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General Principles
Third Edition
SENIOR EDITORS EDITORS

TAO LE, MD, MHS LUKE R.G. PIKE, MD, DPhil
Associate Clinical Professor Resident, Harvard Radiation Oncology Program
Chief, Section of Allergy and Immunology Massachusetts General Hospital
Department of Medicine Brigham & Women’s Hospital
University of Louisville
M. SCOTT MOORE, DO
WILLIAM L. HWANG, MD, PhD Clinical Research Fellow
Resident, Harvard Radiation Oncology Program Affiliated Laboratories, Scottsdale
Massachusetts General Hospital
Brigham & Women’s Hospital
New York / Chicago / San Francisco / Athens / London / Madrid / Mexico City
Milan / New Delhi / Singapore / Sydney / Toronto
0 GP_3e_FM_i-xiv.indd 1 10/28/16 3:14 PM

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DEDICATION
To the contributors to this and future editions, who took time to share their knowledge,
insight, and humor for the benefit of students and physicians everywhere.
and
To our families, friends, and loved ones, who supported us

in the task of assembling this guide.

This page intentionally left blank

v
Contents
Contributing Authors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . vi CHAPTER 4. Microbiology . . . . . . . . . . . . . . . . . . . 229
Faculty Reviewers . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . vii Bacteriology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 230
Preface . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . ix Mycology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 286
How to Use This Book . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . x Parasitology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 298
Acknowledgments . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . xi Virology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 311
How to Contribute . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . xiii Microbiology: Systems . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 355
Antimicrobials . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 371
CHAPTER 1. Anatomy and Histology . . . . . . . . . . . 1
Cellular Anatomy and Histology . . . . . . . . . . . . . . . . . . . . . . 2 CHAPTER 5. Pathology . . . . . . . . . . . . . . . . . . . . . . 395
Gross Anatomy and Histology . . . . . . . . . . . . . . . . . . . . . . . 15
CHAPTER 6. General Pharmacology . . . . . . . . . .417
CHAPTER 2. Biochemistry . . . . . . . . . . . . . . . . . . . . 33
Pharmacokinetics and Pharmacodynamics . . . . . . . . . 418
Molecular Biology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 34 Toxicology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 427
Nucleotide Synthesis . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 35
Mutations and DNA Repair . . . . . . . . . . . . . . . . . . . . . . . . . . . 50 CHAPTER 7. Public Health Sciences . . . . . . . . . . 435
Enzymes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 64 Epidemiology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 436
The Cell . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 71 Statistics . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 445
Connective Tissue . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 75 Public Health . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 449
Homeostasis and Metabolism . . . . . . . . . . . . . . . . . . . . . . . . 83 Patient Safety and Quality Improvement . . . . . . . . . . . 453
Amino Acids . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 98 Ethics . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 456
Nutrition . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 118 Life Cycle . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 461
Fed Versus Unfed State . . . . . . . . . . . . . . . . . . . . . . . . . . . . 128 Psychology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 465
Laboratory Tests and Techniques . . . . . . . . . . . . . . . . . . 169
Genetics . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 179 Image Acknowledgments . . . . . . . . . . . . . . . . . . . . . . . . . 469
Index . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 477
CHAPTER 3. Immunology . . . . . . . . . . . . . . . . . . . 187
About the Editors . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 512
Principles of Immunology . . . . . . . . . . . . . . . . . . . . . . . . . 188
Pathology . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 207

vi
CONTRIBUTING AUTHORS
Ezra Baraban, MD Margaret MacGibeny, MS
Yale School of Medicine Rutgers Robert Wood Johnson Medical School and
Class of 2016 Princeton University MD/PhD program
Nashid H. Chaudhury Class of 2020
Medical Scientist Training Program
Benjamin B. Massenburg
Yale School of Medicine
Icahn School of Medicine at Mount Sinai
Class of 2020
Class of 2017
Richard Giovane, MD
Resident, Department of Family Medicine Jake Prigoff, M
University of Alabama Resident, Department of Surgery
Jessica F. Johnston, MSc New York Presbyterian Hospital
Medical Scientist Training Program
Ritchell van Dams, MD, MHS
Intern, Department of Medicine
Class of 2020
Norwalk Hospital
Young H. Lim
Medical Scientist Training Program Zachary Schwam, MD
Yale School of Medicine Yale School of Medicine
Class of 2020 Class of 2016

vii
FACULTY REVIEWERS
Susan Baserga, MD, PhD Gerald Lee, MD
Professor, Molecular Biophysics & Biochemistry Genetics and Assistant Professor, Department of Pediatrics
Therapeutic Radiology University of Louisville School of Medicine
Alexandros D. Polydorides, MD, PhD
Sheldon Campbell, MD, PhD Associate Professor of Pathology and Medicine (Gastroenterology)
Associate Professor of Laboratory Medicine Icahn School of Medicine at Mount Sinai
Co-director, Attacks and Defenses Master Course
Sylvia Wassertheil-Smoller, PhD
Director, Laboratories at VA CT Healthcare System
Distinguished University Professor and
Director, Microbiology Fellowship
Molly Rosen and Maneoloff Chair in Social Medicine, Emerita
Department of Epidemiology and Population Health
Conrad Fischer, MD Albert Einstein College of Medicine
Residency Program Director, Brookdale University Hospital
Brooklyn, New York Howard M. Steinman, PhD
Associate Professor, Medicine, Physiology, and Pharmacology Professor, Department of Biochemistry
Touro College of Medicine Assistant Dean for Biomedical Science Education
Albert Einstein College of Medicine
Matthew Grant, MD
Assistant Professor of Medicine (Infectious Disease) Peter Takizawa, PhD
Director, Yale Health Travel Medicine Assistant Professor, Department of Cell Biology
Yale School of Medicine Director, Medical Studies
Marcel Green, MD
Resident Physician, Department of Psychiatry George J. Trachte, PhD
Mount Sinai Health System, St. Luke’s–Roosevelt Hospital Professor, Department of Biomedical Sciences
University of Minnesota
Peter Heeger, MD
Irene and Arthur Fishberg Professor of Medicine Prashant Vaishnava, MD
Translational Transplant Research Center Assistant Professor, Department of Medicine
Department of Medicine Mount Sinai Hospital and Icahn School of Medicine at Mount
Icahn School of Medicine at Mount Sinai Sinai
Jeffrey W. Hofmann, MD, Ph Ana A. Weil, MD
Resident, Department of Pathology Instructor in Medicine
University of California, San Francisco Massachusetts General Hospital


ix
Preface
With this third edition of First Aid for the Basic Sciences: General Principles, we con-
tinue our commitment to providing students with the most useful and up-to-date
preparation guides for the USMLE Step 1. For the past year, a team of authors and
editors have worked to update and further improve this third edition. This edition
represents a major revision in many ways.
■ Brand new Public Health and Patient Safety sections have been added.
■ Every page has been carefully reviewed and updated to reflect the most high-yield
material for the Step 1 exam.
■ New high-yield figures, tables, and mnemonics have been incorporated.
■ Margin elements, including flash cards, have been added to assist in optimizing the
studying process.
■ Hundreds of user comments and suggestions have been incorporated
■ Emphasis on integration and linkage of concepts was increased.
This book would not have been possible without the help of the hundreds of students
and faculty members who contributed their feedback and suggestions. We invite stu-
dents and faculty to please share their thoughts and ideas to help us improve First Aid
for the Basic Sciences: General Principles. (See How to Contribute, p. xiii.)
Louisville Tao Le
Boston William Hwang

x
How to Use This Book

Both this text and its companion, First Aid for the Basic Sciences: Organ Systems, are
designed to fill the need for a high-quality, in-depth, conceptually driven study guide
for the USMLE Step 1. They can be used alone or in conjunction with the original
First Aid for the USMLE Step 1. In this way, students can tailor their own studying
experience, calling on either series, according to their mastery of each subject.
Medical students who have used the previous editions of this guide have given us
feedback on how best to make use of the book.
■ It is recommended that you begin using this book as early as possible when learn-
ing the basic medical sciences. We advise that you use this book as a companion to
your preclinical medical school courses to provide a guide for the concepts that are
most important for the USMLE Step 1.
■ As you study each discipline, use the corresponding section in First Aid for the
Basic Sciences: General Principles to consolidate the material, deepen your under-
standing, or clarify concepts.
■ As you approach the test, use both First Aid for the Basic Sciences: General Principles
and First Aid for the Basic Sciences: Organ Systems to review challenging concepts.
■ Use the margin elements (ie, Flash Forward, Flash Back, Key Fact, Clinical Cor-
relation, Mnemonic, Flash Cards) to test yourself throughout your studies.
To broaden your learning strategy, you can integrate your First Aid for the Basic Sci-
ences: General Principles study with First Aid for the USMLE Step 1, First Aid Cases
for the USMLE Step 1, and First Aid Q&A for the USMLE Step 1 on a chapter-by-
chapter basis.

