Ganong's Review of Medical Physiology, 23rd Edition

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524 SECTION VI Cardiovascular Physiology GM-CSF erythro Late normoblast Reticulocyte Red blood cell GM-CSF thrombo Megakaryocyte Platelets Hemopoietic stem cell IL-1 IL-6 IL-3 GM-CSF GM-CSF IL-5 M-CSF G-CSF Monocyte Monocyte Tissue macrophage GM-CSF G-CSF SCF C o m m i t t e d s t e m c e l l s (progenitor cell) FIGURE 32–3 Development of various formed elements of the blood from bone marrow cells. Cells below the horizontal line are found in normal peripheral blood. The principal sites of action of erythropoietin (erythro) and the various colony-stimulating factors (CSF) that stimulate the differentiation of the components are indicated. G, granulocyte; M, macrophage; IL, interleukin; thrombo, thrombopoietin; SCF, stem cell factor. compete with O 2 for binding to deoxygenated hemoglobin, decreasing the affinity of hemoglobin for O 2 by shifting the positions of the four peptide chains (quaternary structure). The details of the oxygenation and deoxygenation of hemoglobin and the physiologic role of these reactions in O 2 transport are discussed in Chapter 36. When blood is exposed to various drugs and other oxidizing agents in vitro or in vivo, the ferrous iron (Fe 2+ ) that is nor- Juvenile Segmented Neutrophil Eosinophil Basophil Polymorphonuclear cells IL-4 IL-3 Bone marrow lymphocyte precursor Bursal equiv. Thymus B T Lymphocytes mally in the molecule is converted to ferric iron (Fe 3+ ), forming methemoglobin. Methemoglobin is dark-colored, and when it is present in large quantities in the circulation, it causes a dusky discoloration of the skin resembling cyanosis (see Chapter 36). Some oxidation of hemoglobin to methemoglobin occurs normally, but an enzyme system in the red cells, the dihydronicotinamide adenine dinucleotide (NADH)methemoglobin reductase system, converts methemoglobin
FIGURE 32–4 Human red blood cells and fibrin fibrils. Blood was placed on a polyvinyl chloride surface, fixed, and photographed with a scanning electron microscope. Reduced from ×2590. (Courtesy of NF Rodman.) back to hemoglobin. Congenital absence of this system is one cause of hereditary methemoglobinemia. Carbon monoxide reacts with hemoglobin to form carbon monoxyhemoglobin (carboxyhemoglobin). The affinity of hemoglobin for O 2 is much lower than its affinity for carbon monoxide, which consequently displaces O 2 on hemoglobin, reducing the oxygen-carrying capacity of blood (see Chapter 36). TABLE 32–2 Characteristics of human red cells. a CHAPTER 32 Blood as a Circulatory Fluid & the Dynamics of Blood & Lymph Flow 525 Male Female Hematocrit (Hct) (%) 47 42 Red blood cells (RBC) (10 6 /μL) 5.4 4.8 Hemoglobin (Hb) (g/dL) 16 14 Mean corpuscular volume (MCV) (fL) Mean corpuscular hemoglobin (MCH) (pg) Mean corpuscular hemoglobin concentration (MCHC) (g/dL) Mean cell diameter (MCD) (μm) = Hct × 10 RBC (106 /μL) = Hb × 10 RBC (106 /μL) = Hb × 100 Hct = Mean diameter of 500 cells in smear 87 87 29 29 34 34 7.5 7.5 a Cells with MCVs > 95 fL are called macrocytes; cells with MCVs < 80 fL are called microcytes; cells with MCHs < 25 g/dL are called hypochromic. CLINICAL BOX 32–1 Red Cell Fragility Red blood cells, like other cells, shrink in solutions with an osmotic pressure greater than that of normal plasma. In solutions with a lower osmotic pressure they swell, become spherical rather than disk-shaped, and eventually lose their hemoglobin (hemolysis). The hemoglobin of hemolyzed red cells dissolves in the plasma, coloring it red. A 0.9% sodium chloride solution is isotonic with plasma. When osmotic fragility is normal, red cells begin to hemolyze when suspended in 0.5% saline; 50% lysis occurs in 0.40–0.42% saline, and lysis is complete in 0.35% saline. In hereditary spherocytosis (congenital hemolytic icterus), the cells are spherocytic in normal plasma and hemolyze more readily than normal cells in hypotonic sodium chloride solutions. Abnormal spherocytes are also trapped and destroyed in the spleen, meaning that hereditary spherocytosis is one of the most common causes of hereditary hemolytic anemia. The spherocytosis is caused by mutations in proteins that make up the membrane skeleton of the erythrocyte, which normally maintain the shape and flexibility of the red cell membrane, including spectrin, the transmembrane protein band 3, and the linker protein, ankyrin. The condition can be cured by splenectomy, but this is not without other risks. Red cells can also be lysed by drugs and infections. The susceptibility of red cells to hemolysis by these agents is increased by deficiency of the enzyme glucose 6phosphate dehydrogenase (G6PD), which catalyzes the initial step in the oxidation of glucose via the hexose monophosphate pathway (see Chapter 1). This pathway generates dihydronicotinamide adenine dinucleotide phosphate (NADPH), which is needed for the maintenance of normal red cell fragility. Severe G6PD deficiency also inhibits the killing of bacteria by granulocytes and predisposes to severe infections. HEMOGLOBIN IN THE FETUS The blood of the