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1
Figure 2–2 Proteins associated with the membrane lipid bilayer.
(a) The fluid mosaic model of membrane structure emphasizes that the phospholipid
bilayer of a membrane also contains proteins inserted in it or associated with its surface
(peripheral proteins) and that many of these proteins move within the fluid lipid phase.
Integral proteins are firmly embedded in the lipid layers; those that completely span the
bilayer are called transmembrane proteins. Hydrophobic amino acids of these proteins
interact with the hydrophobic fatty acid portions of the membrane lipids. Both the proteins
and lipids may have externally exposed oligosaccharide chains.
(b) When cells are frozen and fractured (cryofracture), the lipid bilayer of membranes is
often cleaved along the hydrophobic center. Splitting occurs along the line of weakness
formed by the fatty acid tails of phospholipids. Electron microscopy of such cryofracture
preparation replicas provides a useful method for studying membrane structures. Most of
the protruding membrane particles seen (1) are proteins or aggregates of proteins that
remain attached to the half of the membrane adjacent to the cytoplasm (P or protoplasmic
face). Fewer particles are found attached to the outer half of the membrane (E or
extracellular face). Each protein bulging on one surface has a corresponding depression (2)
on the opposite surface.
2
Figure 2–3 Membrane proteins.
Both protein and lipid components often have covalently attached oligosaccharide chains
exposed at the external membrane surface. These contribute to the cell’s glycocalyx, which
provides important antigenic and functional properties to the cell surface. Membrane
proteins serve as receptors for various signals coming from outside cells, as parts of
intercellular connections, and as selective gateways for molecules entering the cell.
Transmembrane proteins often have multiple hydrophobic regions buried within the lipid
bilayer to produce a channel or other active site for specific transfer of substances through
the membrane.
3
Figure 2–4 Experiment demonstrating the fluidity of membrane proteins.
(a) Two types of cells were grown in tissue cultures, one with fluorescently labeled
transmembrane proteins in the plasmalemma (right) and one without.
(b) Cells of each type were fused together experimentally into hybrid cells.
(c) Minutes after the fusion of the cell membranes, the fluorescent proteins of the labeled
cell spread to the entire surface of the hybrid cells. Such experiments provide important
data supporting the fluid mosaic model. However, many membrane proteins show more
restricted lateral movements, being anchored in place by links to the cytoskeleton.
4
Figure 2–5 Major mechanisms by which molecules cross membranes.
Lipophilic and some small, uncharged molecules can cross membranes by simple diffusion
(a).
Most ions are transported through membranes in proteins whose structure includes an ion‐
specific channel (b).
Many other larger, water‐soluble molecules require binding to sites on selective carrier
proteins or transporters, which then change their conformations and release the molecule
to the other side of the membrane (c). Channel and carrier proteins may facilitate diffusion
requiring no energy or may involve active transport requiring energy from ATP.
5
Figure 2–6 Three major forms of endocytosis.
There are three general types of endocytosis:
(a) Phagocytosis involves the extension from the cell of large folds called pseudopodia that
engulf particles, for example bacteria, and then internalize this material into a cytoplasmic
vacuole or phagosome.
(b) In pinocytosis the cell membrane invaginates (dimples inward) to form a pit containing
a drop of extracellular fluid. The pit pinches off inside the cell when the cell membrane
fuses and forms a pinocytotic vesicle containing the fluid.
(c) Receptor‐mediated endocytosis includes membrane proteins called receptors that bind
specific molecules (ligands). When many such receptors are bound by their ligands, they
aggregate in one membrane region, which then invaginates and pinches off to create a
vesicle or endosome containing both the receptors and the bound ligands.
6
Figure 2–6 Three major forms of endocytosis.
There are three general types of endocytosis:
(a) Phagocytosis involves the extension from the cell of large folds called pseudopodia that
engulf particles, for example bacteria, and then internalize this material into a cytoplasmic
vacuole or phagosome.
(b) In pinocytosis the cell membrane invaginates (dimples inward) to form a pit containing
a drop of extracellular fluid. The pit pinches off inside the cell when the cell membrane
fuses and forms a pinocytotic vesicle containing the fluid.
(c) Receptor‐mediated endocytosis includes membrane proteins called receptors that bind
specific molecules (ligands). When many such receptors are bound by their ligands, they
aggregate in one membrane region, which then invaginates and pinches off to create a
vesicle or endosome containing both the receptors and the bound ligands.
7
Figure 2–6 Three major forms of endocytosis.
There are three general types of endocytosis:
(a) Phagocytosis involves the extension from the cell of large folds called pseudopodia that
engulf particles, for example bacteria, and then internalize this material into a cytoplasmic
vacuole or phagosome.
(b) In pinocytosis the cell membrane invaginates (dimples inward) to form a pit containing
a drop of extracellular fluid. The pit pinches off inside the cell when the cell membrane
fuses and forms a pinocytotic vesicle containing the fluid.
(c) Receptor‐mediated endocytosis includes membrane proteins called receptors that bind
specific molecules (ligands). When many such receptors are bound by their ligands, they
aggregate in one membrane region, which then invaginates and pinches off to create a
vesicle or endosome containing both the receptors and the bound ligands.
8
Figure 2–7 Receptor‐mediated endocytosis involves regulated membrane trafficking.
Major steps during and after endocytosis are indicated diagrammatically in part a. Ligands
bind at high affinity to specific surface receptors, which then associate with specific
cytoplasmic proteins, including clathrin and adaptor proteins, and aggregate in membrane
regions to form coated pits. Clathrin facilitates invagination of the pits, and another ‐
peripheral membrane protein, dynamin, forms constricting loops around the developing
neck of the pit, which cause the region to pinch off as a coated vesicle. The clathrin lattice
of coated pits (CP) and vesicles (CV) is shown ultrastructurally in part b.
The internalized vesicles lose their clathrin coats and ‐usually merge by membrane fusion
with other endosomal vesicles. Ligands may have different fates within the endosomal
compartment:
• Receptors and ligands may be carried to late endosomes and then to lysosomes for
degradation.
• Ligands may be released internally and the receptors recycled to the cell surface.
• Vesicles may move to and fuse with another cell surface, where the ligands are released
again outside the cell (transcytosis).
(Figure 2–7b, with permission, from Dr John Heuser, Department of Cell Biology and
Physiology, Washington University School of Medicine, St. Louis, MO.)
9
Figure 2–8 Major types of membrane receptors.
Protein and most small ligands are hydrophilic molecules that bind transmembrane protein
receptors to initiate changes in the target cell. (a) Channel‐linked receptors bind ligands
such as neurotransmitters and open to allow influx of specific ions. (b) Enzymatic receptors
are usually protein kinases that are activated to phosphorylate (and usually activate) other
proteins upon ligand binding. (c) G‐protein–coupled receptors bind ligand, changing the
conformation of its G‐protein subunit, allowing it to bind GTP, and activating and releasing
this protein to in turn activate other proteins such as ion channels and adenyl cyclase.
10
Figure 2–9 Polyribosomes: free or bound to the endoplasmic reticulum.
Free polyribosomes (not attached to the endoplasmic reticulum, or ER) synthesize cytosolic
and cytoskeletal proteins and proteins for import into the nucleus, mitochondria, and
peroxisomes.
Proteins that are to be incorporated into membranes, stored in lysosomes, or eventually
secreted from the cell are made on polysomes attached to the membranes of ER. The
proteins produced by these ribosomes are segregated during translation into the interior of
the ER’s membrane cisternae.