xi
Acknowledgments
This has been a collaborative project from the start. We gratefully acknowledge the
thoughtful comments and advice of the residents, international medical graduates,
medical students, and faculty who have supported the editors and authors in the de-
velopment of First Aid for the Basic Sciences: General Principles.
For support and encouragement throughout the process, we are grateful to Thao
Pham and Louise Petersen.
Furthermore, we wish to give credit to our amazing editors and authors, who worked
tirelessly on the manuscript. We never cease to be amazed by their dedication,
thoughtfulness, and creativity.
Thanks to our publisher, McGraw-Hill Education, for their assistance and guidance.
For outstanding editorial work, we thank Allison Battista, Christine Diedrich, Ruth
Kaufman, Isabel Nogueira, Emma Underdown, Catherine Johnson, and Hannah
Warnshuis. A special thanks to Rainbow Graphics, especially David Hommel, for
remarkable production work.
We are also very grateful to the faculty at Uniformed Services University of the
Health Sciences (USUHS) for use of their images and Dr. Richard Usatine for his
outstanding dermatologic and clinical image contributions.
For contributions and corrections, we thank Abraham Abdul-Hak, Mohamed Abdulla,
Zachary Aberman, Andranik Agazaryan, Zain Ahmed, Anas Alabkaa, Allen Avedian,
Syed Ayaz, Andrew Beck, Michael Bellew, Konstantinos Belogiannis, Candace
Benoit, Brandon Bodie, Aaron Bush, Robert Case, Jr., Anup Chalise, Rajdeep
Chana, Sheng-chieh Chang, Yu Chiu, Renee Cholyway, Alice Chuang, Diana
Dean, Douglas Dembinski, Kathryn Demitruk, Regina DePietro, Nolan Derr,
Vikram Eddy, Alejandra Ellison-Barnes, Leonel Estofan, Tim Evans, Matt Fishman,
Emerson Franke, Margaret Funk, Alejandro Garcia, William Gentry, Richard
Godby, Shawn Gogia, Marisol Gonzalez, William Graves, Jessie Hanna, Clare
Herickhoff, Joyce Ho, Jeff Hodges, David Huang, Andrew Iskandar, Anicia Ivey,
Jeffrey James, Angela Jiang, Bradford Jones, Caroline Jones, Charissa Kahue, Sophie
Kerszberg, Michael Kertzner, Mani Khorsand Askari, Peeraphol La-orkanchanakun,
Juhye Lee, Jessica Liu, Jinyu Lu, James McClurg, Gregory McWhir, Rahul Mehta,
Kristen Mengwasser, Aleksandra Miucin, Morgan Moon, Jan Neander, Michael
Nguyen, Jay Patel, Nehal Patel, Iqra Patoli, Matthew Peters, Yelyzaveta Plechysta,
Qiong Qui, Peter Francis Raguindin, Kenny Rivera, Luis Rivera, Benjamin Robbins,
Jorge Roman, Julietta Rubin, Kaivan Salehpour, Abdullah Sarkar, Hoda Shabpiray,
Neal Shah, Chris Shoff, Rachael Snow, Gregory Steinberg, Ryan Town, Michael
Turgeon, Hunter Upton, Zack Vanderlaan, Christopher Vetter, Liliana Villamil
Nunez, Sukanthi Viruthagiri, David Marcus Wang, and Andy Zureick.
Louisville Tao Le
Boston William Hwang


xiii
How to Contribute
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CHAPTER 1
Anatomy and Histology
CELLULAR ANATOMY AND HISTOLOGY 2 Splenic Anatomy 20

The Cell 2 The Lymphatic System 20
Hematopoiesis 8 Peripheral Nervous System 23
The Integumentary System 25
GROSS ANATOMY AND HISTOLOGY 15 The Respiratory System 29
Abdominal Wall Anatomy 15 The Adrenal Glands 31
The Gastrointestinal System 17
1 GP_3e_CH_01_Anat-Histol_1-32.indd 1 10/26/16 2:58 PM

2 CHAPTER 1 ANATOMY AND HISTOLOGY
Cellular Anatomy and Histology
THE CELL
The cell is the most basic structural and functional unit of life. Living organisms are com-
posed of cells, which may exist as independent units or form more complex organisms.
Each cell is a collection of integral, diverse components, required for the biochemical
processes that sustain the life of the organism. The most important eukaryotic cellular
components will be covered in the following sections.
Plasma Membrane
Every eukaryotic cell is enveloped by an asymmetric lipid bilayer membrane. This
membrane consists primarily of two sheets of phospholipids, each one-molecule thick
(Figure 1-1B). Phospholipids are amphipathic molecules, containing both a water-
soluble hydrophilic region and a fat-soluble hydrophobic region (Figure 1-1).
Aqueous phase (extracellular)
Polar or
hydrophilic groups
“Oil” or nonpolar phase
Nonpolar or
hydrophobic groups
Aqueous phase (cytoplasm)

A
A. Phospholipid B
B. Lipid bilayer/
cell membrane
Aqueous phase
Aqueous phase
Nonpolar
phase
polar phase
Non
Aqueous
phase
Lipid
bilayer
C
C. Micelle D
D. Liposome (unilamellar)
Aqueous Lipid
compartments bilayers
EE. Liposome (multilamellar)
F I G U R E 1 - 1 . Amphipathic lipids. A Phospholipid, with a phosphate head group and a lipid

tail; B lipid bilayer with both aqueous and nonpolar phases; C micelle in aqueous solution
surrounding a nonpolar core; D unilamellar; and E multilamellar liposomes.

ANATOMY AND HISTOLOGY CHAPTER 1 3
■ The hydrophilic portions (ie, phosphate groups) of each phospholipid layer face
both the aqueous extracellular environment as well as the aqueous cytoplasm.
■ The hydrophobic portions of each phospholipid layer (ie, fatty acid chains) make
up the fat-soluble center of the phospholipid membrane.
This bilayer membrane also contains steroid molecules (derived from cholesterol), KEY FACT
glycolipids (fatty acids with sugar moieties), sphingolipids, proteins, and glycoproteins
Biologically important proteins include
(proteins with sugar moieties). The cholesterol and glycolipid molecules alter the physi- transmembrane transporters, ligand-
cal properties of the membrane (eg, increase the melting point) in relative proportion receptor complexes, and ion channels.
to their quantity. The proteins serve important and specific roles in the transport and Protein dysfunction underlies many
trafficking of nutrients across the membrane, signal transduction, and interactions diseases.
between the cell and its environment.
The cell membrane performs the following functions:

■ Enhances cellular structural stability.
■ Protects internal organelles from the external environment.
■ Regulates the internal environment (chemical and electrical potential).
■ Enables interactions with the external environment (eg, signal transduction and
cellular adhesion).
FLASH
Nucleus and Nucleolus FORWARD
The nucleus is the control center of the cell. The nucleus contains genetically encoded Genetic mutations may cause
information in the form of DNA, which directs the life processes of the cell. It is sur- dysfunction of regulatory proteins,
often leading to debilitating diseases.
rounded by the nuclear membrane, which is composed of two lipid bilayers: The inner
For example, xeroderma pigmentosum
membrane defines the boundaries of the nucleus, and the outer membrane is continuous is an autosomal recessive disorder of
with the rough endoplasmic reticulum (RER) (Figure 1-2). In addition to DNA, the nucleotide excision repair that leads
nucleus houses a number of important proteins that enable the maintenance (protec- to increased sensitivity to UV light and
tion, repair, and replication), expression (transcription), and transportation of genetic increased rates of skin cancer.
material (capping, transport).
Most of the cell’s ribosomal RNA (rRNA) is produced within the nucleus by the nucleo-
lus. The rRNA then passes through the nuclear pores (transmembrane protein com-
plexes that regulate trafficking across the nuclear membrane) to the cytosol, where it
associates with the RER.
Rough Endoplasmic Reticulum and Ribosomes

As previously described, the RER is home to the majority of the cell’s ribosomes. The
rough in rough endoplasmic reticulum comes from the many ribosomes that stud the
KEY FACT
membrane of the RER. Ribosomes associate with transfer RNA (tRNA) to translate mes-
senger RNA (mRNA) into amino acid sequences and, eventually, into proteins (Figure The RER in neurons is referred to as
1-3). The RER functions primarily as the location for membrane and secretory protein Nissl body when viewed under a
production as well as protein modification (Figure 1-2). The RER is highly developed in microscope.
cell types that produce secretory proteins (eg, pancreatic acinar cells or plasma cells).
Smooth Endoplasmic Reticulum

FLASH
The smooth endoplasmic reticulum (SER) is the site of fatty acid and phospholipid FORWARD
production and therefore is highly developed in cells of the adrenal cortex and steroid-
The cytochrome P-450 system is a
secreting cells of the ovaries and testes. Hepatocytes also have a highly developed SER,
family of enzymes located in the SER or
as they are constantly detoxifying hydrophobic compounds through conjugation and mitochondria that metabolize millions
excretion. of endogenous and exogenous
compounds.
Golgi Apparatus
Shortly after being synthesized, proteins from the RER are packaged into transport
vesicles and secreted from the RER. These vesicles travel to and fuse with the Golgi
apparatus. Within the lumen of the Golgi apparatus, secretory and membrane-bound

Key:
brane
mem
Clathrin sma
Pla
Secretory
vesicle
COPI Late Early
endosome endosome
CLINICAL COPII
Lysosome
CORRELATION
Retrograde trans
Inclusion-cell (I-cell) disease, also
known as mucolipidosis type II, results Anterograde
from a defect in N-acetylglucosaminyl- Golgi
1-phosphotransferase, leading to apparatus
a failure of the Golgi apparatus to
phosphorylate mannose residues (ie,
mannose-6-phosphate) on N-linked cis
glycoproteins. Thus, hydrolytic
enzymes are secreted extracellularly,
rather than delivered to lysosomes, Endoplasmic
hindering the digestion of intracellular reticulum
waste. Coarse facial features and
restricted joint movements result (refer Nuclear envelope
to Biochemistry chapter for discussion
of lysosomal storage disorders).
F I G U R E 1 - 2 . Representation of the rough endoplasmic reticular branch of protein
sorting. Newly synthesized proteins are inserted into the endoplasmic reticulum membrane, or
CLINICAL enter the lumen from membrane-bound polyribosomes, depicted as light blue spheres studding
CORRELATION the endoplasmic reticulum. Those proteins are then transported out of the endoplasmic
reticulum to the Golgi apparatus. Transport to the Golgi apparatus (anterograde transport)
A number of lysosomal storage
is mediated by COPII membrane proteins. Transport from the Golgi apparatus back to the
diseases, such as Tay-Sachs disease,
endoplasmic reticulum (retrograde transport) is mediated by COPI membrane proteins.
result from lysosomal dysfunction
The proteins can be modified in the various subcompartments of the Golgi apparatus and
and the accumulation of protein are then segregated and sorted in the trans-Golgi network. Secretory proteins accumulate in
metabolites targeted for destruction or secretory storage granules, from which they may be expelled. Proteins destined for the plasma
further modification. membrane, or those that are secreted in a constitutive manner, are carried out to the cell
surface in transport vesicles. This transport is mediated by clathrin membrane proteins. Some
proteins enter prelysosomes (late endosomes) and fuse with endosomes to form lysosomes.
60S
Ribosome
proteins undergo modification. Depending on their final destination, these proteins may
be modified in one of the three major regions of Golgi networks: cis (CGN), medial
E P A (MGN), or trans (TGN). These proteins are then packaged in a second set of transport
5' 3' vesicles, which bud from the trans side and are delivered to their target locations (eg,
organelle membranes, plasma membrane, and lysosomes; Figure 1-2).
40S
Functions of the Golgi Apparatus

