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Questions and Answers

Which of the following is NOT a primary area of RBC biology that is crucial for normal erythrocyte survival and function?

  • Mitochondrial function (correct)
  • Hemoglobin structure and function
  • RBC metabolism
  • Normal chemical composition and structure of the RBC membrane

Peripheral proteins span from the outer surface of the membrane to the inner surface.

False (B)

What is the main structural component of the RBC membrane?

phospholipid bilayer

Loss of ____ leads to a decrease in the phosphorylation of spectrin and a loss of membrane deformability

<p>ATP</p> Signup and view all the answers

Which of the following ions are freely permeable to the RBC membrane?

<p>Chloride (Cl-) (B)</p> Signup and view all the answers

RBC volume and water homeostasis are maintained by controlling the intracellular concentrations of chloride and bicarbonate.

<p>False (B)</p> Signup and view all the answers

Match the following terms with their descriptions:

<p>Integral proteins = Proteins that span from the outer surface of the membrane to the inner surface Peripheral proteins = Proteins located only on the inner cytoplasmic side of the cell membrane Spherocytes = RBCs with a decreased surface-to-volume ratio Bite cells = RBCs with missing portions of membrane</p> Signup and view all the answers

What happens to the intracellular concentration of sodium and calcium when ATP is depleted during storage?

<p>They increase</p> Signup and view all the answers

What percentage of ATP needed by red blood cells is generated by glycolysis?

<p>90% (D)</p> Signup and view all the answers

Red blood cells use oxidative metabolism to produce ATP.

<p>False (B)</p> Signup and view all the answers

What is the main reason red blood cells rely on anaerobic metabolism?

<p>To avoid consuming the oxygen they are meant to deliver.</p> Signup and view all the answers

The Luebering-Rapoport shunt permits the accumulation of ________ in red blood cells.

<p>2,3-diphosphoglycerate</p> Signup and view all the answers

Match the following pathways with their primary function in red blood cells:

<p>Glycolysis = Generates 90% of ATP Pentose Phosphate Pathway = Produces 10% of ATP Methemoglobin Reductase Pathway = Influences post-transfusion RBC survival and function Luebering-Rapoport Shunt = Permits accumulation of 2,3-diphosphoglycerate</p> Signup and view all the answers

Which of the following best describes the effect of increased 2,3-DPG levels on the hemoglobin-oxygen dissociation curve?

<p>Shift to the right, decreasing oxygen affinity. (D)</p> Signup and view all the answers

The tense form (T form) of hemoglobin has a higher affinity for oxygen than the relaxed form (R form).

<p>False (B)</p> Signup and view all the answers

What is the primary role of hemoglobin?

<p>gas transport</p> Signup and view all the answers

Match the form of hemoglobin with its oxygen affinity:

<p>Tense form (T form) = Lower affinity for oxygen Relaxed form (R form) = Higher affinity for oxygen</p> Signup and view all the answers

How can transfusion of stored blood cause a shift to the left of the hemoglobin-oxygen dissociation curve?

<p>Transfused blood is 2,3-DPG deficient due to storage before use, which causes a high oxygen affinity.</p> Signup and view all the answers

RBCs should be stored in the liquid state at a temperature range of ____.

<p>1C - 6C</p> Signup and view all the answers

2,3-DPG can re-form in stored RBCs after in vivo circulation.

<p>True (A)</p> Signup and view all the answers

The rate of restoration of 2,3-DPG is NOT influenced by which of the following?

<p>How long the blood has been stored before transfusion (@)</p> Signup and view all the answers

CPDA-1 can only be stored for up to 21 days.

<p>False (B)</p> Signup and view all the answers

Match the following anticoagulant preservative solutions with their functions:

<p>Citrate (sodium citrate / citric acid) = Chelates calcium; prevents clotting Monobasic sodium phosphate = Maintains pH during storage; necessary for maintenance of adequate levels of 2,3-DPG Dextrose = Substrate for ATP production Adenine = Production of ATP (extends shelf-life from 21 days to 35 days); found only in CPDA-1</p> Signup and view all the answers

Top three benefits of RBC additive solutions:

  1. extends shelf-life of RBCs to __ days by adding nutrients
  2. allows for the harvesting of more _______ from the unit
  3. produces a packed RBC of _____ that is easier to infuse

<p>42, plasma and platelets, lower viscosity</p> Signup and view all the answers

what are the four additive solutions licensed in the United States.

