Intro to Anatomy and Physiology

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1
Define anatomy
the study of form
2
Define physiology
the study of function
3
4 ways of examining the structure of the body
inspection (looking)
palpation (feeling)
auscultation (listening)
percussion (tapping)
4
Define gross anatomy
study of organs and body parts without the use of magnification
ex. cadavers
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Define regional anatomy
study of all structures in a region
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Define systematic anatomy
study of one system at a time
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Define medical imaging
use of imaging equipment without the use of surgery
ex. x-rays
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Define histology
study of tissues
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Define cytology
the study of cells
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Define embryology
study of development from fertilized egg to 8th week utero
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Define gerontology
study of older individuals
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Define histopathy
study of tissues for signs of disease process
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Define neurophysiology
study of nervous system physiology
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Define endocrinology
physiology of the endocrine system
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Define pathophysiology
mechanism of diease
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Define exercise physiology
how the body responds to exercise
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Define cardiovascular physiology
activity of the heart and blood vessel
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How do scientists study anatomy and physiology?
from hypothesis
design and implement an experiment
collect data
analyze data
report results
peer review
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Independent variable
you control it (found on x axis of graphs)
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Dependent variable
what you measure (found on y axis)
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Control group
untreated, used for comparison
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psychosomatic effects
effects of subject's state of mind on her or his physiology
tested by giving placebo to control group
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Structural hierarchy
atom
molecule
organelle
cell
tissue
organ
organ system
organism
***living things are organized this way
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Anatomical Variation
no two humans are exactly alike
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Interrelatedness of body systems
No body system works in isolation
All systems affect every other system
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Physiological variation
sex, age, diet, weight, physical activity, etc.. impact physiology
failure to consider variation can lead to overmedication
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Reference man
22 years
154 pounds
light physical activity
2,800 kcal/day
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Reference woman
22 years
128 pounds
light physical activity
2,000 kcal/day
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Homeostasis
tendency of body to maintain a relatively constant internal environment
process that body works to achieve
body monitors temp, pressure, and chemistry
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3 Parts of homeostatic mechanism
receptor
integrating (control) center
effector
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Receptor
structure that senses change in the body
Ex: during exercise, receptor notices 102 degree body temp
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Integrating (control) center
control center that processes the sensory information
makes a decision and directs the response
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Effector
cell or organ that carries out the final corrective action to restore homeostasis
Ex: during exercise, creates sweat and moves blood towards extremities
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Negative feedback
reversal of initial stimulus
ex: if too cold, vessels in the skin constrict and shivering begins so heat is produced
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Positive feedback
enhancement of initial stimulus
ex: childbirth
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Cell theory
-all organisms are composed of cells and cell products
-cell is the simplest structural and functional unit of life
-an organism's structure and functions are due to the activities of the cell
-cells come only from preexisting cells
-cells of all species exhibit biochemical similarities
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How many types of cells in human body?
about 200 types all varying in shapes
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squamous shape
thin, flat, scaly
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cuboidal shape
squarish looking
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columnar shape
taller than wide
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polygonal shape
multiple sides, irregularly angular shapes
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stellate shape
star like
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spheroid to ovoid shape
round to oval
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discoid shape
disc shaped
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fusiform shape
thick in the middle, tapered toward the ends
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fibrous shape
thread like
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Human cell size
most cells are 10-15 micrometers in diameter
need microscope to see
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Largest cell
egg cell (100 micrometers long)
can see with naked eye
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Why is cell size limited?