F I G U R E 1 - 3 . Schematic
representation of translation. Here, ■ Distributes proteins and lipids from the endoplasmic reticulum to the plasma mem-
the 40S and 60S subunits of rRNA brane, lysosomes, and secretory vesicles.
are shown, translating a portion of ■ Modifies N-oligosaccharides on asparagines.
mRNA in the 5′ to 3′ direction. Many ■ Adds O-oligosaccharides to serine and threonine residues.
of these ribosomes are located within ■ Assembles proteoglycans from core proteins.
the membrane of the RER so that
their initial protein product ends up
■ Adds sulfate to sugars in proteoglycans and tyrosine residues on proteins.
within the lumen of the RER, where ■ Adds mannose-6-phosphate to specific proteins (targets the proteins to the lysosome).
it undergoes further modification.
E site, holds Empty tRNA as it Lysosomes
Exits; P site, accommodates growing
Peptide; A site, Arriving Aminoacyl The lysosome is the trash collector of the cell. Bound by a single lipid bilayer, the lyso-
tRNA. some is responsible for hydrolytic degradation of obsolete cellular components. Extra-

cellular materials, ingested via endocytosis or phagocytosis, are enveloped in an endo- CLINICAL
some (temporary vesicle), which fuses with the lysosome, leading to enzymatic CORRELATION
degradation of endosomal contents. Lysosomal enzymes (nucleases, proteases, and
Chédiak-Higashi disease, resulting
phosphatases) are activated at a pH below 4.8. To maintain this pH, the membrane of from abnormal microtubular assembly,
the lysosome contains a hydrogen ion pump, which uses adenosine triphosphate (ATP) leads to impaired polymorphonuclear
to pump protons into the lysosome, against the concentration gradient. leukocytes (PMNs) phagocytosis and
frequent infections.
Mitochondria
The mitochondria are the primary site of ATP production in aerobic respiration. The
CLINICAL
proteins of the outer membrane enable the transport of large molecules (molecular CORRELATION
weight ~10,000 daltons) for oxidative respiration. The inner membrane is separated
Various inherited disorders can
from the outer by the intermembranous space and is more selectively permeable (Figure
be maternally transmitted via
1-4). The inner membrane has a large surface area due to its numerous folds, known as
mitochondrial chromosomes. These
cristae, and it maintains its selectivity with transmembrane proteins. These transmem- can show a variable expression in
brane proteins constitute the electron transport chain, and maintain a proton gradient a population due to heteroplasmy,
between the intermembranous space and the lumen of the inner membrane. The role or the presence of heterogenous
of the electron transport chain is to generate energy for storage in the bonds of ATP. mitochondrial DNA in an individual.
These diseases primarily affect the
Microtubules and Cilia muscles, cerebrum, or the nerves,
where energy is needed the most.
Microtubules are aggregate intracellular protein structures important for cellular sup- For example, myoclonic epilepsy with
port, rigidity, and locomotion. They consist of α- and β-tubulin dimers, each bound ragged-red fibers is a mitochondrial
to two guanosine triphosphate (GTP) molecules, giving them a positive and negative disorder characterized by progressive
polarity. They combine to form cylindrical polymers of of 24 nm in diameter and vari- myoclonic epilepsy, short stature,
able lengths (Figure 1-5A). Polymerization occurs slowly at the positive end of the hearing loss, and “ragged-red fibers” on
microtubule, but depolymerization occurs rapidly unless a GTP cap is in place. biopsy.
Microtubules are incorporated into both flagella and cilia. Within cilia, the microtu-
bules occur in pairs, known as doublets. A single cilium contains nine doublets around KEY FACT
its circumference, each linked by an ATPase, dynein (Figure 1-5B). Dynein, anchored
to one doublet, moves toward the negative end of the microtubule along the length of Drugs that act on microtubules:
a neighboring doublet in a coordinated fashion, resulting in ciliary motion. Kinesin is Drug Disease
another intracellular transport ATPase that moves toward the positive end of a micro- Mebendazole/ Parasitic
tubule, opposite of dynein. albendazole infections
Taxanes Cancers
Griseofulvin Fungal infections
Vincristine/ Cancers
Matrix:
citric acid enzymes, vinblastine
β-oxidation, pyruvate Colchicine Gout
dehydrogenase Cristae of mitochondria
CLINICAL
CORRELATION
A number of diseases arise from
ineffective or insufficient ciliary
motion.
Kartagener syndrome: A dynein arm
defect that impairs ciliary motion
and mucus clearance that results in
recurrent lung infections, hearing
loss, infertility, and dextrocardia situs
Intermembrane: Inner membrane: Outer membrane:
phosphotransferase electron carriers, ATP synthase Acyl CoA synthetase, inversus.
enzymes particles, membrane transporters glycerophosphate acyl Dextrocardia/situs inversus: Proper
transferase
directional development does
not occur during embryogenesis,
F I G U R E 1 - 4 . Structure of the mitochondrial membranes. The inner membrane contains causing all internal organs to be
many folds, or cristae, and the enzymes for the electron transport chain, used in aerobic located on the opposite side of the
cellular respiration, are located here. body.

A 24 nm α−tubulin β−tubulin
(+) end
5 nm
Cross section Longitudinal section Tubulin

dimer
B Enlarged microtubule doublet
Shared
A heterodimers
B
Microtubule B Dynein
Microtubule A
Nexin link
Radial
spokes Microtubule
doublet
Plasma
membrane
Inner
dynein arm
Outer
dynein arm
F I G U R E 1 - 5 . Microtubules. A Structure. The cylindrical structure of a microtubule is

depicted as a circumferential array of 13 dimers of α- and β-tubulin. The tubulin dimers are
being added to the positive end of the microtubule. B Ciliary structure. Nine microtubule
doublets, circumferentially arranged, create motion via coordinated dynein ATP cleavage.
Epithelial Cell Junctions

Transmembrane proteins mediate intercellular interaction by providing cellular adhe-
sion and cell signaling. Cellular adhesion and communication are vitally important to
both the integrity and the function of an organ.
Organs and tissues exposed to the external environment are the most resilient. These
tissues are referred to as epithelial, primarily due to their embryologic origin. The
epithelial cells of these external tissues contain an array of cell junctions that medi-
CLINICAL
CORRELATION ate cellular adhesion and communication processes. There are five principal types of
cell junctions: zonula occludens (tight junctions), zonula adherens (intermediate
Malignant epithelial cells contained junctions), macula adherens (desmosomes), hemidesmosomes, and gap junctions
by the basal membrane are termed (communicating junctions) (Figure 1-6).
carcinoma in situ. Loss of cell
junctions allows penetration through
the basement membrane as invasive Zonula Occludens
carcinoma. When cells enter the Tight junctions, also referred to as occluding junctions, have the following two primary
bloodstream or lymphatics and functions:
establish new tumors at distant sites,
they are considered metastatic. ■ Determine epithelial cell polarity, separating the apical pole from the basolateral
pole.
■ Regulate passage of substances across the epithelial barrier (paracellular transport).
MNEMONIC
In a typical epithelial tissue, the membranes of adjacent cells meet at regular intervals
CADHErins are Calcium-dependent to seal the paracellular space, preventing the paracellular movement of solutes. These
ADHEsion proteins. connections occur during the interaction of the junctional protein complex with neigh-
boring cells, composed of claudins and occludins.

