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2. Summary of Blood #2

Hemoglobin is a metalloprotein in vertebrate red blood cells that transports oxygen and carbon dioxide, composed of four polypeptide chains. Its synthesis involves heme production in mitochondria and globin synthesis in the cytosol, continuing through various developmental stages in the bone marrow. Clinical considerations include conditions like methemoglobinemia and carboxyhemoglobin, while hemostasis involves vascular spasm, platelet plug formation, and coagulation through intrinsic and extrinsic pathways.

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0% found this document useful (0 votes)
20 views2 pages

2. Summary of Blood #2

Hemoglobin is a metalloprotein in vertebrate red blood cells that transports oxygen and carbon dioxide, composed of four polypeptide chains. Its synthesis involves heme production in mitochondria and globin synthesis in the cytosol, continuing through various developmental stages in the bone marrow. Clinical considerations include conditions like methemoglobinemia and carboxyhemoglobin, while hemostasis involves vascular spasm, platelet plug formation, and coagulation through intrinsic and extrinsic pathways.

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Daniel Dowding
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Hemoglobin Overview

 Function: Hemoglobin is a metalloprotein in vertebrate RBCs that transports oxygen and


carbon dioxide and acts as a buffer.
 Structure: Composed of four polypeptide chains (two alpha and two beta) that each bind
to a heme group (iron-containing pigment), forming a hemoglobin molecule.

Hemoglobin Biosynthesis

 Process: Hemoglobin is synthesized through a series of steps involving heme production


in mitochondria and globin synthesis in the cytosol of immature red blood cells.
 Development: Hb production continues from proerythroblast to reticulocyte stages in the
bone marrow, even after the loss of the nucleus.

Heme and Globin Synthesis

 Heme Synthesis: Initiated in mitochondria and involves condensation of succinyl CoA


and glycine, with delta-aminolevulinate formed and further processed in the cytosol.
 Globin Synthesis: After heme synthesis, it combines with globin polypeptides to form
hemoglobin; globin varies across species while the heme portion remains constant.

Hemoglobin Derivatives

1. Oxyhemoglobin (HbO2): Formed in the lungs when hemoglobin binds oxygen.


2. Reduced Hemoglobin (HHb): Forms in tissues when oxyhemoglobin releases O2 and
binds H+.
3. Carbaminohemoglobin: Hemoglobin binds CO2 at the N-terminal of polypeptides in
tissues.
4. Methemoglobin: Iron in hemoglobin is oxidized to Fe3+, preventing O2 binding;
normally 1.7-2.4% of Hb.
5. Carboxyhemoglobin: Hemoglobin binds carbon monoxide, which has a much higher
affinity for Hb than O2.

Clinical Considerations

 Methemoglobinemia: Occurs when defenses against oxidative damage are


overwhelmed, often due to toxins like acetaminophen. Treatment may involve
antioxidants or blood transfusions.
 Carboxyhemoglobin: Formed from CO exposure, leading to reduced oxygen transport.

Hemostasis

 Process: Involves three steps: vascular spasm, platelet plug formation, and coagulation.
1. Vascular Spasm: Constriction of blood vessels to reduce blood flow.
2. Platelet Plug Formation: Temporary sealing of vessel openings.
3. Coagulation: Involves intrinsic and extrinsic pathways, activating coagulation
factors to form a clot.

Coagulation Pathways

 Intrinsic Pathway: Activated when blood contacts foreign surfaces.


 Extrinsic Pathway: Triggered by tissue factor released from damaged tissues, requiring
coagulation factor VII.

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