In both pathways misfolded proteins are conjugated to ubiquitin and targeted for
proteasomal degradation.
11
Figure 2–10 Rough and smooth endoplasmic reticulum.
(a) The endoplasmic reticulum is an anastomosing network of intercommunicating
channels or cisternae formed by a continuous membrane, with some regions that bear
polysomes appearing rough and other regions appearing smooth. While RER is the site for
synthesis of most membrane‐bound proteins, three diverse activities are associated with
smooth ER: (1) lipid biosynthesis, (2) detoxification of potentially harmful compounds, and
(3) sequestration of Ca++ ions. Specific cell types with well‐developed SER are usually
specialized for one of these functions.
(b) By TEM cisternae of RER appear separated, but they actually form a continuous channel
or compartment in the cytoplasm. The interconnected membranous cisternae of RER are
flattened, while those of SER are frequently tubular. 14,000X.
(c) In a very thin cultured endothelial cell, both ER (green) and mitochondria (orange) can
be visualized with vital fluorescent dyes that are sequestered specifically into those
organelles. This staining method with intact cells clearly reveals the continuous, lacelike ER
present in all regions of the cytoplasm.
(Figure 2–10c, with permission, from Invitrogen.)
12
Figure 2–11 Movement of polypeptides into the RER.
The newly translated amino terminus of a protein to be incorporated into membranes or
sequestered into vesicles contains 15‐40 amino acids that include a specific sequence of
hydrophobic residues comprising the signal sequence or signal peptide. This sequence is
bound by a signal‐recognition particle (SRP), which then recognizes and binds a receptor on
the ER. Another receptor in the ER membrane binds a structural protein of the large
ribosomal subunit, more firmly attaching the ribosome to the ER. The hydrophobic signal
peptide is translocated through a protein pore (translocon) in the ER membrane, and the
SRP is freed for reuse. The signal peptide is removed from the growing protein by a
peptidase and translocation of the growing polypeptide continues until it is completely
segregated into the ER cisterna.
13
Figure 2–12 Protein localization and cell morphology.
The ultrastructure and general histologic appearance of a cell are determined by the nature
of the most prominent proteins the cell is making.
(a) Cells that make few or no proteins for secretion have very little RER, with essentially all
polyribosomes free in the cytoplasm.
(b) Cells that synthesize, segregate, and store various proteins in specific secretory granules
or vesicles always have RER, a Golgi apparatus, and a supply of granules containing the
proteins ready to be secreted.
(c) Cells with extensive RER and a well‐developed Golgi apparatus show few secretory
granules because the proteins undergo exocytosis immediately after Golgi processing is
complete. Many cells, especially those of epithelia, are polarized, meaning that the
distribution of RER and secretory vesicles is different in various regions or poles of the cell.
(d) Epithelial cells specialized for secretion have distinct polarity, with RER abundant at
their basal ends and mature secretory granules at the apical poles undergoing exocytosis
into an enclosed extracellular compartment, the lumen of a gland.
14
Figure 2–13 Golgi apparatus.
The Golgi apparatus is a highly plastic, morphologically complex system of membrane vesicles and
cisternae in which proteins and other molecules made in the RER undergo further modification and
sorting into specific vesicles destined for different roles in the cell.
(a) TEM of the Golgi apparatus provided early evidence about how this organelle functions. To the
left is a cisterna of RER and close to it are many small vesicles at the cis face (CF), or receiving face,
of the Golgi apparatus, merging with the first of several flattened Golgi cisternae. In the center are
the characteristic flattened, curved, and stacked medial cisternae of the complex. Cytological and
molecular data suggest that other transport vesicles (TV) move proteins serially through the
cisternae until at the trans face (TF), or shipping region, larger condensing secretory vesicles (SV)
and other vacuoles emerge to carry the modified proteins elsewhere in the cell. Formation and
fusion of the vesicles through the Golgi apparatus is controlled by specific membrane proteins.
X30,000.
Inset: a small region of a Golgi apparatus in a 1‐μm section from a silver‐stained cell, demonstrating
abundant glycoproteins within cisternae.
(b) Morphological aspects of the Golgi apparatus are revealed more clearly by SEM, which shows a
three‐dimensional snapshot of the region between RER and the Golgi membrane compartments.
Cells may have multiple Golgi apparatuses, each with the general organization shown here and
typically situated near the cell nucleus. 30,000X.
(c) The Golgi apparatus location can be clearly seen in intact cultured cells processed by
immunocytochemistry using an antibody against golgin‐97 to show the many complexes of Golgi
vesicles (green), all near the nucleus, against a background of microfilaments organized as stress
fibers and stained with fluorescent phalloidin (violet). Because of the abundance of lipids in its
many membranes, the Golgi apparatus is difficult to visualize in typical paraffin‐embedded, H&E‐
stained sections. In developing white blood cells with active Golgi complexes, the organelle can
sometimes be seen as a faint unstained juxtanuclear region (sometimes called a “Golgi ghost”)
surrounded by basophilic cytoplasm.
(Figure 2–13b reproduced, with permission, from Naguro T, Iino A. Prog Clin Biol Res. 1989;295:250;
Figure 2–13c, with permission, from Invitrogen.)
15
Figure 2–14 Summary of functions within the Golgi apparatus.
The main molecular processes are listed at the right, with the major compartments where
they occur. In the trans Golgi network, the proteins and glycoproteins combine with
specific receptors that guide them to the next stages toward their destinations.
16
Figure 2–15 Secretory granules.
TEM of one area of a pancreatic acinar cell shows numerous mature, electron‐dense
secretory granules (S) in association with condensing vacuoles (C) of the Golgi apparatus
(G). Such granules form as the contents of the Golgi vacuoles become more condensed. In
H&E‐stained sections secretory granules are often shown as intensely eosinophilic
structures, which in polarized epithelial cells are concentrated at the apical region prior to
exocytosis. X18,900.
17
Figure 2–16 Lysosomes.
Lysosomes are spherical membrane‐enclosed vesicles that function as sites of intracellular
digestion and are particularly numerous in cells active after the various types of
endocytosis. Lysosomes are not well shown on H&E‐stained cells but can be visualized by
light microscopy after staining with toluidine blue.
(a) Cells in a kidney tubule show numerous purple lysosomes (L) in the cytoplasmic area
between the basally located nuclei (N) and apical ends of the cells at the center of the
tubule. Using endocytosis, these cells actively take up small proteins in the lumen of the
tubule, degrade the proteins in lysosomes, and then release the resulting amino acids for
reuse. X300.
(b) Lysosomes in cultured vascular endothelial cells can be specifically stained using
fluorescent dyes sequestered into these organelles (green), which are abundant around the
blue Hoechst‐stained nucleus. Mitochondria (red) are scattered among the lysosomes.
(c) In the TEM lysosomes (L) have a characteristic very electron‐dense appearance and are
shown here near groups of Golgi cisternae (G). The less electron‐dense lysosomes
represent heterolysosomes in which digestion of the contents is under way. The cell is a
macrophage with numerous fine cytoplasmic extensions (arrows). X15,000.
(Figure 2–16b, with permission, from Invitrogen.)
18
Figure 2–17 Lysosomal functions.
Synthesis of lysosomal enzymes occurs in the RER, with packaging in the Golgi apparatus.
Endocytosis produces vesicles that fuse with endosomes before merging with lysosomes.
Phagocytic vacuoles (or phagosomes) fuse with primary lysosomes to become secondary
lysosomes (or heterolysosomes), in which ingested material is degraded.