Apical
Tight junction (zonula occludens)—prevents paracellular
E-cadherin movement of solutes; composed of claudins and occludins.
Actin Adherens junction (belt desmosome, zonula adherens)—below

filaments tight junction, forms “belt” connecting actin cytoskeletons of
adjacent cells with CADherins (Ca2+-dependent adhesion
proteins). Loss of E-cadherin may allow metastasis.
Cytokeratin
Desmosome (spot desmosome, macula adherens)—structural
Desmoplakin support via intermediate filament interactions. Autoantibodies
pemphigus vulgaris.
Connexon Gap junction—channel proteins called connexons permit

with central electrical and chemical communication between cells.
channel
Cell membrane
Basolateral Basement membrane
Integrins—membrane proteins that maintain Hemidesmosome—connects keratin in basal cells to
integrity of basolateral membrane by binding underlying basement membrane. Autoantibodies bullous
to collagen and laminin in basement membrane. pemphigoid. (Hemidesmosomes are down “bullow.”)
F I G U R E 1 - 6 . Epithelial cell junctions. Five types of epithelial cell junctions are depicted along with their supporting and component
proteins.
Zonula Adherens CLINICAL

Intermediate junctions are located just below tight junctions, near the apical surface CORRELATION
of an epithelial layer. Like the zonula occludens, the zonula adherens are located in a Pemphigus vulgaris: An
beltlike distribution. Inside the cell, these transmembrane protein complexes are associ- autoimmune disease of the skin
ated with actin microfilaments. Outside the cell, cadherins from adjacent cells use a due to anti-desmosome antibodies.
calcium-dependent mechanism to span wider intercellular spaces than can the zona This disrupts the cohesion between
occludens. Loss of E-cadherin may allow cancer cells to metastasize. keratinocytes, leading to fragile blisters.
The antibodies are distributed in a
reticular or “net-like” pattern. Nikolsky
Macula Adherens sign is positive.
As opposed to the beltlike distribution of the zonula occludens and adherens, desmo-
somes resemble spot welds—single rivets erratically spaced below the apical surface of
the epithelium. Intracellularly, they are associated with keratin intermediate filaments, CLINICAL
providing strength and rigidity to the epithelial surface. Like the zonula adherens, mac- CORRELATION
ula adherens are also mediated by calcium-dependent cadherin interactions. Bullous pemphigoid: An
autoimmune disease of the skin due
Hemidesmosomes to anti-hemidesmosome antibodies.
These disrupt the dermal-epidermal
These asymmetrical anchors provide epithelial adhesion to the underlying connective junction resulting in separation of the
tissue layer, the basement membrane. The hemidesmosomes contain integrin (instead layers in the form of tense bullae. The
of cadherins), an anchoring protein filament that binds the cell to the basement mem- antibodies are distributed linearly along
brane. Although the intracellular portion structurally resembles that of the desmosome, the basement membrane. Nikolsky sign
none of the protein components are conserved, except for the cytoplasmic association is negative.
with intermediate filaments.
Gap Junctions FLASH

FORWARD
These intercellular junctions allow for rapid transmission of electrical or chemical
Gap junctions allow for “coupling” of
information from one cell to the next. A connexon is formed from a complex of six
cardiac myocytes, enabling the rapid
connexin proteins. Each single connexon exists as a hollow cylindrical structure span- transmission of electrical depolarization
ning the plasma membrane. When a connexon of one cell is bound to a connexon of and coordinating contraction during
an adjacent cell, a gap junction is formed, creating an open channel for fluid and the cardiac cycle.
electrolyte transport across cell membranes.

HEMATOPOIESIS
Hematopoietic cells are stem cells residing in the bone marrow that can give rise to all
mature components of circulating blood cells and immune systems.
Blood
Blood is composed of cells suspended in a liquid phase. This liquid phase, which
consists of water, proteins, and electrolytes is known as plasma. O2-carrying red blood
cells, known as erythrocytes, make up about 45% of blood by volume. This percentage
is known as the hematocrit. Erythrocytes can be separated from white blood cells, or
leukocytes, and platelets by centrifugation. Erythrocytes form the lowest layer, and
leukocytes form the next layer, also known as the buffy coat. Plasma from which the
platelets and clotting factors have been extracted is called blood serum.
The Pluripotent Stem Cell

The hematopoietic stem cell is the grandfather of all major blood cells. These cells reside
within the bone marrow, where hematopoiesis (blood cell production) occurs. They are
capable of asymmetrical reproduction: simultaneous self-renewal and differentiation.
■ Self-renewal, integral to the maintenance of future hematopoietic potential, pre-
serves the pool of stem cells.
■ Differentiation leads to the production of specialized mature cells, necessary for
carrying out the major functions of blood.
CLINICAL Two differentiated cell lines derive from the pluripotent stem cell: myeloid and lym-
CORRELATION phoid (Figure 1-7). These cells are considered committed, meaning that they have
begun the process of differentiation and have lost some of their potential to become
RBC cytoskeletal abnormalities (eg,
hereditary spherocytosis, elliptocytosis)
cells in an alternate lineage. The myeloid lineage produces six different types of colony-
and hemoglobinopathies (eg, forming units (CFUs), each ending in a distinct mature cell: erythroid (producing
thalassemias, sickle cell anemia) cause erythrocytes), megakaryocyte (producing platelets), basophil, eosinophil, neutrophil,
significant morbidity and mortality. and monocyte (differentiates into macrophage). The lymphoid lineage produces two
cell lines: T cells and B cells.
Erythrocytes
Erythrocytes are nonnucleated, biconcave disks designed for gas exchange. These cells
measure approximately 8 μm in diameter, and their biconcave shape increases their
surface area for gas exchange, and allows them to squeeze through narrow capillaries.
CLINICAL These cells lack organelles, which are extruded shortly after they enter the bloodstream.
CORRELATION Instead, they contain only a plasma membrane, a cytoskeleton, hemoglobin, and gly-
The reticulocyte count increases when
colytic enzymes that help them survive via anaerobic respiration (90%) and the hexose
the bone marrow increases production monophosphate shunt (10%). This limits the red blood cell life span to approximately
to replenish red cell levels in the blood 120 days, after which they are mainly removed via macrophages in the spleen, and to
in response to anemia. a lesser extent, via the liver. Mature erythrocytes are replaced by immature reticulocytes
produced in the bone marrow. Reticulocytes are distinguished from mature erythrocytes
by their slightly larger diameter and reticular (mesh-like) network of ribosomal RNA.
Erythropoietin is the hormone that stimulates erythroid progenitor cells to mature by
binding to JAK2, a nonreceptor tyrosine kinase.
RBCs are highly dependent on glucose as their energy source, and glucose is transported
across the RBC membrane via the glucose transporter (GLUT-1). They are susceptible
to free radical damage, but can synthesize glutathione, an important antioxidant. Hemo-
globin’s ability to transport oxygen is closely associated with the production of 2,3-bisphos-
phoglycerate (2,3-BPG); 2,3-BPG decreases the affinity of hemoglobin for oxygen, thus
improving oxygen delivery to tissues. The iron in hemoglobin is maintained in the
ferrous state; ferric iron (Fe3+) is reduced to the ferrous (Fe2+) state via an NADH-
dependent methemoglobin reductase system. Finally, RBCs contain certain enzymes

Pluripotent stem cell
Myeloid stem cell Lymphoid stem cell
Erythropoiesis Thrombopoiesis Granulocytopoiesis Lymphopoiesis
Erythroid Thrombocyte Granulocyte/monocyte B– T–

progenitor cell progenitor cell progenitor cell lymphoblast lymphoblast
B– T–
Myeloblast Monoblast lymphocyte lymphocyte
Proerythroblast Megakaryoblast
Eosinophilic Basophilic Neutrophilic

promyelocyte promyelocyte promyelocyte Plasma cell
Basophilic Promegakaryocyte
erythroblast Promonocyte
T-helper T-cytotoxic
Eosinophilic Basophilic Neutrophilic
myelocyte myelocyte myelocyte
Polychromatic
erythroblast
Neutrophilic
Orthochromatic metamyelocyte Monocyte
erythroblast Megakaryocyte Eosinophilic Basophilic
metamyelocyte metamyelocyte
Band
Reticulocyte
Erythrocyte Platelets Eosinophil Basophil Neutrophil Macrophage
F I G U R E 1 - 7 . Blood cell differentiation. A chart of the pluripotent hematopoietic stem cell’s differentiation potential.

CLINICAL of nucleotide metabolism, and a deficiency in these enzymes (eg, adenosine deaminase,
CORRELATION pyrimidine nucleotidase, and adenylate kinase) is involved in some of the hemolytic
anemias.
Activating mutations in JAK2 can
cause myeloproliferative disorders
like polycythemia vera, essential Leukocytes
thrombocythemia, and myelofibrosis. Leukopoiesis is the process of white blood cell production from hematopoietic stem
The most common mutation for
cells. Neutrophils, basophils, mast cells, and eosinophils develop through a common
polycythemia vera is V617F (Figure 1-8).
promyelocyte lineage. Monocytes develop from a monoblast. Lymphocytes, although
separate from myeloid cells, are also considered leukocytes and arise from the lymphoid
stem cell.
EPO
All leukocytes are involved in some aspect of the immune response:

brane
Cell mem ■ Neutrophils affect nonspecific innate immunity in the acute inflammatory
JAK2
P
JAK2
P
response.
P-Y343 ■ Basophils and mast cells mediate allergic responses.
SHP-1
■ Eosinophils help fight parasitic infections.
Inhibitor
recruitment ■ Lymphocytes are integral to both cellular and humoral immunity.
F I G U R E 1 - 8 . Erythropoietin Neutrophils
(EPO) receptor. These products of the myeloid lineage act as acute-phase granulocytes. They begin in
the bone marrow as myeloid stem cells (Figure 1-7) and mature over a period of 10–14
KEY FACT days, producing both primary and secondary granules (promyelocyte stage; Figures 1-9
and 1-10). Once mature, these leukocytes are vital to the success of the innate immune
Leukos = Greek for white. system and are especially prominent in the acute inflammatory response.
Cytos = Greek for cell.
Histologically, these cells are distinguished by their large spherical size, multilobed
nuclei, and azurophilic primary granules (lysosomes). These cells have earned the
CLINICAL alternative name polymorphonucleocytes (PMNs) due to their multilobed nucleus.
CORRELATION
The key to their immune function lies in the ability of PMNs to phagocytose microbes
Chronic granulomatous disease: and destroy them via reactive oxygen species (superoxide, hydrogen peroxide, peroxyl
Congenital deficiency of NADPH radicals, and hydroxyl radicals). Neutrophils contain several enzymes, most notably
oxidase impedes the oxidative burst NADPH oxidase, which produces O2− radicals, directing the oxidative burst, as well as
in neutrophils, causing a difficulty the myeloperoxidase (MPO) system, which uses hydrogen peroxide and chloride to
in forming the reactive oxygen
generate hypochlorous acid (HOCl), a potent bactericidal oxidant.
compounds used to kill pathogens.
This results in recurrent bouts of
bacterial infection, most commonly
pneumonia and skin abscesses.
KEY FACT
Important neutrophil chemotactic

agents: C5a, IL-8, leukotriene B4 (LTB4),
kallikrein, platelet-activating factor.
F I G U R E 1 - 9 . Peripheral blood smear with neutrophilia. This peripheral blood smear

displays an extreme leukemoid reaction (neutrophilia). Most cells are band and segmented
neutrophils.

