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LF266: Blood and Circulation > Lecture 4: Blood Cells and Plasma > Flashcards

Lecture 4: Blood Cells and Plasma Flashcards

1
Q

What is haematology?

A
  • Study of blood n in particular the medical specialty concerned w blood disorders
    • Blood n tissues in which it is formed represent large single organ system
    • Hematopoietic system basics
      ○ Key paradigms underlying stem cell biology, cancer n thrombosis
      ○ Involved in every aspect of patient care from
      § Routine blood counts
      § Blood transfusion
      Specialized management of patients w leukemia or hemophilia
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2
Q

How much blood does the human body typically contain, and what are its primary components?

A
  • The human body contains 4.7-5L of blood
    • Blood contains cell n plasma (fluid)
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3
Q

What are the primary types of cells found in blood?

A

Blood contains white cells, red cells, thrombocytes (platelets), and, in pregnant individuals, fetal cells.

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4
Q

What components make up the plasma portion of blood?

A

Plasma consists of water, electrolytes, dissolved gases, urea, proteins, lipids, glucose, and various other substances in trace quantities. Additionally, substances such as alcohol and nicotine may be detected in plasma under certain conditions.

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5
Q

How does blood look when centrifuged?

A
  • 55% plasma: sits on top
  • <1 % buffy coat: WBC and platelets, sits in between
  • 45% RBC: sits at the bottom of test tube
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6
Q

What are the concentration of the major cells types found in blood?

A
  • Erythrocytes (RBC): 4-6 x 10^12 per L (40-50% vol)
  • Leukocytes (WBC): 4-11 x 10^9 per L
  • Thrombocytes (platelets): 1-4 x 10^11 per L
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7
Q

Describe the blood cell lineages

A
  • Blood stem cell → myeloid stem cell / lymphoid stem cell
  • Myeloid stem cell → RBC / platelets / myeloblast
  • Myeloblast → WBC granulocytes (eosinophil / basophil / neutrophil)
  • Lymphoid stem cell → lymphoblast → B lymphocyte / T lymphocyte / NKC
  • WBCs come from both myeloid and lymphoid lineages - all nucleated
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8
Q

What is the origin of lymphoid cells?

A

Lymphoid cells originate from the clear fluid of the thoracic lymph duct and are derived from lymph. They play crucial roles in the lymphoid and immune systems and are commonly found in lymph nodes and the spleen.

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9
Q

Where do myeloid cells originate?

A

Bone marrow.

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10
Q

How does an erythrocyte (red blood cell) adapt to carrying oxygen through very fine blood vessels?

A
  • An erythrocyte can deform to fit through narrow vessels, with its diameter of 7-8 microns folding to fit through holes as small as 3 microns in diameter.
  • This deformation allows it to navigate through the smallest capillaries.
  • The shape adaptation is maintained by the cytoskeletal system, particularly through interactions with proteins like spectrin and actin, which form an underlying mesh providing flexibility.
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11
Q

What are the consequences of having too few or too many erythrocytes in the blood?

A
  • Too few erythrocytes → anemia
    • Pallor, breathlessness, fatigue due to lack of O2 transport to tissues
  • Too much erythrocytes → polycythemia
    • Raised blood viscosity n strain on heart
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12
Q

What is erythropoietin?

A
  • glycoprotein hormone that stimulates RBC production (HEMATOPOIESIS)
    • Synthetic drug misused in sports ie cycling, more RBC can transfer to the O2 more quickly
    • Polycythaemia causes blood to become thick n viscous -> heart can’t pump it -> fatal
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13
Q

Where are leukocytes present during their production and function?

A

Where are leukocytes present during their production and function?

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14
Q

How can leukocytes be recognized and distinguished?

A
  • Morphology: Observing their shape and structure under a microscope.
  • Stains and dyes: Using specific dyes to highlight different cellular components.
  • Histochemistry: Testing for the presence of specific enzymes or proteins in the cells.
  • Antibodies to cell surface markers: Using antibodies that bind to specific proteins on the cell surface to identify different leukocyte types.
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15
Q

What are the characteristics of different leukocyte types?