Autophagosomes, such as those depicted here with a mitochondrion in the process of
digestion, are formed after nonfunctional or surplus organelles become enclosed with
membrane and the resulting structure fuses with a lysosome. The products of lysosomal
digestion are recycled to the cytoplasm, but indigestible molecules remain in a membrane‐
enclosed residual body, which may accumulate in long‐lived cells as lipofuscin. In some
cells, such as osteoclasts, the lysosomal enzymes are secreted into a restricted extracellular
compartment.
19
Figure 2–18 Autophagy.
Autophagy is a process in which the cell uses lysosomes to dispose of excess or
nonfunctioning organelles or membranes. Membrane that appears to emerge from the SER
encloses the organelles to be destroyed, forming an autophagosome that then fuses with a
lysosome for digestion of the contents. In this TEM the two autophagosomes at the upper
left contain portions of RER more electron dense than the neighboring normal RER and one
near the center contains what may be mitochondrial membranes plus RER. Also shown is a
vesicle with features of a residual body (RB). 30,000X.
20
Figure 2–19 Mitochondria in the light microscope.
(a) In certain sectioned cells stained with H&E, mitochondria appear throughout the
cytoplasm as numerous eosinophilic structures. The mitochondria usually appear round or
slightly elongated and are more numerous in cytoplasmic regions with higher energy
demands, such as near the cell membrane in cells undergoing much active transport. The
central nuclei are also clearly seen in these cells.
(b) Entire mitochondria can be shown in cultured cells, such as the endothelial cells shown
here, and often appear as the elongated structures (shown in yellow or orange here),
usually arrayed in parallel along microtubules. Such preparations also show that
mitochondrial shape can be quite plastic and variable. Specific mitochondrial staining such
as that shown here involves incubating living cells with specific fluorescent compounds that
are specifically sequestered into these organelles, followed by fixation and
immunocytochemical staining of the microtubules. In this preparation, microtubules are
stained green and mitochondria appear yellow or orange, depending on their association
with the green microtubules. The cell nucleus was stained with DAPI.
(Figure 2–19b, with permission, from Invitrogen.)
21
Figure 2–20 Mitochondrial structure and ATP formation. (Opposite)
The two mitochondrial membranes and the matrix can be seen in the TEM and diagram.
(a) The outer membrane is smooth and the inner membrane has many sharp folds called cristae
that increase its surface area greatly. Cristae are more numerous in mitochondria of highly active
cells. The innermost mitochondrial matrix is a gel containing numerous enzymes. The inner
membrane surface in contact with the matrix is studded with many multimeric protein complexes
resembling globular units on short stalks. These contain the ATP synthase complexes that generate
most of the cell’s ATP.
(b) Metabolites such as pyruvate and fatty acids enter mitochondria via membrane porins and are
converted to acetyl CoA by matrix enzymes of the citric acid cycle (or Krebs cycle), yielding some
ATP and NADH (nicotinamide adenine dinucleotide), a major source of electrons for the electron‐
transport chain. The movement of electrons through the protein complexes of the inner
membrane’s electron‐transport system is ‐accompanied by the directed movement of protons (H+)
from the matrix into the intermembranous space. The inner ‐membrane is impermeable to protons,
and the result is an electrochemical gradient across the membrane. The other membrane‐
associated proteins make up the ATP synthase systems, each of which forms a globular complex on
a stalk‐like structure projecting from the matrix side of the inner ‐membrane. A channel in this
enzyme complex allows proton flow down the electrochemical gradient and across the membrane
back into the matrix. The channeled movement of protons causes rapid spinning of specific
polypeptides in the globular ATP synthase complex, converting the energy of proton flow into
mechanical energy. Other subunit proteins of the complex store this energy in the new phosphate
bond of ATP which then leaves the mitochondrion for use throughout the cell.
22
Figure 2–21 Peroxisomes.
Peroxisomes are small spherical, membranous organelles, containing enzymes that use O2
to remove hydrogen atoms from fatty acids, in a reaction that produces hydrogen peroxide
(H2O2) that must be broken down to water and O2 by another enzyme, catalase.
(a) By TEM peroxisomes (P) generally show a matrix of moderate electron density.
Aggregated electron‐dense particles represent glycogen (G). X30,000.
(b) Peroxisomes (P) in most species are characterized by a central, more electron‐dense
crystalloid aggregate of constituent enzymes, as shown here. X60,000.
(c) A cultured endothelial cell processed by immunocytochemistry shows many
peroxisomes (green) distributed throughout the cytoplasm among the vitally stained
elongate mitochondria (red) around the DAPI‐stained nucleus (blue). Peroxisomes shown
here were specifically stained using an antibody against the membrane protein PMP70.
(Figure 2–21c, with permission, from Invitrogen.)
23
Figure 2–22 Microtubules and actin filaments in cytoplasm.
(a) Microtubules (MT) and actin microfilaments (MF) can both be clearly distinguished in
this TEM of fibroblast cytoplasm, which provides a good comparison of the relative
diameters of these two cytoskeletal components. X60,000.
(b) Arrays of microfilaments and microtubules are easily demonstrated by
immunocytochemistry using antibodies against their subunit proteins, as in this cultured
cell. Actin filaments (red) are most concentrated at the cell periphery, forming prominent
circumferential bundles from which finer filaments project into cellular extensions and
push against the cell membrane. Actin filaments form a dynamic network important for cell
shape changes such as those during cell division, locomotion, and formation of cellular
processes, folds, pseudopodia, lamellipodia, microvilli, etc, which serve to change a cell’s
surface area or give direction to a cell’s crawling movements.
Microtubules (green/yellow) are oriented in arrays that generally extend from the
centrosome area near the nucleus into the most peripheral extensions. Besides serving to
stabilize cell shape, microtubules form the tracks for kinesin‐based transport of vesicles and
organelles into the cell periphery and dynein‐based transport toward the cell nucleus.
(Figure 2–22b, with permission, from Dr Albert Tousson, University of Alabama—
Birmingham High Resolution Imaging Facility, Birmingham.)
24
Figure 2–23 Dynamic instability of microtubules.
At stable tubulin concentrations some microtubules grow while others shrink, each existing
in a condition called dynamic instability. In cytoplasmic areas where the tubulin
concentration is high, tubulin GTP is added at a microtubule’s (+) end faster than the
incorporated GTP can be hydrolyzed. The resulting “GTP cap” stabilizes that end of the
microtubule and promotes further rapid growth. As free tubulin concentrations decrease,
the rate of growth also decreases, thereby allowing GTP hydrolysis to catch up. The
resulting “GDP cap” at the microtubule end is unstable and favors rapid depolymerization
(termed “catastrophe”). This increases the local concentration of free, monomeric tubulin
that “rescues” the microtubule before it completely disappears and produces another short
period of microtubule elongation.
Dynamic instability allows the growing ends of microtubules to explore the cytoplasm and
become stabilized when they contact stabilizing structures, such as kinetochores on
chromosomes early in mitosis (see Chapter 3).
25
Figure 2–24 Centrosome.
The centrosome is the microtubule‐organizing center for the mitotic spindle and consists of
paired centrioles. The TEM reveals that the two centrioles in a centrosome exist at right
angles to each other in a dense matrix of free tubulin subunits and other proteins. Each
centriole consists of nine microtubular triplets. In a poorly understood process, the ‐
centrosome duplicates itself and is divided equally during a cell’s interphase, each half
having a duplicated centriole pair. At the onset of mitosis, the two daughter centrosomes
move to opposite sides of the nucleus and become the two poles of the mitotic spindle of
microtubules attaching to chromosomes.