A B
F I G U R E 1 - 1 0 . Electron microscopy of neutrophils. A Highly activated neutrophils (N) with apoptotic neutrophils (black arrow) and
cell debris (black arrowhead). B Neutrophil.
Eosinophils
MNEMONIC
Eosinophils follow the same pattern of maturation as neutrophils, beginning in the bone
marrow as eosinophilic CFUs. Eosinophils also contain granules with eosinophil per- Causes of eosinophilia—
oxidase. However, they differ in that they are slightly larger than neutrophils with cat- NAACP
ionic proteins, such as major basic protein (antiparasitic) and eosinophilic cationic Neoplasia
protein (antiparasitic) within acidophilic (ie, eosinophilic) granules. Once fully mature, Asthma
eosinophils possess a large, bilobed nucleus (not multi-segmented like neutrophils) and Allergic processes
sparse endoplasmic reticulum and Golgi vesicles (Figure 1-11). Chronic adrenal insufficiency
Parasites (invasive)
Basophils and Mast Cells
Distinguished by large, coarse, darkly staining granules, basophils produce peroxidase,
heparin, and histamine (Figure 1-12). Basophils also release kallikrein, which acts as
an eosinophil chemoattractant during hypersensitivity reactions, such as contact aller-
gies and skin allograft rejection. Because they share a great deal of structural similarities,
basophils can be considered the blood-borne counterpart of the mast cell, which resides
within tissues, near blood vessels. Both mast cells and basophils produce histamine and
A B
F I G U R E 1 - 1 1 . Eosinophil microscopy. A Mature eosinophil with bright red granules.

B Electron microscopy of eosinophils with bilobed nuclei and specific granules in the shape of
a football with a crystalline core made from major basic protein.

F I G U R E 1 - 1 2 . Basophil microscopy. A Electron micrograph of a normal intact mast cell

CLINICAL with homogenous electron-dense granules. B Basophil.
CORRELATION
Mast cells release histamine, which
leads to type I allergic reactions,
heparin, but mast cells also contain serotonin (5-HT), which basophils lack. Mast cells
resulting in unpleasant allergy degranulate during the acute phase of inflammation, acting, via their released granule
symptoms and anaphylaxis. contents, on the nearby vasculature. This leads to vasodilation, fluid transudation, and
swelling of interstitial tissues.
Monocyte Lineage
Monocytes
KEY FACT Monocytes are the myeloid precursor to the mononuclear phagocyte, the tissue mac-
rophage. Morphologically, they appear as spherical cells with scattered small granules,
In tissue = macrophage akin to lysosomes. The blood monocyte is a large (10–18 μm), motile cell that margin-
In blood = monocyte ates along the vessel wall in response to the expression of specific cell adhesion proteins.
During an inflammatory response, these cell adhesion proteins (namely, platelet endo-
thelial cell adhesion molecule, or PECAM-1) facilitate monocyte diapedesis (transmi-
gration) across vessel walls into surrounding tissues. Once in close proximity to the
inflammatory foci, the monocyte differentiates into a macrophage with increased phago-
cytic and lysosomal activity (Figure 1-13).
Macrophages
During differentiation, monocyte cell volume and lysosome numbers increase. These
lysosomes fuse with phagosomes to degrade ingested cellular and noncellular material.
A B
F I G U R E 1 - 1 3 . Macrophage microscopy. A Active macrophage and B multinucleated giant

cell.

Macrophages (20–80 μm) also contain a large number of cell surface receptors. These CLINICAL
differ, depending on the tissue in which the macrophage matures, contributing to the CORRELATION
diversity of macrophage functions (Table 1-1).
Lipid A from bacterial
lipopolysaccharide (LPS) binds CD14
As described in Table 1-1, monocyte-derived cells are distributed among several organs on macrophages to induce cytokine
and tissues (including connective tissue and bone) where they reside (termed tissue- release. Toxic shock syndrome is caused
resident macrophages). Alternatively, monocytes can migrate into tissues during an acute by preformed Staphylococcus aureus
inflammatory response and, there, transform into reactive macrophages to aid the innate toxic shock syndrome toxin (TSST-1),
immune system. Once out of the circulation, monocytes have a half-life of up to 70 which acts as a superantigen and
hours. Their numbers within inflamed tissues begin to overcome those of neutrophils causes massive cytokine release.
after approximately 12 hours.
Multinucleated Giant Cells KEY FACT

At sites of chronic inflammation, such as tuberculous lung tissue, macrophages some-
Macrophages are activated by IFN-γ.
times fuse to produce multinucleated phagocytes (Figure 1-13). These microbicidal cells They can function as antigen-
can be produced in vitro via interferon-γ (IFN- γ) or interleukin-3 (IL-3) stimulation. presenting cells via MHC II.
Antigen-Presenting Cells
Antigen-presenting cells (APCs) are essential to the adaptive immune system. These
monocyte-derived phagocytic cells take up antigens (primarily protein particles), process FLASH
them, display them bound to the major histocompatibility complex (MHC) II cell FORWARD
surface marker, and travel to lymph nodes, where they recruit other cells of the immune
Dendritic cells are the most important
system into action. Dendritic cells are especially important in the initial exposure to a APCs in the body and they are
new antigen. Successful differentiation from monocytes depends on an endothelial cell responsible for initiation of adaptive
signal that is secondary to foreign antigen exposure. In the absence of this second signal, immunity.
these sensitized monocytes transform into macrophages.
Lymphocytes
Lymphocytes are easily distinguished from other leukocytes by their shared morphology
(Figures 1-14 and 1-15). After differentiating from lymphoblasts within the marrow, they
migrate to the blood as spherical cells, 6–15 μm in diameter. Typically, the nucleus
contains tightly packed chromatin, which stains a deep blue or purple and occupies
approximately 90% of the cell cytoplasm.
As the primary actors in the adaptive immune response, lymphocytes undergo bio-
chemical transformation into active immune cells via coordinated stimulatory signals.
These activated lymphocytes then enter the cell cycle, producing a number of identical
daughter cells. They eventually settle into G0 as a memory cell while they await the
T A B L E 1 - 1 . Distribution of Mononuclear Phagocytes
Marrow Monoblasts, promonocytes, monocytes, macrophages
Blood Monocytes
Body cavities Pleural macrophages, peritoneal macrophages
Inflamm tory Epithelioid cells, exudate macrophages, multinucleated giant cells

tissues
Tissues Liver (Kupffer cells), lung (alveolar macrophages), connective tissue (histiocytes), F I G U R E 1 - 1 4 . Light microscopy
spleen (red pulp macrophages), lymph nodes, thymus, bone (osteoclasts), of a lymphocyte from a blood smear.
synovium (type A cells), mucosa-associated lymphoid tissue, gastrointestinal Medium-sized agranular lymphocyte
tract, genitourinary tract, endocrine organs, central nervous system (microglia), (stained purple) with a high nuclear
skin (dendritic cells) to cytoplasmic ratio and a condensed
chromatin pattern.

CD20 CD21 CD8 CD4
CD19 CD3 CD3
B cell Tc Th
A B
F I G U R E 1 - 1 5 . Lymphocytes. A B cell and B T cell.
next stimulation event. Alternatively, following replication, daughter cells can become
terminally differentiated lymphocytes, primed for effector and secretory roles in immu-
nologic defense of the host organism.
B Cells and Plasma Cells

B cells are the “long-range artillery” in the adaptive immune response. After the lympho-
blast stage, the lymphocyte lineage diverges into B cells and T cells, each performing
separate roles in the adaptive, or humoral, immune response. Once committed, B
cells develop in the Bone marrow and then migrate to other lymphoid organs. As they
develop, B cells express immunoglobulins (IgM and IgD) on their surface, in associa-
tion with costimulatory proteins. These B-cell antigen receptor complexes allow for
the recognition of foreign antigens and subsequent activation of the B cell. Downstream
cell signaling leads to the expression of necessary genes for terminal differentiation to
plasma cells that produce and secrete antibodies to aid the specific immune response.
B cells that recognize self-antigens are triggered to undergo programmed cell death, or
apoptosis, to reduce the chance of autoimmunity.
T Cells
MNEMONIC
T cells are the “infantry” of the adaptive immune response. During maturation in the
MHC × CD = 8 (eg, MHC II × CD4 = 8, Thymus, early T cells begin expressing several surface receptors simultaneously, includ-
and MHC I × CD8 = 8). ing the T-cell receptor (TCR), CD4, and CD8. If one of these CD receptors recognizes
receptors of thymic APCs, either MHC II or I, respectively, then this T cell is positively
selected, proliferates, and matures. If a T cell recognizes self-antigen, then it is nega-
KEY FACT tively selected, and undergoes apoptosis. All T cells express CD3, and either CD4
(helper T cells), or CD8 (cytotoxic T cells).
Helper T cells “help” by mediating the
specificity of the adaptive immune Helper T Cells
response. They act as a messenger
between APCs and B cells, triggering Two subtypes of T helper cells are derived from the CD4+ progenitor: Th1 and Th2.
humoral immunity. Th1 responses occur in the presence of intracellular pathogens. Helminthic or parasitic
infections, on the other hand, drive Th2-mediated immune responses.
Helper T cells spring into action when they recognize foreign antigens bound to MHC
II. Once activated, they secrete cytokines, chemical messengers that recruit and activate
other immune effector cells. These cytokines, also called interleukins, specifically attract
B cells, which, in turn, divide and differentiate into plasma cells. After the immune
response is complete, some helper T cells become memory cells—quiescent immune
cells that retain their specificity in case of a rechallenge with the same antigen in the
future. The presence of memory cells increases the speed and efficiency of future
immune responses.
Cytotoxic T Cells
CD8+ T cells also proliferate in response to cytokines; however, they only recognize
antigens in association with class I MHC. These cells are actively involved in immune
surveillance of intracellular pathogens.