an overly large cell cannot support itself and may rupture
for a given increase in diameter, volume increases more than surface area
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Plasma membrane
surrounds cell
defines boundaries
keeps inside in and outside out
made of proteins and lipids
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Cytoplasm
includes organelles, cytoskeleton, inclusions, and cytosol
gel like
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Extracellular fluid
fluid outside of cells
includes tissue (interstitial) fluid
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Cytoskeleton
-determines cell shape
supports structure
organizes cell contents
directs movement of materials within the cell
contributes to movements of the cell as a whole
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3 parts cytoskeleton
microfilaments
intermediate filaments
microtubules
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microfilaments
6nm thick (thinnest)
helps with movement
made of actin protein
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intermediate filaments
8-10nm thick (medium)
gives cell shape, resists stress
made of keratin protein
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microtubules
25nm thick (largest)
maintains cell shape, holds organelles, acts as railroad tracks for walking motor protein, make axonemes of cilia and flagellum form mitotic spindle
made of tubulin protein
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Organelles
internal structures of a cell, carry out specialized metabolic tasks
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Membranous organelles
nucleus, mitochondria, lysosomes, peroxisomes, endoplasmic reticulum, and golgi complex
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Nonmembranous organelles
ribosomes, centrosomes, centrioles, and basal bodies
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Nucleus
largest organelle
cells can be anuclear or multinucleate
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nuclear envelope
double membrane around the nucleus
perforated by nuclear pores
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Nuclear pores
regulate molecular traffic through envelope
hold the two membrane layers together
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Nuclear lamina
web of protein like filaments
provides points of attachment for chromatin
helps regulate cell life cycle
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Nucleoplasm
material in nucleus
composed of chromatin and nucleoli
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Chromatin
threadlike
composed of DNA and protein
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Nucleoli
masses where ribosomes are produced
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Endoplasmic reticulum
system of channels (cisternae) enclosed by membrane
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Rough endoplasmic reticulum
parallel, flattened sacs covered with ribosomes
-continuous w/ outer membrane of nuclear envelope
-produces phospholipids and proteins of the plasma membrane
-synthesizes proteins that are packaged in other organelles or secreted from cell
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Smooth endoplasmic reticulum
lacks ribosomes
-cisternae are more tubular and branching
-thought to be continuous with rough ER
-synthesizes steroids and other lipids
-detoxifies alcohol and other drugs
-calcium storage
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Golgi complex
a system of cisternae that synthesizes carbohydrates and puts finishing touches on protein synthesis
-receives newly synthesized proteins from rough ER
-sort proteins, splices some, adds carbohydrate moieties to some, and packages them into membrane bound golgi vesicles
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Golgi vesicles
-some vesicles become lysosomes
-some migrate to plasma membrane and fuse to it
-some become secretory vesicles that store a protein product for later release
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pathogen
disease forming organism
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Lysosome
vesicle/package of enzyme (probably a protein) bound by a membrane
"Suicide Sac"
-has the ability to breakdown the cell
-body puts pathogen in vesicle which connects to lysosome and lysosomes breaks down the pathogen
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Ribosome
-small granules of protein and RNA
-make proteins
-found in nucleoli, cytosol, and outer surfaces of rough ER and nuclear envelope
-read coded genetic messages (messenger RNA) and assemble amino acids into proteins specified by the code
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Functions of Ribosome
intracellular hydrolytic digestion of proteins, nucleic acids, complex carbohydrates, phospholipids, and other substances
autophagy
autolysis
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Autophagy
digestion of cell's surplus organelles (ability of cell to break itself down)
(self to eat)
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Autolysis
"cell suicide"
digestion of a surplus cell y itself
(self to split)
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Peroxisomes
resemble lysosomes but contain different enzymes and are produced by endoplasmic reticulum
specialized vesicle
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function of peroxisome
use molecular oxygen to oxidize organic molecules
abundant in liver and kidneys
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enzymes
catalyze reactions
names usually end in -ase
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Proteosomes
hollow cylindrical organelle that disposes of surplus proteins
looks like meat grinder
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function of proteosomes
contain enzymes that break down tagged, targeted proteins into short peptides amino acids
-tags proteins it wants to get rid of
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Mitochondria
organelles specialized fro synthesizing ATP
looks like a "footprint" or kidney bean
continually change shape from spheroidal to thread like
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cristae
inner membrane folds of mitochondria
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matrix
spaces between the cristae of the mitochondria
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How does mitochondrion make ATP?