<p>Adsol (AS-1), Nutricel (AS-3), Optisol (AS-5), and SOLX (AS-7)</p> Signup and view all the answers

Match the RBC additive solutions with their common ingredients:

<p>AS-1 = saline, adenine, glucose, mannitol AS-3 = saline, adenine, glucose, citrate, phosphate AS-5 = saline, adenine, glucose, mannitol AS-7 = saline, adenine, glucose, mannitol</p> Signup and view all the answers

Autologous transfusion allows individuals to donate blood for their own use to meet their needs for blood transfusion.

<p>True (A)</p> Signup and view all the answers

Rejuvenation of RBCs is the process by which ATP and 2,3-DPG levels are restored or enhanced by _______.

<p>metabolic alterations</p> Signup and view all the answers

FDA-approved rejuvenation solution contains which of the following

<p>phosphate (A), inosine (B), adenine (C)</p> Signup and view all the answers

rejuvenated RBCs may be prepared up to five days after expiration when stored in CPD, CPDA-1 and AS-1 storage solutions

<p>False (B)</p> Signup and view all the answers

why do rejuvenated RBCs need to be washed before infusion?

<p>to remove inosine, which may be toxic</p> Signup and view all the answers

RBC rejuvenation is time-consuming and expensive. Why would this process be used?

<p>it preserves selected autologous and rare units of blood for later use</p> Signup and view all the answers

rejuvenated RBCs must be transfused within ____ after washing, otherwise it must be frozen for long-term storage.

<p>24 hours</p> Signup and view all the answers

Flashcards

RBC membrane

A semipermeable membrane that encloses the red blood cell, composed of a lipid bilayer and a protein cytoskeleton. It allows for deformability, permeability, and maintains cell volume.

Integral proteins

Proteins that extend across the entire RBC membrane, from the outer to the inner surface. They play a vital role in its structure and function.

Peripheral proteins

Proteins located only on the inner surface of the RBC membrane. They help maintain the membrane's shape and stability.

RBC deformability

The ability of RBCs to bend and deform, allowing them to squeeze through narrow capillaries.

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RBC permeability

The property of the RBC membrane to allow certain substances to pass through while blocking others, crucial for maintaining cell volume and preventing hemolysis.

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Spherocytes

A condition where RBCs lose their normal shape and become spherical, reducing their surface area and leading to premature destruction.

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Bite cells

RBCs with a portion of their membrane missing, creating a bite-like indentation. This can be caused by various factors, including infection or oxidative stress.

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RBC membrane loss

The loss of RBC membrane, resulting in altered shape and function, leading to premature destruction.

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Glycolysis in RBCs

The main pathway used by red blood cells (RBCs) to generate energy (ATP), creating 90% of their energy needs.

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Pentose Phosphate Pathway in RBCs

A metabolic pathway in RBCs that produces NADPH, necessary to protect against oxidative damage and maintaining the structure of hemoglobin.

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Methemoglobin Reductase Pathway

A pathway that reduces methemoglobin back to functional hemoglobin, ensuring efficient oxygen transport.

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Luebering-Rapoport Shunt

An important regulatory mechanism in RBCs that increases the release of oxygen to tissues by lowering the affinity of hemoglobin for oxygen.

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2,3-Diphosphoglycerate (2,3-DPG)

A byproduct of the Luebering-Rapoport shunt, it plays a crucial role in regulating the oxygen affinity of hemoglobin.

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Hemoglobin-Oxygen Dissociation Curve

The ability of hemoglobin to bind and release oxygen is affected by the partial pressure of oxygen. Higher oxygen pressure leads to greater oxygen saturation, while lower pressure results in oxygen release. This relationship is not directly proportional but instead follows a sigmoid curve.

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Right Shift of the Hemoglobin-Oxygen Dissociation Curve

A shift to the right of the hemoglobin-oxygen dissociation curve indicates a decrease in hemoglobin's affinity for oxygen. This means hemoglobin releases oxygen more readily, which can be beneficial in situations like hypoxia where tissues need more oxygen.