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kudottu kokonainen elämäntarina: tarina onnellisesta
avioliitosta, joka päättyi miehen uljaaseen kuolemaan. Se
sisälsi myös elämänfilosofian, joka on mutkaton ja
luterilainen. Tarinan eli minun isoäitini ja hän omisti myöskin
tuon elämänkatsomuksen.
Koko paikkakunta on keltainen.

Joku kapea juova vain
on vihreätä ja valkoista
ja sinistä näillä main.
Ja tuulimylly on kankaalla
ja jauhaa ja pyörii ja soi.
Ja poika seisoo sen vieressä
ja nauraa minkä voi.
Ja tyttö on miltei punainen,
hän on aivan palavissaan.
Ja poika on juuri kosinut
ja tyttö on antanut jaa'n.
MORAALI:
Vaan taivaalla ovat symboolit.
On ensiksi elämänpuu:
joka siitä maistaa, hän elämästä
ja onnesta huumautuu.
Ja taivaalla on tuntilaseja —
jonossa, rivittäin —:
ajan hiekka tippuu laseista,
käy nöyränä, kumarapäin
luo hautas mustan, se määräsi on,
se jokaisen määrä on.
Ja Jumalan silmä on taivaalla:
elämä on loputon.
HISTORIA:
Vaan keskellä ryijyä vuosiluku
on vanha ja himmentynyt.
Minun isoäitini rukouksia
monia hymissyt
on kutoessaan ja muistaessaan
nuoren miehen sen,
joka seilasi aavoja valtameriä
tyyrissä Alicen.
Minun isoäitini yksin jäi
leskeksi ja puutteeseen
kun Alice, uljas fregatti
upposi lasteineen…
PUER NATUS IN BETLEHEM
Me istuimme kirkossa kaikin, etupenkissä, hytisten. Ja

ikkunaholveissa tuikuttivat liekit kynttelien ja huurua tulvi
ovesta, kun kansaa saapui. Ja soi papinkello tornissa
levottomana. Urut jo huminoi kuin kaukainen syksyukkonen.
Ja nyt jo veisattiin ja lukkarin basson kohina yhtyi vapiseviin ja
valittaviin huiluihin vanhojen urkujen. Vaan kirkon yllä
veisasivat parvet enkelien.
Me istuimme kirkossa kaikin, etupenkissä, hytisten. Tänä

aamuna tunsimme elävän rovastin sanojen: ne juoksivat
saarnatuolista, luo ihmisten tulivat. Me näimme miltei
kalveten: ne olivat ihanat, ne olivat hunajan pisarat tai
Saaronin liljat tai pyhä manna Siionin korvessa, jota kerran
syödä sai koko Juudan kansa nälissään. Ne täyttivät taivaan
ja maan ja ihmeellisen lohdutuksen toivat tullessaan.
Me istuimme kirkossa kaikin, etupenkissä, hytisten. Ja

äkkiä näimme kedot ja laumat paimenten: ne olivat alttarin
luona. Koko Juudean kalpea maa oli hitaasti alkanut kynttelin
liekkien lomitse pilkoittaa. Se oli himmeä ensin, se oli kuin
utuinen yö. Vaan nyt jo, katso, lammaskatras kedolla ruohoa
syö ja purppuraviitta-paimenet sauvaansa nojaavat. Ja nyt jo,
katso, enkeliparvet, suuret, valoisat koko taivaan täyttävät
soitollaan. Ja nyt jo paimeniin on tarttunut onni ja riemahdus.
He rientävät Betlehemiin.
Oi, pieni piltti lepää keskellä eläinten. Hän on kuin lehdellä

kaste, hän on aivan nnellinen, hän ei tiedä kalkista,
orjanruususta, ristinpuusta. Hän on juuri taivaasta lähtenyt ja
nähnyt elämän hyvin ihmettelevin silmin. Hän on lapsi viaton.
Vaan tähti on hänen yllänsä. Se Kuoleman tähti on. Oi, hyvä
Maaria, taudita hänet seimessä unehen, oi, hyvä Maaria,
tuuditathan hänet syvään unehen.
Me istuimme kirkossa kaikin, etupenkissä, hytisten. Me

miltei itkimme kajahdellessa rovastin sanojen. Sitä pientä
pilttiä paimenet suuresti ylistivät ja aamun tullen saapuneet
itämaan tietäjät. Vaan myöhemmin hänet tylysti ristille
ripustettiin. Me emme tätä käsittäneet, me vaivuimme
kyyneliin: me olimme pieniä lapsia. Ja kynttiläin himmeitten
me näimme kanssamme surevan kuolemaa Jeesuksen.
Me istuimme kirkossa kaikin, etupenkissä, hytisten. Me

kuulimme rovastin sanovan lempeän aamenen. Ja katosta
lensi enkeli. Se purjehti valkoisin ja kirkkaanvärisin siivin
ihmisten penkkeihin. Se veisasi riemulaulua meidän
kanssamme. Sen me sitten näimme monesti keskellä unien.
Puer natus in Betlehem,

Cust' iloitze Jerusalem,
Halle, Halleluja.
VAATIMATTOMASTA HAUTAUKSESTA
Kylän laidassa asui tyttö, jota lapsena ihailin.

Hän kuoli sitten ja taivaassa sai morsiuskammarin,
kuten kaikki pienet tytöt, jotka varhain kuolevat.
Hänet pantiin arkkuun valkeaan ja surevat vanhemmat
sen ottivat varoen polvilleen rekeen istuessaan
ja ajoivat kiviportille lumisen hautausmaan.
Minä olin niin pieni poika. En paljon ymmärtänyt.
Minä kuulin, kun kulkuset helisivät. Marjatta, Marjatta nyt
on tulossa, sanoin äidilleni, nyt mennään tervehtimään.
Vaan sitten näin itkevän Miettiskän ja Miettisen kumaran pään.
Ja äkkiä olin ääneti. Ja valtavan onneton.
Ja minä en tiennyt ollenkaan, mikä kuolema on.
Ja kirkonkellot läppäsivät
vanhassa tornissa…
Ja isäni, joka on pappi, tuli portille paljain päin:

hänen kainalossansa käsikirjan mustat kannet näin.
Ja lukkari tuli myöskin. Ja sitten he veisasivat
ja kääntyivät hitaasti takaisin menemään molemmat.
Ja Miettisen vanhemmat pojat, ja Kasper ja Heinonen
ja Miettinen itse ja Kalle kulkivat laahustaen
ja kantoivat pientä arkkua. Oi, äiti, sano, oi,
miks kirkon tornissa iso-kello noin taukoamatta soi?
Ja äitini puristi kättäni ja me joukkoon liityttiin
ja mentiin ääneti lumista tietä. Pieniin kämmeniin
kävi tammipakkanen kovasti. Missä siis Marjatta on?
minä kysyin hiljaa äidiltäni ja olin onneton.
Ja kirkonkellot läppäsivät
vanhassa tornissa.
Hän on mennyt taivaan saleihin. Hänen ruumiinsa

haudataan: hänen valkoinen arkkunsa lasketaan juuri
helmaan maan. Minun äitini itki myöskin ja silitti päätäni. Niin
minä silloin hyrähdin minäkin katkeriin kyyneliin. Minä tiesin
äkkiä jotakin, jonka kaikki toiset jo ties. On Kuolema ollut
minulle sitten niin tuttu mies…
LEGENDA VÄSYNEISTÄ NAISISTA
On kolme köyryä niskaa, kolme naista ahkeraa. Tämän

päivän ehtooksi kitketty on koko naurismaa. Olen uupunut,
sanoo Malviina, olen kaamean uupunut, minun niskaani
polttaa ja sydäntäni on kummasti vihlaissut. Ja Sanna:
Lähden täältä, menen pojua imettämään, hän on siellä
hirveän janoissaan. Vaan Miina: Minä jään tähän viime
minuutille, vaikka loppuni sitten ois: saa kartanon rengit
kuljettaa minun ruumiini kauniisti pois.
On kolme köyryä niskaa, kolme naista kalpeaa, jotka

kankein jaloin piennarta pitkin kotiinsa vaeltaa. Tuli Jumalan
kääsit vastaan. Ja pieni enkelikin on kiivennyt hymyillen
Jumalan rinnalle Jumalan kääseihin. Ja Jumala katsoo heitä
ja viittaa kädellään. Ja raudikko-orhi karahduttaa koivikon
hämärään.
On kolme köyryä niskaa, kolme naista ihanaa, he

naurispellon pientareella nauraen vilkuttaa.
SOTAMIEHEN HAUTAUKSESTA
Rummut, rummut: Tararam, tararam. Me olimme

kunniakomppania, me tiesimme: juhlallisesti joka ainoa askel
ja jäykkien kasvojen eljet niinkauankuin marssia kaupungin
kaduilla kesti. Me olimme ennen kuin veljet, kun elimme
keskellä rauhanaikaa. Nyt rummut raikaa: Tararam, tararam.
Rummut, rummut: tararam, tararam.

Me marssimme hitaasti, kiväärit olalla, kasvot jäässä,
hyvin hitaasti marssimme ruumisvaunujen jäljessä, joissa
meidän veljemme arkussa makas, granaatinsirpale
päässä,
ja järki aivoista, sielu rinnasta poissa.
Hän kuoli keskellä rauhanaikaa.
Ja rummut raikaa:
Tararam, tararam.
Rummut, rummut: tararam, tararam.