A
  • Lymphocytes: Similar in size to red blood cells (RBCs), mostly consisting of a nucleus with little cytoplasm.
  • Neutrophils: Slightly larger than RBCs, with a lobed nucleus and granules in the cytoplasm.
  • Monocytes: About three times the size of RBCs, with a single large C-shaped nucleus.
  • Eosinophils: Stain pink, with a blue nucleus.
  • Basophils: Granulated cells that appear dark blue overall.
  • Histochemistry can be used to test for the presence of specific enzymes or proteins outside the cell membranes of these leukocytes.
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16
Q

How does morphology contribute to the identification of cells?

A
  • Cells in suspension typically have a round shape, while those in tissues may adopt different forms, such as dendritic cells.
  • Nuclei within cells may exhibit distinctive shapes, aiding in identification.
  • Cell size can vary, providing further clues about cell type.
  • Granules present in the cytoplasm of certain cells can also be indicative of their identity.
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17
Q

What are the components of the H&E stain?

A
  • Hematoxylin: a blue-purple basic dye that binds to nucleic acids, imparting a blue color to cell nuclei.
  • Eosin: a pink acidic dye that binds to proteins, resulting in pink staining of the cytoplasm.
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18
Q

How does eosin staining contribute to cell identification?

A
  • Crucial role in cell identification by binding to proteins in the cytoplasm, causing it to appear pink.
  • This staining pattern can help differentiate various cell types, as certain cells, such as eosinophils, exhibit distinctive pink granules when stained with eos
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19
Q

What is histochemistry?

A

Technique used to study the chemical composition of biological tissues by applying specific chemical reactions to visualize the presence of certain molecules or enzymes.

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20
Q

How is histochemistry applied in leukocyte identification?

A
  • In leukocyte identification, non-specific esterases are commonly used to label the monocyte lineage.
  • These esterases cleave alpha-naphthyl acetate to alpha-naphthol, which reacts with pararosaniline to produce a red-brown color. This staining helps differentiate monocytes from other cell types and is often counterstained with hematoxylin for better visualization.
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21
Q

What is cytochemistry used for in cell detection?

A
  • Utilizes fluorescent chromophores linked to antibodies to detect specific molecules or antigens within cells.
  • Allows for the visualization and identification of cellular components based on the presence or absence of fluorescence signals generated by the interaction between antibodies and their target molecules.
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22
Q

How does histochemistry aid in the identification of cell types?

A
  • Using antibodies linked to enzymes that convert substrates into colored products to detect specific antigens or molecules in tissue sections.
  • By visualizing the distribution and localization of these colored products, histochemistry enables the identification and characterization of different cell types based on their unique molecular markers and staining patterns.
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23
Q

What markers are associated with B cells?

A
  • B cells express CD38 and CD138 markers, which are used to identify and characterize these immune cells.
  • CD38 is a cell surface glycoprotein involved in cell adhesion and signaling, while CD138, also known as syndecan-1, is a proteoglycan that plays a role in cell-matrix interactions and cell signaling.
24
Q

How do changing markers throughout cell lineage help in understanding diseases?

A
  • Can identify abnormalities or dysregulations that may occur at different stages of cellular maturation.
  • Helps in understanding the molecular mechanisms underlying diseases and designing targeted therapies to correct aberrant cellular processes.
24
Q

Why are stem cells negative for certain markers?

A
  • They possess a unique molecular profile that distinguishes them from differentiated cells.
  • These markers are often associated with lineage-specific differentiation and are absent in undifferentiated stem cells, allowing researchers to identify and isolate stem cell populations based on their marker expression.
24
Q

What are the major components of plasma proteins?

A
  • Plasma proteins are classified into several major groups, including albumin, alpha (α) globulins (such as alpha-1 and alpha-2 globulins), beta (β) globulins, and gamma (γ) globulins.
  • Albumin is the most abundant plasma protein, while gamma globulins primarily consist of immunoglobulins or antibodies.
25
Q

Where are plasma proteins synthesized?

