2. megaloblastic anemia
Formed due to lack of vitamin B12 or folic acid

Describe appearance of Spherocytes

They are dense, dark red and small
Elevated MCHC with lifelong moderate anemia
shorted life span
Hereditary spherocytosis
Ab-coated RBC formed from immune response
Spleen cleans off Ab's and remove part of RBC membrane

What are the three major parts of a hemoglobin molecule

1. Heme
2. Globin
3. 2,3 diphosphoglycerate (2,3-DPG)

How may molecules of iron per heme?

4 iron atoms (Fe2+)

Name the three types of synthesized hemoglobin

1. embryonic hemoglobin
2. fetal hemoglobin
3. adult hemoglobin

Name the thee types of adult hemoglobin and its percentages

Hemoglobin A (95 - 98%)
Hemoglobin A2 (3 - 5%)
Hemoglobin F (<2%)

Main function of hemoglobin

Principal purpose is oxygen delivery
Additional functions: Pull CO2 away from the tissues and keeping the blood in a balanced pH

Explain Oxygen dissociation curve

1. S-shaped
2. Shows how the hgb molecules and oxygen respond to normal and abnormal physiologies
3. In high levels of O2, molecule is fully saturated and more willing to give to tissues

In lungs if PO2 is 100 mm Hg then hemoglobin will be ___ % saturation

97

Shift to right

more likely to release oxygen to tissue
H+ increase
P-CO2 increase
temp increase

Lower affinity (less attraction)
- Anemia
- Acidosis
- Increased 2,3-DPG

Shift to left

Less likely to release oxygen to tissue
Higher affinity (more attraction)

H+ decrease
P-CO2 decrease
temp decrease

- Decreased body temp
- abnormal hemoglobin
- alkalosis
- Decreased 2,3-DPG

Name the three types of abnormal hemoglobin

These are often formed by accidental or intentional ingestion or they can be inherited defects
1. Methemoglobin
- iron oxidized for Fe 3+ state instead of Fe2+
- > 10% person become cyanotic
2. Sulfhemoglobin
-exposure to sulfonamide or sulfa drugs

3. carboxyhemoglobin
- increased in smokers and some industrial workers
- high infinity for carbon monoxide (200 times greater) no oxygen delivery to tissue
- formed during carbon monoxide poisoning

Two types of hemolysis

1. extravasular
2. intravascular

Extravascular hemolysis

red blood cells are lysed in organs

Intravascular hemolysis


red blood cells are lysed directly into the blood
10% of hemolysis
Lysis takes place directly inside vessel and hemoglobin released into plasma
Hemoglobinemia - red tinged blood in plasma
hemoglobinuria - free hemoglobin in urine

In venous circulation if PO2 is 40 mm Hg then hemoglobin saturation is ___ saturation

75%

Which of these hemoglobins is an embryonic hemoglobin





Hgb Gower

How many total genes does a person posses for the production of alpha chain

4

Name one condition that may shift the OC curve to the left


Inheriting a high oxygen affinity hemoglobin

If polychromasia is increased in the peripheral smear, the ------should be elevated


Reticulocyte count

If 2,3-DPG increases, the hemoglobin molecule releases more oxygen.

This is known as a Right-shifted

which of the following statements regarding 2,3-DPG is correct?

It controls hemoglobin affinity for oxygen

When the iron in the hemoglobin molecule is in the ferric (Fe3+) state, hemoglobin is termed


Methemoglobin

What percent of hemoglobin is synthesized in the reticulocyte stage


35%

Epsilon and zeta chains are part of which of the following hemoglobin


Hgb Portland

Fetal hemoglobin consists of which of the following chain?


(alpha2, gamma2) or (a2,Y2)