Ah, veljemme oli nyt ruumis. Hän oli jo mätä.
Hänen nimensä oli jo sisällyksetön sana.
Me ääneti mietimme jokainen kaikkea, kaikkea tätä
kun marssimme jäykkänä kunniakomppaniana.
Me elämme keskellä rauhanaikaa.
Ja rummut raikaa:
Tararam, tararam.
MIKKO PUHTISESTA
Olin tutkinut puoleen yöhön. Olin löytänyt viimein sen

jota kaipasin dokumenteista. Mikko Puhtinen
oli von der Buchtien kantaisä, ukonkarilas:
toden totta, jo laski hiukan, oi kreivitär, kunnias!
Minä aukaisin uudinta hiukan ja katselin yöhön ja näin,
miten Otavan kyöpelivaunu oli vierinyt länteen päin.
Näin, kuinka puistossa kaikki oli himmeän hiljaista. Niin
tulin vihdoin silmäni ohjanneeksi flyygelin ikkuniin.
Kuka valvoo siellä? mä huusin.
Joku vastasi: Puhtinen.
Meren äärellä, kuutamossa,
minä tapasin neidon sen,
meren äärellä.
Otin liinan ja shaalin ja lähdin ja kolkutin voimakkain

ja rohkein iskuin. Ja flyygelin pariovet auki sain.
Koko porstua tuoksui homeelle. Näin valuvan kynttilän
suurpirtin honkapöydällä. Peräpenkillä istui hän,
toden totta, Mikko Puhtinen, hyvin vakavin naamoin. Ja pää
oli hänellä jalo. Ja ilmeessä oli jotakin viehättävää.
Oi, hyvää iltaa, mä sanoin,
oi, Mikko Puhtinen.
meren äärellä.
Minä niiasin hänelle syvään. Vaan jäykkänä istui hän.

Minun rohkea tuloni häntä ei näyttänyt häiritsevän.
On ihana yö, minä sanoin. Hän tuijotti, tuijotti vain.
Tänä yönä, jatkoin, meidän sukupuumme selville sain.
Koko Buchtien, Liewencronain, von Birckendahlien
suvut juontuvat teistä, teistä, oi Mikko Puhtinen.
Miten onnellinen te olette,
oi Mikko Puhtinen…
meren äärellä.
Hän syöksähti kiivaasti ylös. Hänen silmänsä vavahtivat.

Hän iski honkapöytään teräsnyrkkinsä molemmat.
Se on valhe, hän huusi. Sitten hän itsensä hilliten
taas lysähti raskaasti penkille. Olen Mikko Puhtinen,
joka syntyi suomalaiseks, joka eli kuin Suomen mies,
joka milloinkaan ei tietänyt, miten painaa juhdan ies,
joka iski pirulta parran, joka ruotsilta listitsi pään,
joka hirtettiin kuin suomalainen ja karsikon hämärään
pääs isäinsä luokse nukkumaan. Olet kumminkin sanonut,
että poikani poika on Birckendahl tai kreivi von der Bucht?
Mene, huuda: Mikko Puhtinen, joka ammoin hirtettiin,
on kirouksensa singonnut joka ainoaan petturiin!
Olen suomalainen, hän sanoi,
olen Mikko Puhtinen.
Meren äärellä, kuutamossa
meren äärellä.
***
Meren äärellä, kuutamossa minä tapasin

neidon sen, meren äärellä kulki hän autiolla
laulua hyräillen. Minä otin häneltä laulun hänen
kantaisästään ja kirjoitin sen kirjaan herra
Mustapään.
V
DOMINUS KRABBE
1. Pappilan nuorenherran kertomus
Hän vaelsi alakuloisena, kuten nuoret miehet aina,

vaikka sydäntä ei suinkaan vielä maailman huolet paina,
hän vaelsi tukka liehuen ja mieli jossain poissa.
Hän kuuli, kuinka lasikellot soivat vaahteroissa.
Hän kulki kotipihalla ja samalla maailmalla.
Hän seisoi hetken epäröiden kanslian ikkunan alla.
Suviyössä valitti tuuli,
lasikellot, lasikellot…
Ja laiha liekki tuikutti, tuikutti ikkunasta. Hän hätkähti ja

vaivoin välttyi takaisin juoksemasta. Se on isäni tietysti, mietti
hän, hän valvoo poikaansa tänään. Oi, poika, poika, isälläsi
on suruja nieltävänään: sinä etkö kadu viipymistäsi kylän
karkeloissa — vain sielus mistaat ja sydämesi syntipaikoissa
noissa.
Hän tarrasi ikkunaluukkuihin ja keljuili ylös vähän ja miltei

kauhusta kirkaisi kun katsoi sisään. Tähän hän totta ei ollut
valmistunut keskellä nykyistä aikaa: suviyössä olis siis
kaikitenkin hitonmoista taikaa!
Hän käsitti salamannopeasti: kaamea menninkäinen oli

kansliassa ja kirjoitti. Jokin uho, kalsea, jäinen kävi lasien
lävitse pihalle kuin luurangon kostea hiki… Hän tunsi äkkiä
Pappi Krabben. Se istui ruutua liki, se kohotti tyhjän
katseensa, hän tunsi tuon saman saaliinhimon syttyvän
siihen, jonka niin, oli sakaristossa maaliin ja kankaaseen joku
mestari ennen siveltimellä luonut. Niin, tietysti se taaskin oli
krouvissa viinoja juonut (se krouvi sijaitsi kirkolla, hänet erotti
piispa siksi, kun hän möi viinaa ja joi hän viinaa henkensä
pidättimiksi).
Hän sisään kävi ja rohkaisten luontonsa rykäisi ovella

lujaan ja arveli sillä saattaneensa haamun umpikujaan. Vaan
se oli aivan rauhallinen, ei syöksynyt ilmaan lainkaan. »Oi
iltaa poikani», sanoi se vain, »miten suuren kunnian sainkaan
kun vaivauduit minun luokseni näin myöhään yöllä ja tahdoit
minun mieltäni riemastuttaa, niin, oi poikani, mahdoit, mahdoit
hyvin nukkua vain sinun vuoteellas. Vaan äläpäs, äläpäs
huoli, jos sitten hieman juteltais, ota, istu, tuossa on tuoli…»
Ja sitten hän haamulta tietää sai: se kirkossa saarnata halas.

Se kylmeni harppujen huminalle ja taivaasta vaelsi alas,
se hetkeksi vanhan pappilan kanslian pulpettipenkille palas
ja sytytti haarakynttilän ja istuen myöhään yöhön
koko palavan henkensä voimalla vaipui saarnanvalmistustyöhön.
Sen sulka rapisi paperilla ja kirjainten jono musta
kuin huusi jo lain ja evankeliumin sanoman julistusta…
Suviyössä valitti tuuli.
Lasikellot, lasikellot
soivat vaahteroissa.
Vaan sitten se haihtui kuin usma pois. Ei näkynyt enää

häntä. Hän oli riuska ja kippura ja paksu ja pienenläntä ja yllä
keltainen sortuukki ja jalassa pieksunhylyt, kuten sakariston
taulussa, ja silmät jäiset ja tylyt.
2. Piika Amandan kertomus
Ja meidän piika Amanda oli herännyt aamulla varhain,

vaikka piikain uni, kuten tunnettua, on juuri amulla parhain.
Hän oli kuullut nurkissa kolkutusta. Ja hissun kissun kulki
jokin kaamea olento porstuassa ja ovia ryskien sulki, ja juoksi
pihalla, puutarhassa ja anturat maahan iski kuin nuija-juntta,
ja kumminkaan ei haukkunut Halli-piski.
Ja Amanda kylmässä hiessä ui ja nousi ja ovelle juoksi ja

raoitti varovaisesti ja palasi ikkunan luoksi kun mitään ei
nähnyt eteisessä, ja aukaisi ikkunanverhot. Vaan ulkona värisi
aurinko ja kedolla leikkivät perhot ja lehmät ynisi
karjatarhassa. Lahdella sumu leijas… Mikä hitto häntä unien
keskeltä turhaan ylös peijas?
Vaan äkkiä kämmenin hamuilevin hän punaiset kasvonsa

peitti: jokin valkoinen olento tallin edessä satulan selkään
heitti pienvärisen korskuvan valakkahevosen, ja itse hyppäsi
selkään.
Oli haamulla liperit leuan alla ja jalassa pieksunhylyt, kuten
sakariston taulussa, ja silmät jäiset ja tylyt…
3. Renki Epramin kertomus
Ja meidän Eprami kuului olleen tulossa kotiin. Hän mietti,

miten iloisen yön hän Nikulan Alman aitassa juuri vietti.
Hänen ajatuksensa ruusunpunaiset kiersivät tuttuja maita,
hänen huulensa vihelsi nuotteja villejä, drillejä onnekkaita.
Hän astui rennosti Ripakon kujaa kun aurinko nousi. Hän
saapui järvelle kimmeltävälle ja yli sen sousi ja katseli kuinka
korsissa sipisi, aalloilla lipisi tuuli. Hän telkkien vitinän,
ruislinnun haikean ritinän kuuli. Hän niitulla näki vilkkuvan
keltaisten kurppien nokkien, hän pajuista äkkäsi kerttujen
parvet ja ilmasta lokkien. Hänen venheensä kokka törmäsi
suhisten kaislaan ja santaan ja notkein ja nuorin jäsenin
hyppäs hän pappilan rantaan. Poissa on kulta…
Ja aurinko heitteli pappilan laseihin punaista tulta.