human fetus normally contains fetal hemoglobin (hemoglobin F). Its structure is similar to that of hemoglobin A except that the β chains are replaced by γ chains; that is, hemoglobin F is α 2γ 2. The γ chains also contain 146 amino acid residues but have 37 that differ from those in the β chain. Fetal hemoglobin is normally replaced by adult hemoglobin soon after birth (Figure 32–8). In certain individuals, it fails to disappear and persists throughout life. In the body, its O 2 content at a given PO 2 is greater than that of adult hemoglobin because it binds 2,3-BPG less avidly. Hemoglobin F is critical to facilitate movement of O 2 from the maternal to the fetal circulation, particularly at later stages of gestation where oxygen demand increases (see Chapter 34). In young embryos there are, in addition, ζ and ε chains, forming Gower 1
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Ranges of Normal Values in Human Wh
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Copyright © 2010 by The McGraw-Hil
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iv Key Features of the 23rd Edition
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About the Authors KIM E. BARRETT Ki
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viii CONTENTS 27. Digestion, Absorp
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2 SECTION I Cellular & Molecular Ba
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10 SECTION I Cellular & Molecular B
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80 SECTION II Physiology of Nerve &
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100 SECTION II Physiology of Nerve
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168 SECTION III Central & Periphera
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302 SECTION IV Endocrine & Reproduc
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430 SECTION V Gastrointestinal Phys
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Page 486 and 487: 474 SECTION V Gastrointestinal Phys
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Page 502 and 503: 490 SECTION VI Cardiovascular Physi
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574 SECTION VI Cardiovascular Physi
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588 SECTION VII Respiratory Physiol
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640 SECTION VIII Renal Physiology T
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642 SECTION VIII Renal Physiology m
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644 SECTION VIII Renal Physiology F
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646 SECTION VIII Renal Physiology N
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650 SECTION VIII Renal Physiology G
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652 SECTION VIII Renal Physiology t
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654 SECTION VIII Renal Physiology I
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660 SECTION VIII Renal Physiology C
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662 SECTION VIII Renal Physiology d
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668 SECTION VIII Renal Physiology p
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670 SECTION VIII Renal Physiology l
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672 SECTION VIII Renal Physiology A
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676 SECTION VIII Renal Physiology E
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678 SECTION VIII Renal Physiology o
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680 SECTION VIII Renal Physiology I
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682 SECTION VIII Renal Physiology C
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688 Answers to Multiple Choice Ques
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690 INDEX Angiotensin III, 671 Angi
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692 INDEX Cannabinoids, 145, 179 Ca
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694 INDEX Climbing fibers, 255 Clin
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696 INDEX Endocrine functions of pa
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698 INDEX Flaccid paralysis, 244 Fl
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700 INDEX Hearing (continued) affer
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702 INDEX Intrinsic system, 532 Int
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704 INDEX Monoamines (continued) hi
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706 INDEX Pacemaker (continued) imp
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708 INDEX Proprioceptors, 632-633 P
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710 INDEX Respiratory compensation,
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712 INDEX Supratentorial lesions, 2
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714 INDEX Vestibular system, 213-21
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Ganong's Review of Medical Physiology, 23rd Edition

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