26
Figure 2–25 Actin filament treadmilling.
(a) Actin filaments or microfilaments are helical two‐stranded polymers assembled from
globular actin subunits.
(b) Assembly of actin filaments (F‐actin) is polarized, with G‐actin subunits added to the
plus (+) end and removed at the minus (–) end. Even actin filaments of a constant length
are highly dynamic structures, balancing G‐actin assembly and disassembly at the opposite
ends, with a net movement or flow along the polymer known as treadmilling.
(Figure 2–25a, with permission, from John Heuser, ‐Washington University School of
Medicine, St. Louis, MO.)
27
Figure 2–26 Roles of major actin‐binding proteins in regulating the organization of
microfilaments.
A large number of proteins regulate the assembly of microfilaments and the interactions of
these filaments with one another. By altering microfilament length and cross‐linking, such
proteins greatly influence physical properties of the local cytoplasm.
28
Figure 2–27 Intermediate filaments of keratin.
Intermediate filaments (IF) display an average diameter of 8‐10 nm, between that of actin
filaments and microtubules, and serve to provide mechanical strength or stability to cells. A
large and important class of intermediate filaments is composed of keratin subunits, which
are prominent in epithelial cells. Bundles of keratin filaments called tonofibrils associate
with certain classes of intercellular junctions (J) common in epithelial cells and are easily
seen with the TEM, as shown here in two extensions in an epidermal cell bound to a
neighboring cell. 60,000X.
29
Figure Credits
Figure numbers in boldface indicate those appearing for the first time in this text; figure numbers in lightface indicate those taken from other sources.
Berman I. Color Atlas of Basic Histology. 3rd ed. New York, NY: McGraw‐Hill; 2003.
Eckel CM. Human Anatomy Lab Manual. New York, NY: McGraw‐Hill; 2008.
Fitzpatrick TB, et al. Dermatology in General Medicine. New York, NY: McGraw‐Hill; 1971.
Hartwell L, Hood L, Goldberg M., et al. Genetics: From Genes to Genomes. 4th ed. New York, NY: McGraw‐Hill; 2010.
Kaushansky K, Lichtman M, Beutler E, et al. Williams Hematology. 8th ed. New York, NY: McGraw‐Hill; 2010.
Lewis R, Gaffin D, Hoefnagels M, et al. Life. 5th ed. New York, NY: McGraw‐Hill; 2004.
Lichtman MA, Shafer MS, Felgar RE, Wang N: Lichtman’s Atlas of Hematology. New York, NY: 2007. http://www.accessmedicine.com.
McKinley M, O’Loughlin VD. Human Anatomy. 2nd ed. New York, NY: McGraw‐Hill; 2008.
McKinley M, O’Loughlin VD. Human Anatomy. 3rd ed. New York, NY: McGraw‐Hill; 2012.
McKinley MP, O’Loughlin VD, Bidle TS. Anatomy & Physiology: An Integrative Approach. New York, NY: McGraw‐Hill; 2013.
Murray RK, Bender DA, Botham KM, et al. Harper’s Illustrated Biochemistry. 28th ed. New York, NY: McGraw‐Hill; 2009.
Raven P, Johnson GB, Losos JB, et al. Biology. 7th ed. New York, NY: McGraw‐Hill; 2005.
Weiss L, Greep RO. Histology. 4th ed. New York, NY: McGraw‐Hill; 1977.
Widmaier EP, Raff H, Strang KT. Vander’s Human Physiology. 11th ed. New York, NY: McGraw‐Hill; 2008.
Chapter 1
1‐14: McKinley et al 1‐5.
Chapter 2
2‐3: McKinley et al 4‐5a; 2‐6: McKinley, O’Loughlin (2nd ed) 2‐7; 2‐8: McKinley et al 4‐19; 2‐10a: McKinley, O’Loughlin 2‐8; 2‐10b: McKinley, O’Loughlin 2‐8; 2‐13a (left side): McKinley, O’Loughlin 2‐9; 2‐16b: McKinley, O’Loughlin 2‐10; 2‐16c: McKinley, O’Loughlin 2‐10; 2‐20 (top part): McKinley, O’Loughlin (2nd ed) 2‐12; 2‐21b: McKinley, O’Loughlin 2‐11; 2‐24:
McKinley, O’Loughlin (2nd ed) 2‐35.
Chapter 3
3‐2: McKinley, O’Loughlin 2‐17; 3‐10: Hartwell et al 17‐22b; 3‐12 (right): McKinley, O’Loughlin 2‐19; 3‐18: Lewis et al 9‐10.
Chapter 4
4‐4: Raven 7‐13; 4‐5: Weiss 3‐12; 4‐20: McKinley, O’Loughlin (2nd ed) 4‐4; 4‐15d: Berman 1‐16; 4‐21a: McKinley, O’Loughlin 4‐6; 4‐21b: McKinley, O’Loughlin 4‐6; 4‐21c: McKinley, O’Loughlin 4‐6c; 4‐27: McKinley et al 4‐14.
Chapter 5
5‐2: McKinley et al 16‐3; 5‐3a: Berman 2‐6; 5‐8a: Berman 2‐7; 5‐12b: Berman 2‐24; 5‐17b: Murray et al 48‐6.
Chapter 6
6‐1c: Berman 2‐20; 6‐1d: Berman 2‐19.
Chapter 7
7‐1: McKinley, O’Loughlin (2nd ed) 6‐1; 7‐5a: Berman 3‐4.
Chapter 8
8‐1: McKinley et al 7‐7; 8‐9: Berman 4‐4; 8‐13a: Berman 5‐7; 8‐14: McKinley, O’Loughlin (2nd ed) 6‐11; 8‐16: McKinley, O’Loughlin (2nd ed) 6‐12a,b; 8‐17a: Berman 5‐3; 8‐17b: Berman 5‐4; 8‐18: McKinley, O’Loughlin (2nd ed) 6‐16; 8‐19a: McKinley, O’Loughlin (2nd ed) 9‐4.
Chapter 9
9‐1: McKinley, O’Loughlin (2nd ed) 14‐1; 9‐2: McKinley, O’Loughlin (2nd ed) 14‐16; 9‐3: McKinley et al 12‐2; 9‐4: McKinley et al 12‐1 (table); 9‐5: Berman 6‐8; 9‐6a: McKinley, O’Loughlin (2nd ed) 14‐14b; 9‐7: McKinley, O’Loughlin (2nd ed) 14‐13c; 9‐8b: Eckel 4‐28b; 9‐9: McKinley, O’Loughlin (2nd ed) 14‐7; 9‐10a: Berman 9‐11a; 9‐17: Eckel 16‐1c; 9‐18a:
McKinley, O’Loughlin (2nd ed) 16‐2b; 9‐19: McKinley, O’Loughlin 15‐4; 9‐20c: McKinley, O’Loughlin (2nd ed) 15‐7a; 9‐21a: McKinley, O’Loughlin (2nd ed) 14‐8(1); 9‐21b: McKinley, O’Loughlin (2nd ed) 14‐8(2); 9‐21c: McKinley, O’Loughlin (2nd ed) 14‐8(3); 9‐21d: McKinley, O’Loughlin (2nd ed) 14‐8(4); 9‐22: Berman 6‐21; 9‐25: McKinley, O’Loughlin (2nd ed) 14‐
10a; 9‐26a: McKinley, O’Loughlin (2nd ed) 14‐12a; 9‐26b: Berman 6‐15; 9‐26d: McKinley, O’Loughlin (2nd ed) 14‐12b; 9‐28b: Berman 6‐19; 9‐28d: Berman 6‐18; 9‐29a: Berman 6‐10; 9‐29c: Berman 6‐12.