Ja Eprami lauloi haikeesti: Poissa on kulta…
Hän mollissa lauloi ja asteli rennosti taloa kohti.
Oi aikainen aamu! Se mutkikas polku läpi koivikon johti.
Hän lauloi mollissa: Poissa on kulta. Ja koivikko hymys.
Vaan äkkiä paukkui ja tantere soi. Ja Eprami lymys

ikikokoisen koivun rungon turviin ja kalveten näki: oli liikkeellä
valkeat menninkäiset ja hautojen väki. Pikimustalla ratsulla
karkasi kelmeä vainaja ohi ja ruoskalla vinkuvasiimaisella sen
kupeita sohi. Verenkarvainen liekki suitsusi ympäri hevosen
suusta. Ja ratsastajalla naama lie ollut pelkästä luusta, pyhä
piplia toisessa kainalossa ja jalassa pieksunhylyt, kuten
4. Kirkonvartija Optaatuksen kertomus
Ja kirkonvartija Optaatus, joka soittaa kelloja aamuin ja on,

kuten kaikki kirkonvartijat, tarkka tuntija haamuin, meni
aamulla varhain sakaristoon ja aikoi siivota siellä: näet on niin
raskasta antaa rovastin liialti tomuja niellä, se tekee kurkun
karkeaksi ja saarna ei oikein luista…
Vaan semmoista suurta säikähdystä ei Optaatus toista

muista: pikimusta ratsu on köytettynä lampetin lenkkiin ja
kauraa se rouskii nuorilla hampaillaan. Ja nurkassa joku
nauraa röhönaurua, paksua, karmivaa. Kun Optaatus sinne
kääntyy, hänen hyvänsävyinen naamansa kauhusta vinoon
vääntyy. Se on pappi Krabbe, se syntinen mies, jonka kuva
on kaapin päällä. Mitä hittoja hänkin, vainaja, on näin päivällä
vielä täällä: kuten tunnettua on vainajilla aikaa yhdestä viiteen
ja sitten niitten on lähdettävä takaisin kiireesti hiiteen… Oli
haamulla rillit nenänpäässä ja jalassa pieksunhylyt, kuten
5. Pappilan neitien kertomus
1.
Me menimme juhlapukuisina herkän-hartaalla miellä ja
yhteen kartanon Mirjamin kanssa satuimme kirkkotiellä. Me
hymyilimme ja tervehdimme. Ja Mittumaarian pellot oli
kukkamerenä: päivänkukat ja apilaat ja kellot kuin laineet
kohisi aidan takana. Väkevä koivujen haju ja kasteen tuoksu
syöksyi vastaan kuin myrskytuuli raju. Ja helähti kirkon
isokello, kun kellonsoittaja veti koko hartiavoimalla kellon
nuoraa. Sitten pimpitti heti papinkello kimein kilinöin. Se
viittasi meidän isään. Me tukkaamme hiukan sipaisimme ja
marssimme rivissä sisään.
Koko kirkkorahvas kahahti ja sitten suvivirsi soi holveissa ja

sen soidessa kaikkosi sydänten kirsi. Se on kaikkein virtten
suloisin, ah, siinä on jaloa voimaa, sen väristessä ja
helistessä totisesti soi maa… Vaan se meni poikki. Me
hämmästyimme. Virtemme jäi puoliin. Jokin peljättävä
kummitus oli kiivennyt saarnastuoliin. Joku vaimo kirkaisi
perällä. Joku pudotti kirjansa. Joku oli jäykistynyt ja huulille oli
syöksynyt manaushoku. Ja isämme, hän oli sakaristosta tullut
ovelle asti ja seisoi ja tuijotti saarnastuolia perin tuikeasti. Ja
lukkari yritti virttä taas. Vaan sävel soristen kuoli… Ja sitten
meillä ei enää ollut muuta kuin saarnastuoli ja kummitus
saarnastuolissa. Se kohotti luurankonyrkin ja pauhasi meille
lain sanoja lausein kiivain ja jyrkin. Sen kaljulla oli kalotti ja
jalassa pieksunhylyt, kuten sakariston taulussa, ja silmät
jäiset ja tylyt.
2.
Me kuulimme, kuinka Herra teki armon Juudean maalle kun

Johanneksen lahjoitti sille vanhalle Sakariaalle, me kuulimme,
kuinka Herodias oli häijy ja jumalaton kun eli alla Herodeksen
kuninkaallisen katon, me kuulimme, miten Salome tanssi
Herodeksen nähden, me kuulimme, miten Herodes antoi
Salomen tanssin tähden pyhän Johanneksen mestattavaksi
aivan ilman syytä, me kirosimme Salomea, sitä kurjaa, kurjaa
kyytä, me siunasimme Johannesta, hyvää Jumalanmiestä,
joka edelläkävi ja Messiaalle tiedot antoi tiestä. — Vaan
saarnattuaan tähän asti kummitus taukosi vähän. »Minä
tahdon tähän lisätä, minä tahdon lisätä tähän että kaikki
tietäis sen seurakunnassa: Olen kuin Herodes muinen, tämä
käsivarsi ja nyrkki tässä, tämä nyrkki kalmanluinen on
kuoleman miekkaa pidellyt ja tappanut miehen kerran, ja
totisesti se mies oli myös, kuten Johannes, mies Herran. Oi
ystävät, ystävät, kalvetkaa, sillä kenkään, kenkään teistä ei
taida silmin synnittömin Herran edessä seistä. Te olette kaikki
Herodeksia, joka ainoa miehen murhan on tehnyt omassa
sielussansa tähden himon turhan. Kuka luulee itsensä
viattomaksi Seebaotin nähden? Joka ainoa oman itsensä on
tappanut Salomen tähden…»
3.
Ja liikutus kävi seurakunnossa, itku nousi ja laski. Ja

rahvas oli kuin vastakaadettu, vastakulottu kaski, ja
vastakylvetty: odottaa sai milloin nousis oras. Joku akka huusi
ja mylvi melkein, joku ukko manas ja poras, joku kimeä-
ääninen pojan-nappula penkillä seisten huusi: »Oi taivaan
profeetta, taivaan profeetta, Messias, Messias uusi.» Ja kaksi
vanhaa-emäntää hihitti mieltä vailla, ja kaunis tyttö
ristikongilla tanssi Salomen lailla…
Ja kummitus vihdoin lopetti. Emme nähneet enää häntä.
Hän oli riuska ja kippura ja paksu ja pienenläntä ja leuassa
pieni piikkiparta ja jalassa pieksunhylyt, kuten sakariston
taulussa, ja silmät jäiset ja tylyt.
6. Vanhan haudankaivajan kertomus
Hän kuului juuri siirtäneen mädän hautalaudan pois

kiviaidalle reunustalta vastaluodun haudan ja sitten ääneti
istahtaneen. Ja hän hautarivit näki ja mietti, että siinä se
nukkui pitäjän vanha väki: oli paroonia ja riiarinnaa ja rovastia
ja muuta — vaan itseasiassa kuitenkin vain rapiata luuta, joka
helponlaisesti murenee ja tomuks ja tuhkaks hajoo, kun
kaivaessaan lapion terällä hiukkasenkin kajoo…
Niin, sielu, sanovat, ikuisesti veisaa ilossa taivaan, vaan

ruumis, miksi se katoaa, miks ruumiin madot sai vaan… Ja
hän sytytti niveräpiippunsa. Niin, oli se kysymys vakaa. Hän
hymähti lievästi itsekseen. Vaan silloin puitten takaa tuli
hitaasti ratsu ja ratsumies. Mitä kummaa ne tekivät tässä
pyhää kirkkorauhaa sunnuntaina noin julkeesti
häiritsemässä? Ravas ratsu Krabben haudalle. Hävis
ratsumies satulasta. Ja silloin hauturi äkkäsi, hän äkkäsi
silloin vasta: oli miehellä piirteet kauheat, oli silmät jäiset ja
tylyt, kuten sakariston taulussa, ja jalassa pieksunhylyt.

Textbook First Aid For The Basic Sciences General Principles Tao Le Ebook All Chapter PDF

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Textbook First Aid For The Basic Sciences General Principles Tao Le Ebook All Chapter PDF

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First Aid for the Basic Sciences.

General Principles Tao Le

First Aid Cases For The USMLE Step 1 Tao Le

First Aid for the USMLE Step 1 2021 Tao Le

First Aid for the USMLE Step 1 2019, Twenty-Ninth

First Aid for the USMLE Step 1 2019, Twenty-Ninth

First Aid For the USMLE Step 1 2020, Thirtieth Edition

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First Aid for the USMLE Step 1 2024 A Student to

Statistics for the Social Sciences A General Linear

SENIOR EDITORS EDITORS

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To our families, friends, and loved ones, who supported us

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How to Use This Book

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Anatomy and Histology

CELLULAR ANATOMY AND HISTOLOGY 2 Splenic Anatomy 20

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Cellular Anatomy and Histology

Aqueous phase (extracellular)

“Oil” or nonpolar phase

Aqueous phase (cytoplasm)

F I G U R E 1 - 1 . Amphipathic lipids. A Phospholipid, with a phosphate head group and a lipid

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The cell membrane performs the following functions:

Rough Endoplasmic Reticulum and Ribosomes

Smooth Endoplasmic Reticulum

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Functions of the Golgi Apparatus

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Cross section Longitudinal section Tubulin

B Enlarged microtubule doublet

F I G U R E 1 - 5 . Microtubules. A Structure. The cylindrical structure of a microtubule is

Epithelial Cell Junctions

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Actin Adherens junction (belt desmosome, zonula adherens)—below

Connexon Gap junction—channel proteins called connexons permit

Zonula Adherens CLINICAL

Gap Junctions FLASH

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The Pluripotent Stem Cell

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Pluripotent stem cell

Myeloid stem cell Lymphoid stem cell

Erythropoiesis Thrombopoiesis Granulocytopoiesis Lymphopoiesis

Erythroid Thrombocyte Granulocyte/monocyte B– T–

Eosinophilic Basophilic Neutrophilic

Erythrocyte Platelets Eosinophil Basophil Neutrophil Macrophage

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All leukocytes are involved in some aspect of the immune response: