RED BLOOD CELL

Red Blood Cells or Erythrocytes

Contain oxygen-carrying protein hemoglobin that gives blood its red color
Biconcave disk 7 - 8 microns in diameter
increased surface area/volume ratio flexible shape for narrow passages no nucleus or other organelles 1/3 of cells weight is hemoglobin

Normal RBC count

no cell division or mitochondrial ATP formation

male 5.4 million/L ---- female 4.8 million/L new RBCs enter circulation at 2 million/second

Adult Reference Ranges for Red Blood Cells Measurement (units) Hemoglobin (gm/dL) Hematocrit (%) Red cell count (10 /L)
6

Men 1317 4050 4.55.5

Women 1215 3646 3.84.8

Reticulocyte count (%)

0.52.5

Mean Cell Volume (m )

3

83101
2732 3337

Mean Corpuscular Hemoglobin (pg) Mean Corpuscular Hemoglobin Concentration (gm/dL)

Erythrocyte Function
Erythrocytes are dedicated to respiratory gas transport Hemoglobin reversibly binds with oxygen and most oxygen in the blood is bound to hemoglobin Composition of hemoglobin
A protein called globin
A heme molecule
made up of two alpha and two beta chains Each heme group bears an atom of iron, which can bind to one oxygen molecule Each hemoglobin molecule thus can transport four molecules of oxygen

Introduction to RBC
Three areas of RBC metabolism essential for survival and function:
RBC membrane Hemoglobin structure and function Cellular energetics

Life span and breakdown of red cells Anemia

RBC Membrane
RBC membrane is a three layer structure: an outer hydrophilic portion composed of glycolipid, glycoprotein, and protein a central hydrophobic layer containing protein, cholesterol, and phospholipid an inner hydrophilic layer containing protein Membrane is a semi-permeable lipid bi-layer supported by a mesh-like cytoskeleton.

RBC Membrane
Cytoskeleton: Network of proteins on the inner surface of the plasma membrane Responsible for maintaining shape, stability, and deformability of RBC The major proteins that make up the cytoskeleton include: Spectrin Actin

Abnormalities of the RBC membrane

Hereditary spherocytosis - Decrease in surface area to volume ratio.
Result of defective cytoskeletal proteins.

Hereditary Elliptocytosis Abnormalities in the or spectrin subunits.

Hemoglobin

Globin protein consisting of 4 polypeptide chains One heme pigment attached to each polypeptide chain
each heme contains an iron ion (Fe+2) that can combine reversibly with one oxygen molecule

Primary Function = Transport oxygen from the lungs to the cells of the body & assist with CO2 removal

Hemoglobin
The normal adult hemoglobin (HbA) molecule contains 2 alpha-globulin chains and 2 beta-globulin chains. Adults also have small amounts of Hb A2 (22) fetuses and infants, the hemoglobin molecule HbF is made up of 2 alpha chains and 2 gamma chains (22). As the infant grows, the gamma chains are gradually replaced by beta chains.

Hemoglobin
Oxyhemoglobin hemoglobin bound to oxygen
Oxygen loading takes place in the lungs

Reduced hemoglobin results from release of O2 from oxyhemoglobin Methemoglobin When the ferrous iron of Hb is converted into ferric iron Carboxyhemoglobin Carbon monoxide is attached to Hb Carbaminohemoglobin hemoglobin bound to carbon dioxide
Carbon dioxide loading takes place in the tissues

Fate and Destruction of Erythrocytes

The life span of an erythrocyte is 100120 days Old erythrocytes become rigid and fragile, and their hemoglobin begins to degenerate Dying erythrocytes are engulfed by macrophages Heme and globin are separated
Iron is removed from the heme and salvaged for reuse
Stored as hemosiderin or ferritin in tissues Transported in plasma by beta-globulins as transferrin

Fate and Destruction of Erythrocytes

Heme is degraded to a yellow pigment called bilirubin
Liver secretes bilirubin into the intestines as bile Intestines metabolize bilirubin into urobilinogen Urobilinogen leaves the body in feces, in a pigment called stercobilin

Globin is metabolized into amino acids which are then released into the circulation

Life Cycle of Red Blood Cells

RBC Metabolic Pathways

Necessary for generation of ATP (energy) Necessary for RBC to maintain:

hemoglobin function membrane integrity and deformability RBC volume

RBC Metabolic Pathways

Generate energy through anaerobic breakdown of glucose Four pathways involved in RBC metabolism:
The pentose phosphate pathway Embden-Meyerhof Pathway Methemoglobin reductase pathway Luebering - Rapaport pathway

The pentose phosphate pathway

Produces NADPH - one of the main lines of defense for RBC against oxidative injury which may be caused by infections or oxidant drugs Deficiency in this pathway results in deficiency of glutathione which results in globin denaturation and precipitation as aggregates inside the RBC (Heinz bodies)

Embden-Meyerhof Pathway

90% of the ATP needed by the RBC is generated through this pathway Also generates NADH which is used in other metabolic pathways

Methemoglobin Reductase Pathway

Important in maintaining heme iron in the reduced or ferrous functional state In absence of enzyme methemoglobin reductase, have an accumulation of methemoglobin (iron in the ferric or oxidized state) Methemoglobin is non-functional, having lost ability to transport oxygen

Leubering-Rapaport Shunt
Causes an accumulation of RBC organic phosphate 2,3-DPG which is very important for hemoglobin's affinity for oxygen

Erythrocyte Disorders
Polycythemia
Abnormal excess of erythrocytes
Increases viscosity, decreases flow rate of blood

Anemia blood has abnormally low oxygen-carrying capacity

Blood oxygen levels cannot support normal metabolism Signs/symptoms include fatigue, paleness, shortness of breath, and chills

Some Diseases of RBCs and O2 Transport

Anemia: Decreased Hemoglobin Content

Iron-deficiency anemia results from:
A secondary result of hemorrhagic anemia Inadequate intake of iron-containing foods Impaired iron absorption

Pernicious anemia results from:

Deficiency of vitamin B12 Lack of intrinsic factor needed for absorption of B12

Anemia: Abnormal Hemoglobin

Thalassemias absent or reduced rate of synthesis of globin chain in hemoglobin
Erythrocytes are thin, delicate, and deficient in hemoglobin

Sickle-cell anemia results from a defective gene

Codes for an abnormal hemoglobin called hemoglobin S (HbS) This defect causes RBCs to become sickle-shaped in low oxygen situations

Polycythemia
Polycythemia excess RBCs that increase blood viscosity Two main polycythemias are:
Polycythemia vera Secondary polycythemia

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