Chapter 1: The Human Body: An Orientation
An Overview of Anatomy and Physiology
I. Anatomy – study of body organization and
structure, and their relationships; Structure
determines the function
 Developmental Anatomy – conception to
adulthood
 Embryology – first 8 weeks of
development
 Structures studied with a microscope
 Cytology –cell
 Histology – tissues
 Ways to study anatomy
 Gross Anatomy – systemic or
regional perspective
 Surface Anatomy – using
anatomical landmarks to locate
internal features
 Anatomical Imaging – non-invasive
way of viewing internal body
structures
II. Physiology – the study of the structure’s function
 Exercise physiology – study changes in the
body after exercise
III. Pathology – study of all disorders
Levels of Structural Organizations
Maintaining Life
Necessary Life Functions: (1) Maintain
Boundaries, (2) Movement, (3) Responsiveness, (4)
Digestion, (5) Metabolism, (6) Excretion, (7)
The Language of Anatomy
I. Directional Terms
 Superior (cranial) – toward the head
 Inferior (caudal) – towards the tail
 Anterior (ventral) – towards the belly
 Posterior (dorsal) – towards the back
 Proximal – near the origin, trunk, or point of
attachment
 Distal – farther the origin, trunk, or point of
attachment/ towards the end
 Medial – along the coronal towards the
sagittal
 Lateral – along the coronal away from sagittal
 Superficial – near the surface
 Deep – far from the surface
II. Body Planes
 Transverse Plane – parallel to the ground
 Coronal Plane – division from front and
back
 Sagittal Plane – division from left and right
III. Body Cavities
 Dorsal – protected by the bone
 Cranial – contains the brain
 Spinal – contains the spinal cord
 Ventral – less protected
 Thoracic – extends superiorly to
the diaphragm; where the heart and
lungs are protected by the ribcage
 Abdominopelvic – extends
inferiorly from the diaphragm;
contains digestive, urinary, and
reproductive organs. The abdomen
is only protected by the trunk
muscles while the pelvic is
somewhat protected by the pelvic
bones.
 Smaller body cavities (Oral, Nasal Orbital,
Middle Ear)
Reproduction, (8) Growth

IV. Regional Terms

 Homeostasis

I. Homeostasis – Ability to regulate internal balances

with response to external changes. Disruption can lead
to disorder in the body

 3 components of homeostatic reflux – (1)

receptors sense stimuli > (2) control centers
assess and integrate appropriate response to the
stimuli > (3) effectors that execute the response
(output)
II. Negative feedback mechanism – reduce or stop
initial stimuli

III. Positive feedback mechanism – increase initial

stimuli
Chapter 2: The Chemical Basis of Life

Basic Chemistry
III. Chemical Bonding
I. Matter, Mass, Weight

 Matter – is anything that occupies space

and has mass. Exists in three forms (solid,
liquid, and gas)
 Mass – amount of matter in a substance or  Ionic bond – characterized as the
object electrostatic attraction between a positively
 Weight – exerted force of gravity on matter and negatively charged ion. Between
metals and nonmetals (not all)
II. Atoms - Atoms are the basic unit of elements  Cation gives up electrons (+) and
Anion gains electrons (-)
 Atoms contain 3 subatomic particles ex. NaCl (Sodium chloride) ED = 2.1
 Proton – positive charge (inside the
nucleus)
 Neutron – no charge (inside the
nucleus)
 Electron – negative charge (outside
the nucleus)
 Important values
 Atomic number - the number of
proton/s in an atom. In a neutral
atom, the number of electrons is
the same as the number of protons
 Atomic mass unit (amu)/Dalton – note: metals tend to be cations and nonmetals anion
the total mass of an atom = number  Covalent bond – characterized as the
of protons + number of neutrons sharing of electrons between non-metals in
 Isotopes
 Elements with the same number of a chemical bond
protons but different number of  Polar covalent bond – when atoms
neutrons resulting in different don’t have enough electronegativity
atomic mass
difference for ionization, the one
  Electronegativity – degree to which an with higher electronegativity will
atom attracts electrons in a chemical bond
hog all the electrons (partially
negative) from the other (partially
positive)
ex. HCl (Hydrochloric Acid) ED = 0.9

 Valence electrons – the electrons in the

outer shell of an atom that will participate
in chemical bonding.
 Octet rule - atoms tend to prefer
having 8 electrons in their valence
shell. (2-8-8).

 Non-polar covalent bond – the

electrons are shared evenly
(typically occurs between atoms of
the same element)
 Moles –23standard quantity to represent the
6.02x10 (Avogadro’s number) of small
substances (atoms, ions, molecules)

IV. Atoms, Molecules, Elements and Compounds ex. salt and sugar dissolved in water

VII. Chemical structures

Diatomic gases include – Br I N Cl H O F

V. Intermolecular Forces – force that mediates
interaction between molecules

 Hydrogen bonding – weak attraction

between a positively charged hydrogen and
negatively charged oxygen or other polar
molecules.
ex. (1) water and (2) ethanol
 Carbons live in ends and bends
 suffix -ane means single bond
 suffix -ene means double bond
 Hydrogen loves carbons
ex. caffeine (C8H10N4O2)

 Fluorine, Oxygen, and Nitrogen can

 also participate in hydrogen bonding
aside from hydrogen

Chemical Reactions and Energy

VI. Solubility and Dissociation
 Solubility is a substance’s ability to
dissolve in another substance
 Electrolytes – ionic compounds that
dissociate in water and conduct electrical
charge
 Non-electrolytes – molecules that do not
dissociate in water and do not create I. Synthesis Reaction – A+B=AB (cross multiply
electrical charge the electrical charge then balance)

II. Decomposition Reactions

VII. Energy – ability to do work

 Potential energy – stored energy that could
III. Single Replacement
do work
 Kinetic Energy – energy doing the work

IV. Double Replacement - Metal x Nonmetal

 Chemical energy – potential energy stored

in the chemical bonds of a substance
 lesser pt of reactant, energy is
required for chemical reaction and
V. Reduction-Oxidation Reactions (Redox the prodcut will have greater pt
Reactions) always occur together  greater pt of reactant, energy is
released for chemical reaction to
occur and the product will have
greater pt
VIII. Speed of Chemical Reactions
  Activation energy – minimum amount of
required energy for chemical reaction to
occur
 Catalyst – substance that speeds up the rate
of chemical reaction without it being
changed
 Enzymes – protein catalyst that
lowers the activation energy, thus,
increasing the speed and rate of
VI. Reversible Reactions chemical reaction
 characterized when formed products revert
back to their old reactants

ex. Ammonium chloride (NH4Cl) reverts back to

ammonium (NH3) and Hydrogen chloride (HCl)
when heated (thermal decomposition) and both
these reactants react to form NH4Cl crystals.
 Forward – there are more NH4Cl
and less NH3; HCl, thus forward is
faster
 Backward – after a while, there will note: temperature and concentration can affect the rate of
be more NH3; HCl thus, backward chemical reaction
rate will be faster
 Equilibrium – the speed rates of
both forward and backward are the
same (does not mean one is more)

Inorganic Chemistry
I. Inorganic Chemistry – are substances that lack
carbon or carbon-hydrogen bonds.
II. Water – polar molecule that forms hydrogen
bonds together or with other polar molecules
 Polarity/Solvent properties
 all chemical reactions in the body
are dependent on water’s solvent
properties
 acts as a transport and exchange
medium as it easily dissolves
nutrients, waste products,
respiratory gases.
 Hydrophilic – substances that
interact with water (polar
molecules and ionic compounds)
 Hydrophobic – substances that
repel water (nonpolar molecules)
 Cohesion – water molecule – water
molecule interaction
 Adhesion – water molecule – another
polar/ionic object
 Salts (Na+Cl-) – ionic compound that
dissociates in water
 PH, Acids and Bases
 Acids – substance that release
hydrogen ions (H+) or proton (H+)
donor
o strong acids – completely
ionize and liberate all their
protons (ex. HCl  H+ +
Cl-)
o weak acids – ionize
incompletely (ex.
)
 Bases – grabs protons or donates
OH- when they dissociate (ex.
NaOH Na+ + OH-) or
(OH- + H+  H2O)
  pH – express acidity or alkalinity
of solution (enzymes only work at
certain pH and a change can result
 Regulates body temp with its high heat in denaturing)
capacity. Sweating results from evaporation
of water from the body releasing heat
 Protects body by acting as a lubricant or
cushion to avoid friction damage or
physical trauma (at joints or body cavities)
 Acts as a reactant by adding water
molecules to chemical bonds to break them a change in pH by 1 in solution represents a 10-fold
down (hydrolysis; water-splitting) change of H+ concentration. The lower the value
means H+ is more concentrated, thus, acidic.