Chapter 10
10‐1: Widmaier 9‐1; 10‐2: McKinley, O’Loughlin (2nd ed) 10‐4; 10‐3: McKinley et al 10‐1; 10‐7a: Berman 7‐2; 10‐7c: Berman 7‐4; 10‐8: McKinley, O’Loughlin (2nd ed) 10‐6; 10‐9: McKinley et al 10‐4; McKinley, O’Loughlin 10‐9; 10‐12: McKinley et al 10‐12; 10‐13: Widmaier 9‐14; 10‐14a: Widmaier 10‐4; Berman 7‐6; 10‐14b: Berman 7‐7; 10‐15: McKinley, O’Loughlin
(2nd ed) 10‐12; 10‐16: McKinley, O’Loughlin (2nd ed) 22‐10a; 10‐17a: Berman 7‐10; 10‐17b: Berman 7‐11; 10‐19a: Berman 7‐12; 10‐21a: McKinley, O’Loughlin (2nd ed) 10‐16.
Chapter 11
11‐1: McKinley, O’Loughlin 22‐1; 11‐2: McKinley, O’Loughlin (2nd ed) 22‐11; 11‐5: Berman 11‐2; 11‐6: McKinley, O’Loughlin (2nd ed) 23‐1; 11‐8a: Berman 11‐11; 11‐8b: Berman 11‐12; 11‐13: McKinley et al 20‐5; 11‐14a: Berman 11‐20; 11‐14b: Berman 11‐22; 11‐15: McKinley et al 20‐8; 11‐16: Berman 11‐25; 11‐21b: Berman 11‐21; 11‐22b: Berman 11‐18; 11‐22c:
Berman 11‐13; 11‐22d: Berman 11‐19;11‐24b: McKinley, O’Loughlin (2nd ed) 24‐2b.
Chapter 12
12‐1: McKinley, O’Loughlin (2nd ed) 21‐2; 12‐3: McKinley et al 18‐2; 12‐4a: Widmaier 12‐67; 12‐4b,c: McKinley, O’Loughlin (2nd ed) 21‐4; 12‐8: Lichtman II.A.4; 12‐10d: Lichtman II.E.7; 12‐11b: Berman 8‐5; 12‐12c: Berman 8‐6; 12‐12d: Berman 8‐1; 12‐13a: Berman 8‐9; 12‐14: McKinley, O’Loughlin (2nd ed) 21‐10.
Chapter 13
13‐1: Kaushansky et al 4‐1; 13‐5: McKinley et al 18‐4b; 13‐7a: Berman 9‐6 through 9‐9; 13‐7b: Berman 8‐8; 13‐10 top, bottom, insets: Berman 9‐2, 9‐1; 9‐4, 9‐5; 13‐13a: Berman 9‐11; 13‐13b: Berman 9‐13; 13‐14: Berman 9‐14.
Chapter 14
14‐1: McKinley et al 21‐1; 14‐2: McKinley et al 22‐17; 14‐3: McKinley et al 22‐18a; 14‐5: McKinley et al 22‐9; 14‐6: McKinley et al 22‐18; 14‐8a: McKinley et al 21‐5; 14‐8c: McKinley et al 21‐5; 14‐11: McKinley et al 22‐14; 14‐13a: Berman 10‐5; 14‐16: McKinley et al 21‐6.
Chapter 15
15‐1: McKinley, O’Loughlin (2nd ed) 26‐1; 15‐2: McKinley, O’Loughlin (2nd ed) 26‐9; 15‐4: McKinley et al 16‐7; 15‐5a: Berman 12‐10; 15‐5b: Berman 12‐12; 15‐6a: McKinley, O’Loughlin 26‐6c; 15‐6b: McKinley/O’Loughlin (2nd ed) 26‐5; 15‐10a: Berman 12‐1; 15‐10b: Berman 12‐4; 15‐12: McKinley, O’Loughlin 26‐10; 15‐13a: Berman 12‐16; 15‐14a: McKinley et al
26‐9a; 15‐14b: McKinley et al 26‐10; 15‐15: Berman 12‐22; 15‐17d: McKinley et al 26‐10c; 15‐22: McKinley, O’Loughlin (2nd ed) 26‐15; 15‐31: McKinley, O’Loughlin (2nd ed) 26‐26; 15‐32a: McKinley et al 26‐23a; 15‐32b: McKinley et al 26‐23b; 15‐33a: Berman 12‐41; 15‐33b: Berman 12‐43.
Chapter 16
16‐1: McKinley, O’Loughlin (2nd ed) 26‐4a; 16‐3b: Berman 13‐26; 16‐5a: Berman 13‐29; 16‐5b: Berman 13‐32; 16‐7: McKinley, O’Loughlin 26‐20; 16‐8: Berman 13‐17; 16‐9a: Berman 13‐21; 16‐11a,b: McKinley, O’Loughlin 26‐19; 16‐12a: Berman 13‐3; 16‐12b: Berman 13‐4; 16‐13b: Berman 13‐7; 16‐19: McKinley et al 26‐17; 16‐20a: Berman 13‐15.
Chapter 17
17‐1: McKinley, O’Loughlin (2nd ed) 25‐1; 17‐3: McKinley et al 16‐6; 17‐4: Berman 14‐1; 17‐6: McKinley, O’Loughlin (2nd ed) 25‐8; 17‐7: Berman 14‐10; 17‐8a: Berman 14‐11; 17‐8b: Berman 14‐12; 17‐9a: Berman 14‐13; 17‐9c: Berman 14‐14; 17‐11a: McKinley et al 26‐11; 17‐11b,c: McKinley, O’Loughlin (2nd ed) 25‐9; 17‐12: Berman 14‐18; 17‐13a: McKinley et al
23‐12; 17‐13b: McKinley, O’Loughlin (2nd ed) 25‐10; 17‐14: Berman 14‐20; 17‐18a: McKinley, O’Loughlin (2nd ed) 25‐11.
Chapter 18
18‐1: McKinley et al 6‐6; 18‐2: McKinley, O’Loughlin (2nd ed) 5‐2; 18‐3: Berman 15‐4; 18‐5: Berman 15‐3; 18‐6a: Berman 15‐2; 18‐6b: McKinley, O’Loughlin (2nd ed) 5‐4a; 18‐7b: Fitzpatrick 70‐9; 18‐9: Fitzpatrick 7‐6; 18‐10: McKinley, O’Loughlin (2nd ed) 19‐5; 18‐11: McKinley et al 16‐3; 18‐12: Eckel 17‐2; 18‐13a: McKinley et al 6‐9; 18‐13c: McKinley, O’Loughlin
(2nd ed) 5‐9; 18‐14a: Berman 15‐15; 18‐14b: Berman 15‐14; 18‐14c: Berman 15‐13; 18‐15a,b: McKinley, O’Loughlin (2nd ed) 5‐8; 18‐16: McKinley et al 6‐10a; 18‐17a: Berman 15‐10; 18‐19: Fitzpatrick 81‐2; 18‐20: McKinley et al 6‐12.