cellular respiration
1. glucose (glycolysis)
2. Pyruvate (prep step)
3. Mitochondrion
4. Kreb's Cycle
5. Electron transport chain
6.ATP
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AMP
adenosine monophosphate
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ADP
adenosine diphosphate
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ATP
adenosine triphosphate
contains the most energy
When molecules need energy to form a reaction, ATP is broken into ADP or AMP and it shares P energy
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Basal body
each is a centriole that originated in centriolar organizing center and then migrated to the membrane
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2 kinds of inclusions
stored cellular products
foreign bodies
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Stored cellular products
glycogen granules, pigments, and fat droplets
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Foreign bodies
viruses, intracellular bacteria, dust particles, and other debris photosynthesized by cell
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Inclusions
never enclosed in a unit membrane
not essential for cell survival
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Matter
anything that has mass and takes up space (solid, liquid, gas)
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atom
smallest unit of matter
basic unit of matter
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protons
positively charged particles found in nucleus and has mass of 1amu
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neutrons
neutral particles found in the nucleus and has mass 1 amu
100
electrons
negatively charged particles found in circling nucleus in orbitals, negligible mass, always in motion
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element
simplest form of matter to have unique chemical properties
102
periodic table
elements arranged by atomic number
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atomic number
number or protons in nucleus
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atomic mass
the number of protons + the number of neutrons
AKA mass number or atomic weight
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6 main elements in human body
Carbon
Hydrogen
Oxygen
Nitrogen
Phosphorus
Sulfur
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Carbon
C
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Hydrogen
H
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Oxygen
O
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Nitrogen
N
110
Phosphorus
P
111
Calcium
Ca
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Sulfur
S
113
Iodine
I
114
Iron
Fe
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Potassium
K
116
Sodium
Na
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Chlorine
Cl
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Magnesium
Mg
119
Chromium
Cr
120
Cobalt
Co
121
Copper
Cu
122
Fluorine
Fl
123
Manganese
Mn
124
Minerals
inorganic elements extracted from soil by plants and passed up food chain to humans
-important fro body structure and enzyme function
125
List of minerals
Ca, P, Cl, Mg, K, Na, S
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Valence elctrons
orbit in the outermost shell and determine chemical bonding properties of an atom
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octet rule
an atom is the most stable when outer shell of electrons is full
128
1st orbital holds
2 electrons
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2nd orbital holds
8 electrons
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3rd orbital holds
8 electrons
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atoms
uncharged particles
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ion
charged particle (atom or molecule) w/ unequal of protons and electrons
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anion
particle that gains electrons
ex. Na^-1
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cation
particle that loses electron
ex. Cl^+1
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ionization
transfer of electrons from one anion to another
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free radicals
short lives particles w/ an unpaired valance electron
VERY reactive
produced by normal metabolic reactions, radiation, and certain chemicals
trigger reactions that destroy molecules and can cause cancer, death of heart tissue and aging
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antioxidents
chemicals that neutralize free radicals
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Electrolyte
substance that ionize in water and form solutions capable of conducting electric current
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Why is electrolyte balance important?
imbalance can lead to coma or cardiac arrest
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isotopes
varieties of an element that differ only in the number of neutrons
can be radioactive
141
relative atomic weight
accounts for the fact that an element is a mixture of isotopes
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radiosotopes
unstable isotopes that decay and give off radiation
every element has at least 1
intense radiation can be ionizing and cause genetic mutations and cancer
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physical half life of radioisotopes
time required fro 50% to decay to stable state
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biological half life of radiation
time required for 50% to disappear from the body
145
organic
molecule that contains carbon and hydrogen
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inorganic
every molecule that does not contain carbon and hydrogen
everything else
147
important inorganic molecules to humans
carbon dioxide
oxygen
water
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cohesion
water binds with water
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adhesion
water binds with other molecules
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universal solvent
water
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hydrophilic
polar or charged (sugar)
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hydrophobic
nonpolar or neutral (fats)
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acid
a proton donor
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base
a proton acceptor
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Neutral pH
7
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Acidic pH
under 7
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Basic pH
over 7
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what is pH
measurement of molarity of H+ on a logarithmic scale
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buffers
chemical solutions that resist changes in pH
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Phenol red pH indicator
acid=yellow
base=pink
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pH of blood
should be slightly basic
crucial for physiological functions
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organic chemistry
the study of compounds containing carbon
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4 categories of carbon compounds
carbohydrates
lipids
proteins
nucleic acids
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How many valence electrons does carbon have?