 Buffers – molecule that maintains

pH at a constant rate
III. Electrolytes – produces + charged and –
charged ions when dissolved in water (has the
ability to conduct electricity in solution)

note: Normal blood pH ranges from 7.35 to 7.45.

Slight deviations outside this range can be fatal

Organic Chemistry  Polysaccharides – chains of simple sugars

I. Organic Chemistry – Carbon containing
compounds that comprise living matter. Many of
these compounds are polymers (carbohydrate and
protein)
 Polymers - chainlike structures that is
formed by a single unit called monomers
that are joined together by dehydration
synthesis
 Dehydration synthesis – one hydrogen (H)
atom is removed from one monomer and a
hydroxyl group (OH) is removed from the
other monomer (releasing H2O)
 Hydrolysis – adding H2O between bonds to
release the monomers
II. Carbohydrate – it contains carbon-hydrogen-
oxygen in a 1:2:1 ratio
 acts as a short term (converted to ATP) and
long term (glycogen for animals, starch and
cellulose for plants) energy storage
 suffix -ose is used for describing and
naming carbohydrates
 Starch – grains or root vegetables
 Glycogen – long term energy
storage molecule in muscles/liver
 Cellulose – can’t be used as
energy but many nutritional
benefits (dietary fibers; leafy
greens)
III. Lipids – energy rich non-polar (hydrophobic)
compounds containing carbon-hydrogen-oxygen in
a 1:2: little oxygen ratio (C57H110O6)
 Triglycerides – one glycerol backbone
with three fatty acids linked to it by
dehydration synthesis
  Monosaccharide – one sugar; the building
block of carbohydrate (fruits, veggies,
honey)
 Glucose – blood sugar; universal
cellular fuel
 Fructose and Galactose – converted
to glucose for cell function  Saturated fats – single C-C bonds
 Deoxyribose and Ribose – part of pack closely at room temperature
nucleic acid structure  Unsaturated fats – double or triple
bonds between C-C causing it to
curve, thus, not solidify at room
temperature
 Omega-3 and Omega-6
polyunsaturated - heart healthy -
the first double bond is found at
the 3rd and 6th carbon
 Disaccharide – two monosaccharides joined by
dehydration synthesis and is broken down by
hydrolysis for digestion

Sucrose: Table sugar

Lactose: Milk

Maltose: Malt sugar

(beer)  Trans Fats - chemically altered
unsaturated fat by hydrogenation
(unsuccessful) (rare in nature,
thus, no enzyme to break it down)

 The structure and function of

protein is dictated by the type and
order of amino acids
 Peptide – 2 amino acids bonded by
dehydration or protein synthesis

 Phospholipids – same to triglycerides

except that one of the fatty acids is
replaced by a phosphate containing region.
the polar side is the one containing the
phosphate and the nonpolar side which  Four Levels of Protein Structure
contains the fatty acids
Dipeptide 2 amino acids joined together
Tripeptide 3 amino acids joined together
Tetrapeptide 4 amino acids joined together
Oligopeptid 2-20 amino acids
e
Polypeptide 21-49 amino acids
Protein More than 50 amino acids
  Primary – sequence of amino acids
in the polypeptide chain
determined by DNA

 Steroids – do not contain fatty acids,

 Secondary - hydrogen bonding
instead, have interlocking four carbon ring
(dotted red lines). The hydrogen
structure.
bonds cause the amino acid chain
 Cholesterol – found in cell
to form pleated (folded) sheets or
membranes and synthesize other
helices (coils).
steroids
 Tertiary – interaction of side
 Bile salts – increase fat absorption
chains (denaturing occurs when
 Reproductive hormones –
these interactions break down)
testosterone and estrogen for
secondary sex characteristics

IV. Proteins
 Amino Acids – monomers of proteins

 Quaternary – formed between the  Functional unit is nucleotide

interaction of 2 or more [phosphate group bonds (covalent)
polypeptide units and can be to deoxyribose at carbon 5,
globular or fibrous deoxyribose is also bonded to 1
nitrogenous base]
 P-group of another nucleotide
connects to carbon 3, making the
sugar-phosphate backbone of DNA
and sequence of the bases which
are now codes [P-group is now
bonded to two sugars (3’5’
phosphodiester bonds)]
 Complementary base pairs are
present on the other strand which
 creates a hydrogen bond between
the bases (2 bonds between AT and
3 bonds between GC)
 The complementary strands are
antiparallel in that the 5' > 3'
direction of one strand runs
counter to the 5' > 3' direction of
the other strand.
 The nucleotide strands coil to form
a double-stranded helix
note: some DNA are non-coding, some makes genes that aren’t
activated, and some makes genes that code for active protein

V. Nucleic Acids – organic living substance found

in cells that can either be a DNA or RNA polymer
made up of nucleotides as monomers (basic unit)
 • Nucleotides – has 3 basic parts
 Pentose sugar – deoxyribose (no O
on carbon 2) for DNA and ribose
(OH in carbon 2) for RNA
 Nitrogenous bases
> Purine (2 rings) – sugar ring will
attach to nitrogenous base at 9th
position
> Pyrimidine (1 ring) - sugar ring
will attach to nitrogenous base at
1st position

 Nucleoside (sugar and base only)

 Phosphate group (PO-34)
 • DNA (deoxyribonucleic acid)
- determines the structure and
sequence of amino acids
- store genetic information

 • RNA (ribonucleic acid) single stranded  Naming nucleosides/tides

 functional unit is nucleotide (P-
group attached to carbon 5 of
 ribose, that is also attached to a
nitrogenous base) and also forms
3’5’ phosphodiester bonds
 nitrogenous base – AU and GC
 3 types – messenger RNA,
ribosomal RNA, and transfer RNA
 • Protein Synthesis (1st level of protein structure)
 Transcription – RNA polymerase
binds complementary RNA bases
to DNA template strand in nucleus
to create mRNA based on DNA
sequence  mRNA goes out of
nucleus and attach to ribosome;
rRNA is a component of ribosome
 Translation – tRNA brings amino
acids based on the anticodon tRNA
has and finds the complementary
bases on mRNA by reading it by 3  AMP
(codon)  tRNA leaves the (adenine+ribose+monophosphate)
ribosome and leave the amino acid  ADP
behind which bond with other (adenine+ribose+diphosphate)
amino acids.  ATP
(adenine+ribose+triphosphate)

- close proximity of 3 (-) charged

P-groups are unstable, thus, stores
high amount of PE
- when phosphate is released
(hydrolysis) small amount of
energy is released, ATP > ADP
- chemical reactions like
catabolism of glucose or other
nutrient release energy to
synthesize ADP > ATP
- when ATP is produced, it is used
for functions that require energy
like anabolism or propel cell
function (muscle contraction);
ATP > ADP
Chapter 3: Cell Biology
 Introduction to Cells

I. Cell Theory
1. All living organisms are made up of cells
2. Cell is the basic structural and functional unit of life
3. All cells arise from pre-existing cells

Important Cell Milestones

II. Parts and Functions of the Cell

Note: Cell size and shape vary depending on their functions

 • Plasma Membrane/Cell Membrane

 Transparent fluid barrier that separates the cell from its environment
 Semi-permeable/selectively permeable - allows only specific substances or molecules to enter
the cell
 Lipid-soluble/non-polar molecules can easily pass while polar molecules cannot
 ECF (extracellular fluid) - high levels of sodium - low levels of potassium
 ICF (intracellular fluid) - high levels of potassium - low levels of sodium

Fluid-Mosaic Model - represents the biological structure of a plasma membrane along its components
that determine its fluid-like nature