Chapter 19
19‐1: McKinley et al 24‐3 (right side); 19‐2: McKinley et al 24‐4; 19‐3: McKinley et al 24‐8; 19‐4: Berman 16‐4; 19‐5a: McKinley, O’Loughlin (2nd ed) 27‐6; 19‐5c: McKinley et al 24‐11a; 19‐5d: McKinley, O’Loughlin (2nd ed) 27‐6; 19‐6b: Berman 16‐11; 19‐6c: McKinley et al 24‐11b; 19‐8a: Berman 16‐8; 19‐9a,b,c: McKinley, O’Loughlin (2nd ed) 27‐7; 19‐13:
McKinley et al 24‐9; 19‐16: McKinley, O’Loughlin (2nd ed) 27‐8; 19‐17a: Berman 16‐18.
Chapter 20
20‐1: McKinley et al 17‐3; 20‐2: McKinley, O’Loughlin (2nd ed) 20‐4; 20‐3: McKinley, O’Loughlin (2nd ed) 20‐15; 20‐4: Berman 17‐1; 20‐5a: McKinley, O’Loughlin 20‐8; 20‐5b: McKinley, O’Loughlin 20‐6; 20‐6: Berman 17‐3; 20‐8: McKinley et al 17‐4; 20‐9: Berman 17‐4, McKinley, O’Loughlin (2nd ed) 20‐10; 20‐12: McKinley, O’Loughlin (2nd ed) 20‐13a; 20‐14:
McKinley, O’Loughlin (2nd ed) 20‐13c,d; 20‐17c: Berman 17‐13; 20‐17e: McKinley, O’Loughlin (2nd ed) rt qt; 20‐18: McKinley, O’Loughlin (2nd ed) 20‐9; 20‐19: Berman 17‐15; 20‐21 (upper right): McKinley et al 17‐18; 20‐22: McKinley, O’Loughlin (2nd ed) 20‐11a; 20‐23: Berman 17‐17.
Chapter 21
21‐1: McKinley, O’Loughlin (2nd ed) 28‐11; 21‐2: McKinley, O’Loughlin (2nd ed) 28‐13; 21‐3: Berman 18‐2; 21‐4a: Berman 18‐5; 21‐5: McKinley et al 28‐18; 21‐6a: Berman 18‐7; 21‐6b: Berman 18‐8; 21‐9a: Berman 18‐10; 21‐9b: Berman 18‐11; 21‐10b: Berman 18‐13; 21‐11a: Berman 18‐14; 21‐12a: Berman 18‐16; 21‐13a: McKinley et al 28‐19; 21‐14a: Berman 18‐
18; 21‐16a: Berman 18‐20; 21‐16b: Berman 18‐21; 21‐17: McKinley, O’Loughlin (2nd ed) 18‐17b; 21‐18: Berman 18‐23.
Chapter 22
22‐1a,b: McKinley, O’Loughlin (2nd ed) 28‐11; 22‐2: McKinley, O’Loughlin (2nd ed) 28‐4; 22‐9: McKinley, O’Loughlin (2nd ed) 3‐7; 22‐10: McKinley et al 28‐6; 22‐11: McKinley et al 28‐8; 22‐13: Berman 19‐8; 22‐14: McKinley, O’Loughlin (2nd ed) 28‐7; 22‐15a: Berman 19‐16; 22‐17: McKinley, O’Loughlin (2nd ed) 28‐6; 22‐19a: Berman 19‐19; 22‐19b: Berman 19‐
20; 22‐19c: Berman 19‐21; 22‐20: McKinley, O’Loughlin (2nd ed) 2‐6; 22‐21c: McKinley et al 29‐7 22‐23a: Berman 19‐22; 22‐24a: Berman 19‐23; 22‐26a: Berman 19‐24; 22‐26b: Berman 19‐25; 22‐26c: Berman 19‐26; 22‐27a: Berman 19‐27.
Chapter 23
23‐1: McKinley 19‐12b; 23‐2: McKinley, O’Loughlin (2nd ed) 19‐19; 23‐8: McKinley et al 16‐16; 23‐10a: Berman 20‐4; 23‐14: McKinley, O’Loughlin (2nd ed) 19‐14a,b; 23‐15: Berman 20‐9; 23‐21: McKinley, O’Loughlin (2nd ed) 19‐20; 23‐23: McKinley et al 16‐25; 23‐24: McKinley et al 26‐26; 23‐25: McKinley et al 16‐32; 23‐28: McKinley, O’Loughlin (2nd ed) 19‐25;
23‐29a,b: McKinley et al 16‐27a,b; 23‐29c: McKinley 19‐27; 23‐29d: McKinley et al 16‐27d; 23‐32: McKinley et al 16‐28; 23‐33: McKinley et al 16‐29.
31
Figure Credits
Figure numbers in boldface indicate those appearing for the first time in this text; figure numbers in lightface indicate those taken from other sources.
Berman I. Color Atlas of Basic Histology. 3rd ed. New York, NY: McGraw‐Hill; 2003.
Eckel CM. Human Anatomy Lab Manual. New York, NY: McGraw‐Hill; 2008.
Fitzpatrick TB, et al. Dermatology in General Medicine. New York, NY: McGraw‐Hill; 1971.
Hartwell L, Hood L, Goldberg M., et al. Genetics: From Genes to Genomes. 4th ed. New York, NY: McGraw‐Hill; 2010.
Kaushansky K, Lichtman M, Beutler E, et al. Williams Hematology. 8th ed. New York, NY: McGraw‐Hill; 2010.
Lewis R, Gaffin D, Hoefnagels M, et al. Life. 5th ed. New York, NY: McGraw‐Hill; 2004.
Lichtman MA, Shafer MS, Felgar RE, Wang N: Lichtman’s Atlas of Hematology. New York, NY: 2007. http://www.accessmedicine.com.
McKinley M, O’Loughlin VD. Human Anatomy. 2nd ed. New York, NY: McGraw‐Hill; 2008.
McKinley M, O’Loughlin VD. Human Anatomy. 3rd ed. New York, NY: McGraw‐Hill; 2012.
McKinley MP, O’Loughlin VD, Bidle TS. Anatomy & Physiology: An Integrative Approach. New York, NY: McGraw‐Hill; 2013.
Murray RK, Bender DA, Botham KM, et al. Harper’s Illustrated Biochemistry. 28th ed. New York, NY: McGraw‐Hill; 2009.
Raven P, Johnson GB, Losos JB, et al. Biology. 7th ed. New York, NY: McGraw‐Hill; 2005.
Weiss L, Greep RO. Histology. 4th ed. New York, NY: McGraw‐Hill; 1977.
Widmaier EP, Raff H, Strang KT. Vander’s Human Physiology. 11th ed. New York, NY: McGraw‐Hill; 2008.
Chapter 1
1‐14: McKinley et al 1‐5.
Chapter 2
2‐3: McKinley et al 4‐5a; 2‐6: McKinley, O’Loughlin (2nd ed) 2‐7; 2‐8: McKinley et al 4‐19; 2‐10a: McKinley, O’Loughlin 2‐8; 2‐10b: McKinley, O’Loughlin 2‐8; 2‐13a (left side): McKinley, O’Loughlin 2‐9; 2‐16b: McKinley, O’Loughlin 2‐10; 2‐16c: McKinley, O’Loughlin 2‐10; 2‐20 (top part): McKinley, O’Loughlin (2nd ed) 2‐12; 2‐21b: McKinley, O’Loughlin 2‐11; 2‐24:
McKinley, O’Loughlin (2nd ed) 2‐35.
Chapter 3
3‐2: McKinley, O’Loughlin 2‐17; 3‐10: Hartwell et al 17‐22b; 3‐12 (right): McKinley, O’Loughlin 2‐19; 3‐18: Lewis et al 9‐10.