4
carbon atoms bind readily w/ each other to form carbon backbones
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functional groups
hydroxyl
carbonyl
carboxyl
amino
phosphate
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hydroxyl
carbohydrates
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carbonyl
lipids
168
carboxyl
proteins
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amino
proteins
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phosphate
DNA, ATP
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macromolecules
very large organic molecules w/ high molecular weights
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polymers
macromolecules made of a repetitive series of identical or similar subunits (monomers)
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starch
polymer of about 3,000 glucose monomers
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polymerization
joining monomers to form a polyer
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Carbohydrate function
easily accessible, readily available source
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monomer
often found as a ring structure in nature
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3 important monosaccharides
glucose, galactose, and fructose
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Blood sugar
glucose
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disaccharide
sugar made of 2 monosaccharides
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3 important disaccharides
sucrose
lactose
maltose
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sucrose
table sugar
glucose + fructose
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lactose
sugar in milk
glucose + galactose
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maltose
grain products
glucose + glucose
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oligosaccharides
short chains of 3 or more monosaccharides
(at least 10)
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polysaccharides
long chains of monosaccharides
(at least 50)
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3 key examples of polysaccharides
glycogen
starch
cellulose
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glycogen
energy storage in cells of liver, muscle, brain, uterus, vagina
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starch
energy storage in plants that is digestible by humans
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cellulose
structural molecule in plants that is important for human dietary fiber
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carbohydrate structure
2:1 structure of hydrogen to oxygen
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monomer of carbohydrate
monosaccharide
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lipids
hydrophobic organic molecules with high ratio of hydrogen to oxygen
have more molecules per gram than carbs
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5 primary types of lipids in humans
fatty acids
triglycerides
phospholipids
eicosanoids
steroids
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Lipids: fats, oils, waxes
long term energy storage/ waterproofing
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monomer of lipids
fatty acids
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saturated fatty acids
have a lot of hydrogen
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unsaturated fatty acids
contain some double bonds between carbons in chains (potential to add nitrogen)
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polunsaturated fatty acids
have multiple bonds between carbons in chain
199
essential fatty acids
must be obtained from food
200
trans fatty acids
-2 covalent single c-c bonds angle in opposites on each side of the c=c double bond
-resist enzymatic breakdown in the human body, remain in circulation longer, deposits in the arteries thus raises the risk of heart disease
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cis fatty acids
-2 covalent single c-c bonds angle in the same direction adjacent to the c=c double bond
202
phospholipids
-similar to neutral fats except one fatty acid is replaced by a phosphate group
-structural foundation of cell membrane
-amphipathic
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fatty acid tails
hydrophobic
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phosphate head
hydrophilic
205
steriod
lipid w/17 carbon atoms in 4 rings
206
eicosanoids
20 carbon compounds derived from arachiolonic acid
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cholesterole
the "parent" steroid from which other steroids are synthesized
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HDL (high density lipoprotein)
"good" cholesterol
-lower ratio of lipid to protein
-may help to prevent cardiovascular disease
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LDL (low density lipoprotein)
"bad" cholesterol
-high ratio of lipid to protein
-contributes to cardiovascular disease
210
examples of lipids in bacteria
-acid fast organisms
-contain mycolic acid in cell walls
-can be stained w/carbolfuschin (red/pink)
-non acid fast stain blue w/methylene blue
-myobacterium tuberculosis
211
protein
a polymer of amino acid
212
monomer of protein
amino acid
central carbon w/ 3 attachments
-amino group (NH2), carboxyl group (-COOH), and radical group (R group)
213
peptide
proteins
any molecule composed of 2 or more more amino acids joined by peptide bonds
214
peptide bonds
special bond found between amino acids
215
naming of peptides
dipeptides have 2 amino acids
tripeptides have 3 amino acids
polypeptides have more than 15
proteins have more than 50
216
dehydration synthesis
creates a peptide bond that joins the amino acid of one group to the carboxyl group of the next
217
conformation
unique, 3 dimensional shape of protein crucial to function
proteins can reversibly change conformation and thus function
it is the shape of the protein that gives it its function
218
denaturation
protein loses shape/function/form
-extreme heat or pH or heavy metals
219
Primary structure of proteins
sequence of amino acids which is encoded in the genes
220
secondary structure
coiled or folded shape held together by hydrogen bonds
221
most common secondary structures
alpha helix: spring like shape
beta helix: pleated, ribbon like
222
tertiary structure of proteins
further bending and folding of proteins into globular and fibrous shapes due to hydrophobic-hydrophilic interations and vander waals forces
223
globular proteins
compact tertiary structure for proteins within cell membrane and proteins that move freely in body fluids
224
fibrous proteins
slender filaments suited for roles in muscle contraction and strengthening of skin and hair
225
quaternary structure of proteins
associations of 2 or more polypeptide chains due to ionic compounds and hydrophobic-hydrophilic interactions
-occurs only in some proteins
226
keratin
tough structural protein of hair, nails, and skin surfaces
227
collagen
protein contained deeper in the layers of skin, bones, cartilage, and teeth
228
ligand
a molecule that reversibly binds to a protein
229
cell adhesion
proteins bind cells together
ex. sperm and egg
keeps tissues from falling apart
230
membrane proteins
govern what passes
carriers transport solutes to other side of membranes
231
motor proteins
molecules with the ability to change shape repeatedly
232
substrate
substance enzyme acts upon
233
product
substance produced in the reaction
234
active site
physical location where enzyme and substrate interact
235
catabolism
break down (to release energy)
236
anabolism
construct molecules (use energy)
237
cofactors
2/3 of human enzymes to require nonprotein cofactor
some are organic
some bind to enzyme and induce a change in its shape which activates the active site
essential to function
238
coenzymes
organic cofactors derived from water soluble vitamins
accepts electrons from an enzyme in one metabolic pathway and transfer them to an enzyme in another
239
Adenosine Triphosphate
body's most important energy transfer molecule
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