A
  • Most plasma proteins, including albumin, alpha globulins, and beta globulins, are synthesized in the liver.
  • However, gamma globulins, which mainly comprise immunoglobulins or antibodies, are produced by plasma cells (a type of white blood cell) in lymphoid tissues such as the spleen and lymph nodes.
26
Q

What is serum?

A
  • Fluid component of blood that remains after blood has clotted and the clot has been removed.
  • It is essentially plasma without the clotting factors.
26
Q

What does serum contain?

A

Serum contains all the proteins present in plasma, including albumin, globulins, fibrinogen, and other solutes, but it lacks the clotting factors involved in the coagulation cascade, as these are removed during the clotting process.

27
Q

How does serum differ from plasma?

A
  • Serum differs from plasma in that it lacks clotting factors such as fibrinogen, prothrombin, and other coagulation factors that are involved in the clotting process.
  • Serum is obtained by allowing blood to clot and then centrifuging it to separate the clot from the liquid component.
28
Q

What is non-denaturing gel electrophoresis?

A

Technique used to separate proteins based on their size and charge without disrupting their native structure.

29
Q

How does non-denaturing gel electrophoresis work?

A
  • Proteins are loaded onto a gel matrix and subjected to an electric field.
  • Because proteins have different sizes and charges, they migrate through the gel at different rates.
    • Smaller proteins move faster and migrate farther, while larger proteins move more slowly and remain closer to the point of origin.
30
Q

What is the significance of covering the gel in SDS?

A
  • SDS (sodium dodecyl sulfate) is a detergent that denatures proteins by binding to them and disrupting their native structure.
  • In non-denaturing gel electrophoresis, covering the gel in SDS ensures that the proteins are uniformly denatured and separated solely based on their size, rather than their native conformation.
31
Q

Why is albumin the darkest band in non-denaturing gel electrophoresis?

A
  • Albumin is the most prevalent protein in serum and plasma, and it migrates to the bottom of the gel due to its smaller size.
  • As a result, it appears as the darkest band because it concentrates near the bottom where the staining intensity is highest.
32
Q

What are “gamma” proteins in non-denaturing gel electrophoresis?

A
  • In non-denaturing gel electrophoresis of serum proteins, the gamma region typically represents antibodies (immunoglobulins), which are produced by plasma cells and migrate as distinct bands due to their size and charge.
  • These proteins are part of the immune response and play a crucial role in defending the body against pathogens.
33
Q

What are plasma proteins for?

A

○ Many proteins are present in low concentrations n hv specialized functions
○ Polypeptide hormones
○ Regulators of BP
Enzymes

34
Q

What role does albumin play in the blood?

A

Carries lipids, hormones (such as steroid hormones), and fatty acids, facilitating their transport in the bloodstream.

35
Q

How does albumin contribute to maintaining osmolarity in the blood?

A

Exerting oncotic pressure, which opposes hydrostatic pressure and prevents fluid from leaking out of the blood vessels into surrounding tissues.

36
Q

What is the significance of albumin binding to calcium?

A

Albumin binds to calcium ions (Ca2+) in the blood, contributing to the regulation of calcium levels and the transportation of calcium to various tissues.

37
Q

How does albumin interact with substances it carries?

A

Albumin binds weakly to substances, allowing it to readily take up molecules such as lipids and hormones and release them as needed based on physiological conditions.

38
Q

What are the functions of complement proteins when activated?

A
  • Opsonization (enhancing phagocytosis)
  • Chemotaxis (attracting immune cells to the site of infection or inflammation)
  • Lysis (causing cell membrane rupture in target cells)
  • Clumping (aggregation of pathogens for easier recognition and clearance)
39
Q

What is the role of γ globulins in the blood?