Chapter 4
4‐4: Raven 7‐13; 4‐5: Weiss 3‐12; 4‐20: McKinley, O’Loughlin (2nd ed) 4‐4; 4‐15d: Berman 1‐16; 4‐21a: McKinley, O’Loughlin 4‐6; 4‐21b: McKinley, O’Loughlin 4‐6; 4‐21c: McKinley, O’Loughlin 4‐6c; 4‐27: McKinley et al 4‐14.
Chapter 5
5‐2: McKinley et al 16‐3; 5‐3a: Berman 2‐6; 5‐8a: Berman 2‐7; 5‐12b: Berman 2‐24; 5‐17b: Murray et al 48‐6.
Chapter 6
6‐1c: Berman 2‐20; 6‐1d: Berman 2‐19.
Chapter 7
7‐1: McKinley, O’Loughlin (2nd ed) 6‐1; 7‐5a: Berman 3‐4.
Chapter 8
8‐1: McKinley et al 7‐7; 8‐9: Berman 4‐4; 8‐13a: Berman 5‐7; 8‐14: McKinley, O’Loughlin (2nd ed) 6‐11; 8‐16: McKinley, O’Loughlin (2nd ed) 6‐12a,b; 8‐17a: Berman 5‐3; 8‐17b: Berman 5‐4; 8‐18: McKinley, O’Loughlin (2nd ed) 6‐16; 8‐19a: McKinley, O’Loughlin (2nd ed) 9‐4.
Chapter 9
9‐1: McKinley, O’Loughlin (2nd ed) 14‐1; 9‐2: McKinley, O’Loughlin (2nd ed) 14‐16; 9‐3: McKinley et al 12‐2; 9‐4: McKinley et al 12‐1 (table); 9‐5: Berman 6‐8; 9‐6a: McKinley, O’Loughlin (2nd ed) 14‐14b; 9‐7: McKinley, O’Loughlin (2nd ed) 14‐13c; 9‐8b: Eckel 4‐28b; 9‐9: McKinley, O’Loughlin (2nd ed) 14‐7; 9‐10a: Berman 9‐11a; 9‐17: Eckel 16‐1c; 9‐18a:
McKinley, O’Loughlin (2nd ed) 16‐2b; 9‐19: McKinley, O’Loughlin 15‐4; 9‐20c: McKinley, O’Loughlin (2nd ed) 15‐7a; 9‐21a: McKinley, O’Loughlin (2nd ed) 14‐8(1); 9‐21b: McKinley, O’Loughlin (2nd ed) 14‐8(2); 9‐21c: McKinley, O’Loughlin (2nd ed) 14‐8(3); 9‐21d: McKinley, O’Loughlin (2nd ed) 14‐8(4); 9‐22: Berman 6‐21; 9‐25: McKinley, O’Loughlin (2nd ed) 14‐
10a; 9‐26a: McKinley, O’Loughlin (2nd ed) 14‐12a; 9‐26b: Berman 6‐15; 9‐26d: McKinley, O’Loughlin (2nd ed) 14‐12b; 9‐28b: Berman 6‐19; 9‐28d: Berman 6‐18; 9‐29a: Berman 6‐10; 9‐29c: Berman 6‐12.
Chapter 10
10‐1: Widmaier 9‐1; 10‐2: McKinley, O’Loughlin (2nd ed) 10‐4; 10‐3: McKinley et al 10‐1; 10‐7a: Berman 7‐2; 10‐7c: Berman 7‐4; 10‐8: McKinley, O’Loughlin (2nd ed) 10‐6; 10‐9: McKinley et al 10‐4; McKinley, O’Loughlin 10‐9; 10‐12: McKinley et al 10‐12; 10‐13: Widmaier 9‐14; 10‐14a: Widmaier 10‐4; Berman 7‐6; 10‐14b: Berman 7‐7; 10‐15: McKinley, O’Loughlin
(2nd ed) 10‐12; 10‐16: McKinley, O’Loughlin (2nd ed) 22‐10a; 10‐17a: Berman 7‐10; 10‐17b: Berman 7‐11; 10‐19a: Berman 7‐12; 10‐21a: McKinley, O’Loughlin (2nd ed) 10‐16.
Chapter 11
11‐1: McKinley, O’Loughlin 22‐1; 11‐2: McKinley, O’Loughlin (2nd ed) 22‐11; 11‐5: Berman 11‐2; 11‐6: McKinley, O’Loughlin (2nd ed) 23‐1; 11‐8a: Berman 11‐11; 11‐8b: Berman 11‐12; 11‐13: McKinley et al 20‐5; 11‐14a: Berman 11‐20; 11‐14b: Berman 11‐22; 11‐15: McKinley et al 20‐8; 11‐16: Berman 11‐25; 11‐21b: Berman 11‐21; 11‐22b: Berman 11‐18; 11‐22c:
Berman 11‐13; 11‐22d: Berman 11‐19;11‐24b: McKinley, O’Loughlin (2nd ed) 24‐2b.
Chapter 12
12‐1: McKinley, O’Loughlin (2nd ed) 21‐2; 12‐3: McKinley et al 18‐2; 12‐4a: Widmaier 12‐67; 12‐4b,c: McKinley, O’Loughlin (2nd ed) 21‐4; 12‐8: Lichtman II.A.4; 12‐10d: Lichtman II.E.7; 12‐11b: Berman 8‐5; 12‐12c: Berman 8‐6; 12‐12d: Berman 8‐1; 12‐13a: Berman 8‐9; 12‐14: McKinley, O’Loughlin (2nd ed) 21‐10.
Chapter 13
13‐1: Kaushansky et al 4‐1; 13‐5: McKinley et al 18‐4b; 13‐7a: Berman 9‐6 through 9‐9; 13‐7b: Berman 8‐8; 13‐10 top, bottom, insets: Berman 9‐2, 9‐1; 9‐4, 9‐5; 13‐13a: Berman 9‐11; 13‐13b: Berman 9‐13; 13‐14: Berman 9‐14.
Chapter 14
14‐1: McKinley et al 21‐1; 14‐2: McKinley et al 22‐17; 14‐3: McKinley et al 22‐18a; 14‐5: McKinley et al 22‐9; 14‐6: McKinley et al 22‐18; 14‐8a: McKinley et al 21‐5; 14‐8c: McKinley et al 21‐5; 14‐11: McKinley et al 22‐14; 14‐13a: Berman 10‐5; 14‐16: McKinley et al 21‐6.
Chapter 15
15‐1: McKinley, O’Loughlin (2nd ed) 26‐1; 15‐2: McKinley, O’Loughlin (2nd ed) 26‐9; 15‐4: McKinley et al 16‐7; 15‐5a: Berman 12‐10; 15‐5b: Berman 12‐12; 15‐6a: McKinley, O’Loughlin 26‐6c; 15‐6b: McKinley/O’Loughlin (2nd ed) 26‐5; 15‐10a: Berman 12‐1; 15‐10b: Berman 12‐4; 15‐12: McKinley, O’Loughlin 26‐10; 15‐13a: Berman 12‐16; 15‐14a: McKinley et al
26‐9a; 15‐14b: McKinley et al 26‐10; 15‐15: Berman 12‐22; 15‐17d: McKinley et al 26‐10c; 15‐22: McKinley, O’Loughlin (2nd ed) 26‐15; 15‐31: McKinley, O’Loughlin (2nd ed) 26‐26; 15‐32a: McKinley et al 26‐23a; 15‐32b: McKinley et al 26‐23b; 15‐33a: Berman 12‐41; 15‐33b: Berman 12‐43.