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Left Shift of the Hemoglobin-Oxygen Dissociation Curve

A shift to the left of the hemoglobin-oxygen dissociation curve indicates an increase in hemoglobin's affinity for oxygen. This means hemoglobin holds onto oxygen more tightly, leading to less oxygen delivery to tissues. This can occur when there are high levels of oxygen in the blood, or as a result of certain medical conditions.

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Factors Affecting Hemoglobin-Oxygen Affinity

The oxygen affinity of hemoglobin can be modulated by various factors, including pH, carbon dioxide (CO2), and organic phosphates. These factors can influence the shape and position of the hemoglobin-oxygen dissociation curve, ultimately altering oxygen delivery to tissues.

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Study Notes

Red Blood Cell (RBC) Biology and Preservation

  • RBCs have a crucial lifespan of 120 days, dependent on three key biological areas:
    • Normal membrane composition and structure
    • Hemoglobin structure and function
    • RBC metabolism
    • Defects in these areas shorten lifespan. RBC metabolic pathways are primarily anaerobic to avoid consuming the oxygen they carry.

RBC Membrane

  • Composed of a semipermeable lipid bilayer with a protein cytoskeleton:
    • Phospholipids form a bilayer, proteins traverse it.
    • Integral proteins: Span the membrane.
    • Peripheral proteins: Located on the inner side of the membrane.
    • Asymmetrical organization: External layer (glycolipids, choline phospholipids); Internal layer (amino phospholipids).
    • Chemical composition: 52% proteins, 40% lipids, 8% carbohydrates.

Deformability

  • RBCs must stay flexible to survive.
    • Loss of ATP decreases spectrin phosphorylation, thus reducing deformability.
    • Increased calcium deposition stiffens the membrane.
    • Loss of membrane leads to abnormal shapes, like spherocytes (reduced surface area) and bite cells (membrane missing).

Permeability

  • Membrane controls RBC volume and prevents hemolysis.
    • Freely permeable to water and anions (Cl-, HCO3-).
    • Impermeable to most cations (Na+, K+).
    • Intracellular Na+/K+ ratios (1:12) and (25:1) are maintained via ATP-driven pumps.
    • Calcium (Ca2+) actively pumped out by ATPase pumps.
    • Storage depletes ATP; Na+, Ca2+ accumulate; K+, water are lost; and cells become rigid.

RBC Metabolism

  • RBCs lack a nucleus and mitochondria, making oxidative metabolism impossible.
  • RBC ATP production is primarily anaerobic.
  • Metabolic pathways are divided:
    • Glycolysis: Generates 90% of RBC ATP.
    • Pentose phosphate pathway: Produces 10% of RBC ATP.
    • Methemoglobin reductase pathway: Defects impact post-transfusion survival and function.
    • Luebering-Rapoport shunt: Allows 2,3-diphosphoglycerate (2,3-DPG) accumulation.
      • 2,3-DPG significantly affects hemoglobin's oxygen affinity, impacting RBC function post-transfusion.

Hemoglobin-Oxygen Dissociation Curve

  • Hemoglobin's role is gas transport (oxygen to tissues, carbon dioxide excretion).
  • 2,3-DPG is a key regulator of hemoglobin's oxygen affinity.
  • Deoxyhemoglobin (T form):
    • Widened space between beta chains.
    • 2,3-DPG binding on a mole-for-mole basis.
    • Anionic salt bridges between chains.
    • Lower oxygen affinity.
  • Oxyhemoglobin (R form):
    • Beta chains pulled together.
    • 2,3-DPG expelled.
    • Higher oxygen affinity.
  • Respiratory movement: allosteric changes during oxygen loading/unloading.
  • Hemoglobin-oxygen dissociation curve: sigmoid curve, not directly proportional to oxygen partial pressure.
  • Oxygen dissociation curve position depends on three ligands: H+ ions, CO2, and organic phosphates (2,3-DPG being most important).
  • Shift to the right:
    • Caused by hypoxia.
    • Increased 2,3-DPG levels alleviate tissue oxygen deficit.
    • Decreased hemoglobin oxygen affinity, increases oxygen delivery to tissues.
  • Shift to the left:
    • Increased hemoglobin-oxygen affinity.
    • Decreased oxygen delivery to tissues (only 12% oxygen released to tissues).
    • Caused by multiple transfusions of 2,3-DPG-depleted blood.

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