A
  • γ globulins, also known as serum antibodies or immunoglobulins (Ig), are a class of proteins involved in the immune response.
  • They function in recognizing and neutralizing pathogens, toxins, and other foreign substances in the bloodstream.
40
Q

What is the function of α-antitrypsin?

A
  • α-antitrypsin is a protease inhibitor that inhibits the enzyme trypsin.
  • By regulating the activity of trypsin, α-antitrypsin prevents excessive proteolytic damage to tissues, particularly in the lungs where trypsin-like enzymes may cause tissue degradation.
41
Q

How does haptoglobin contribute to maintaining iron levels in the body?

A
  • Protein that binds free hemoglobin (Hb) released into the bloodstream, particularly during the breakdown of red blood cells (hemolysis).
  • Helps maintain iron homeostasis in the body
    • Binds to free Hb → prevents oxidative damage
    • Facilitates removal by macrophages → recycle iron from Hb for reuse in new Hb synthesis
42
Q

What are the two pathways involved in blood coagulation?

A
  • Extrinsic: initiated by tissue trauma
  • Intrinsic: activated by blood trauma and damage to cells within blood vessels.
43
Q

How does the coagulation cascade lead to the formation of a blood clot?

A
  • Initiated by the activation of factor X → production and activation of thrombin.
  • Thrombin, in turn, converts fibrinogen into fibrin strands, which crosslink to form a stable blood clot, trapping cellular components.
44
Q

What happens if factor X is not adequately removed from circulation?

A
  • Excessive activation of the coagulation cascade → localized clot formation.
  • Factor X is typically removed by blood flow, but if this removal process is impaired, factor X may accumulate at the site of injury or trauma, contributing to the formation of abnormal blood clots.
45
Q

What is hemostasis?

A

Mechanism by which the body maintains the fluidity of blood within the circulatory system, preventing excessive bleeding or clot formation.

46
Q

How does clotting typically begin in the hemostatic process?

A

Clotting often begins with damage to the endothelium, the lining of blood vessels, triggering a series of events that lead to the formation of a blood clot.

47
Q

What role do thromboxins play in hemostasis?

A
  • Thromboxins, which are vasoconstrictors, are released upon activation of platelets in response to signaling molecules like ADP.
  • Thromboxins contribute to vasoconstriction, reducing blood flow to the damaged area and helping to limit bleeding.
48
Q

How do integrins such as GP1B and GP1A contribute to hemostasis?

A
  • Integrin proteins like GP1B and GP1A bind to factors that are typically unseen unless tissues are damaged.
  • These integrins play a role in platelet activation and aggregation, which are essential processes in forming a blood clot.
49
Q

What is the function of von Willebrand factor (vWF) in hemostasis?

A
  • Released upon endothelial damage and plays a crucial role in platelet adhesion and activation.
  • It helps to stabilize platelet plugs and promotes the formation of blood clots.
50
Q

What role do proteases play in hemostasis?

A

Proteases present in the blood cleave von Willebrand factor (vWF), contributing to the regulation of platelet adhesion and clot formation.

51
Q

How does thrombomodulin contribute to the regulation of clotting?

A
  • Thrombomodulin functions to inhibit further clot formation by preventing thrombin from binding to its receptors.
  • This helps maintain hemostatic balance and prevents excessive clotting.
52
Q

Why is it important to have mechanisms in place to stop clotting during the formation of a blood clot?

A
  • It is crucial to have regulatory mechanisms to prevent excessive clot formation and maintain hemostatic balance.
  • Without these mechanisms, there is a risk of forming excessive or inappropriate blood clots, which can lead to serious health complications such as thrombosis.
53
Q

What are fibrinolytic mechanisms, and how do they contribute to hemostasis?

A
  • Fibrinolytic mechanisms are responsible for breaking down blood clots once they are formed.
  • These mechanisms rely on the protease plasmin, which is derived from its inactive precursor plasminogen.
  • Plasminogen activation is catalyzed by tissue plasminogen activator (tPA) and other factors, leading to the digestion of fibrin and dissolution of the clot.

LF266: Blood and Circulation (12 decks)

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