Chapter 16
16‐1: McKinley, O’Loughlin (2nd ed) 26‐4a; 16‐3b: Berman 13‐26; 16‐5a: Berman 13‐29; 16‐5b: Berman 13‐32; 16‐7: McKinley, O’Loughlin 26‐20; 16‐8: Berman 13‐17; 16‐9a: Berman 13‐21; 16‐11a,b: McKinley, O’Loughlin 26‐19; 16‐12a: Berman 13‐3; 16‐12b: Berman 13‐4; 16‐13b: Berman 13‐7; 16‐19: McKinley et al 26‐17; 16‐20a: Berman 13‐15.
Chapter 17
17‐1: McKinley, O’Loughlin (2nd ed) 25‐1; 17‐3: McKinley et al 16‐6; 17‐4: Berman 14‐1; 17‐6: McKinley, O’Loughlin (2nd ed) 25‐8; 17‐7: Berman 14‐10; 17‐8a: Berman 14‐11; 17‐8b: Berman 14‐12; 17‐9a: Berman 14‐13; 17‐9c: Berman 14‐14; 17‐11a: McKinley et al 26‐11; 17‐11b,c: McKinley, O’Loughlin (2nd ed) 25‐9; 17‐12: Berman 14‐18; 17‐13a: McKinley et al
23‐12; 17‐13b: McKinley, O’Loughlin (2nd ed) 25‐10; 17‐14: Berman 14‐20; 17‐18a: McKinley, O’Loughlin (2nd ed) 25‐11.
Chapter 18
18‐1: McKinley et al 6‐6; 18‐2: McKinley, O’Loughlin (2nd ed) 5‐2; 18‐3: Berman 15‐4; 18‐5: Berman 15‐3; 18‐6a: Berman 15‐2; 18‐6b: McKinley, O’Loughlin (2nd ed) 5‐4a; 18‐7b: Fitzpatrick 70‐9; 18‐9: Fitzpatrick 7‐6; 18‐10: McKinley, O’Loughlin (2nd ed) 19‐5; 18‐11: McKinley et al 16‐3; 18‐12: Eckel 17‐2; 18‐13a: McKinley et al 6‐9; 18‐13c: McKinley, O’Loughlin
(2nd ed) 5‐9; 18‐14a: Berman 15‐15; 18‐14b: Berman 15‐14; 18‐14c: Berman 15‐13; 18‐15a,b: McKinley, O’Loughlin (2nd ed) 5‐8; 18‐16: McKinley et al 6‐10a; 18‐17a: Berman 15‐10; 18‐19: Fitzpatrick 81‐2; 18‐20: McKinley et al 6‐12.
Chapter 19
19‐1: McKinley et al 24‐3 (right side); 19‐2: McKinley et al 24‐4; 19‐3: McKinley et al 24‐8; 19‐4: Berman 16‐4; 19‐5a: McKinley, O’Loughlin (2nd ed) 27‐6; 19‐5c: McKinley et al 24‐11a; 19‐5d: McKinley, O’Loughlin (2nd ed) 27‐6; 19‐6b: Berman 16‐11; 19‐6c: McKinley et al 24‐11b; 19‐8a: Berman 16‐8; 19‐9a,b,c: McKinley, O’Loughlin (2nd ed) 27‐7; 19‐13:
McKinley et al 24‐9; 19‐16: McKinley, O’Loughlin (2nd ed) 27‐8; 19‐17a: Berman 16‐18.
Chapter 20
20‐1: McKinley et al 17‐3; 20‐2: McKinley, O’Loughlin (2nd ed) 20‐4; 20‐3: McKinley, O’Loughlin (2nd ed) 20‐15; 20‐4: Berman 17‐1; 20‐5a: McKinley, O’Loughlin 20‐8; 20‐5b: McKinley, O’Loughlin 20‐6; 20‐6: Berman 17‐3; 20‐8: McKinley et al 17‐4; 20‐9: Berman 17‐4, McKinley, O’Loughlin (2nd ed) 20‐10; 20‐12: McKinley, O’Loughlin (2nd ed) 20‐13a; 20‐14:
McKinley, O’Loughlin (2nd ed) 20‐13c,d; 20‐17c: Berman 17‐13; 20‐17e: McKinley, O’Loughlin (2nd ed) rt qt; 20‐18: McKinley, O’Loughlin (2nd ed) 20‐9; 20‐19: Berman 17‐15; 20‐21 (upper right): McKinley et al 17‐18; 20‐22: McKinley, O’Loughlin (2nd ed) 20‐11a; 20‐23: Berman 17‐17.
Chapter 21
21‐1: McKinley, O’Loughlin (2nd ed) 28‐11; 21‐2: McKinley, O’Loughlin (2nd ed) 28‐13; 21‐3: Berman 18‐2; 21‐4a: Berman 18‐5; 21‐5: McKinley et al 28‐18; 21‐6a: Berman 18‐7; 21‐6b: Berman 18‐8; 21‐9a: Berman 18‐10; 21‐9b: Berman 18‐11; 21‐10b: Berman 18‐13; 21‐11a: Berman 18‐14; 21‐12a: Berman 18‐16; 21‐13a: McKinley et al 28‐19; 21‐14a: Berman 18‐
18; 21‐16a: Berman 18‐20; 21‐16b: Berman 18‐21; 21‐17: McKinley, O’Loughlin (2nd ed) 18‐17b; 21‐18: Berman 18‐23.
Chapter 22
22‐1a,b: McKinley, O’Loughlin (2nd ed) 28‐11; 22‐2: McKinley, O’Loughlin (2nd ed) 28‐4; 22‐9: McKinley, O’Loughlin (2nd ed) 3‐7; 22‐10: McKinley et al 28‐6; 22‐11: McKinley et al 28‐8; 22‐13: Berman 19‐8; 22‐14: McKinley, O’Loughlin (2nd ed) 28‐7; 22‐15a: Berman 19‐16; 22‐17: McKinley, O’Loughlin (2nd ed) 28‐6; 22‐19a: Berman 19‐19; 22‐19b: Berman 19‐
20; 22‐19c: Berman 19‐21; 22‐20: McKinley, O’Loughlin (2nd ed) 2‐6; 22‐21c: McKinley et al 29‐7 22‐23a: Berman 19‐22; 22‐24a: Berman 19‐23; 22‐26a: Berman 19‐24; 22‐26b: Berman 19‐25; 22‐26c: Berman 19‐26; 22‐27a: Berman 19‐27.
Chapter 23
23‐1: McKinley 19‐12b; 23‐2: McKinley, O’Loughlin (2nd ed) 19‐19; 23‐8: McKinley et al 16‐16; 23‐10a: Berman 20‐4; 23‐14: McKinley, O’Loughlin (2nd ed) 19‐14a,b; 23‐15: Berman 20‐9; 23‐21: McKinley, O’Loughlin (2nd ed) 19‐20; 23‐23: McKinley et al 16‐25; 23‐24: McKinley et al 26‐26; 23‐25: McKinley et al 16‐32; 23‐28: McKinley, O’Loughlin (2nd ed) 19‐25;
23‐29a,b: McKinley et al 16‐27a,b; 23‐29c: McKinley 19‐27; 23‐29d: McKinley et al 16‐27d; 23‐32: McKinley et al 16‐28; 23‐33: McKinley et al 16‐29.
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