Plasma Membrane/Cell Membrane

> Transparent fluid barrier that separates the cell from its environment
> Semi-permeable/selectively permeable - allows only specific substances or molecules to enter the cell
> Lipid-soluble/non-polar molecules can easily pass while polar molecules cannot
> ECF (extracellular fluid) - high levels of sodium - low level of potassium + calcium a + chloride ions
> ICF (intracellular fluid) - high levels of potassium - low levels of sodium +enzymes +proteins
+glycogen + potassium ions
Fluid-Mosaic Model - represents the biological structure of a plasma membrane along its components
that determine its fluid-like nature

Membrane Lipids
> Polar heads oriented to face the ICF and ECF > Nonpolar

Phospholipid
> Hydrophilic, polar head (phosphate group + R (choline)

> Hydrophobic, non-polar tail composed of two fatty acids (saturated and unsaturated)

Cholesterol
> Maintains fluidity of the phospholipid bilayer:

1) preventing it to solidify in low temperatures by pushing them apart and 2) preventing it to be

too fluid in high temperatures by holding the phospholipids together.

Fluid-mosaic model
> Explains that the plasma membrane is fluid-like (like a dense liquid) and is neither static nor
rigid
 > Flexible, thus, can change shape and composition through time

Membrane Proteins and their Functions

> Integral proteins - proteins that are embedded within the phospholipid bilayer

> Peripheral proteins - proteins that attach to either the inner or outer surfaces of the bilayer > Surface
proteins - proteins that lies on inner or outer cell surface

Marker Molecules
Helps the cell recognize other cells (Carbohydrate)

Glycoprotein - carbohydrate attached to protein

Glycolipids - carbohydrates attached to lipid

Ex. 1. sperm cell recognizing oocyte 2. white blood cells recognizing foreign invaders
(distinguishing bacteria from donor cells)

Attachment Proteins

○ Cadherins
> Proteins that attach to the protein of another cell

○ Integrins
> Proteins that attach with other molecules from inside and outside the cell

Transport Proteins
> Integral proteins that extend from each side of the membrane (act as a passageway of
substances)

Three common characteristics: a) Specificity - substances can only enter through a protein
specific to the substance b) Competition - substances with the same shape bind to a common
protein (substances in higher concentration are transported at a faster rate) c Saturation -
substances that get transported are limited by the number of transport proteins.

○ Channel Proteins
> solutes don't bind to channel proteins

■ Leak Ion Channels

A Passive Transport Protein

> always open for transport of specific substances

■ Gated Ion Channels

● Ligand Gated Ion Channel

> Ligand (chemical signal) binds with the protein receptor to open

● Voltage-Gated Ion Channel

> Gates open in response to change in membrane potential
 ○ Carrier Proteins
> Proteins bind to protein receptors which triggers a conformational change

■ Uniport
> Carries one specific substance at a time

■ Symport
Cotransport

> Transports two different substances together in the same direction

■ Antiport
Counter-transport

> transports one substance to a different side, then transport a different

substance back to the first side

○ ATP-Powered Pumps
> Have 2 binding sites

> One for the ion to be transported and one for ATP which will release energy to fuel
the transport

Receptor Proteins
> Proteins with exposed specific receptors wherein chemical signals (or other substances) bind
to initiate a response

> can be membrane proteins or glycoproteins

○ Receptor Linked to Channel Proteins

> channel proteins have an exposed receptor wherein chemical signals bind to change

○ Receptors Linked to G Protein Complexes

> the receptor site of a protein binds with a chemical signal which causes the G
protein complex to bind to the protein.

> the guanosine diphosphate from the a-subunit of the complex will then be replaced
with guanosine triphosphate (activation)

> the g-complex leaves the protein and the a-subunit will then dissociate from the
complex to be used for cell

Enzymes
> are integral proteins that catalyze chemical reactions from the inner or outer surface of the cell

> are either always active or activated by G protein complexes

Movement Through the Plasma Membrane

Passive Membrane Transport

> does not require energy (substance moves along the concentration gradient which allows
substances to move from high to low concentration)

> collisions from concentrated area creates energy

○ Diffusion
> movement (high-to-low concentration) of lipid-soluble substances directly through
the phospholipid bilayer to the opposite side of the membrane

> small polar molecules can diffuse (ex. water)

> water diffusion is called osmosis

○ Osmosis
> movement of water from high to low concentration (requires aquaporins)

■ Tonicity
> behavior of cells when placed in a solution (shrink or expand and burst)

> 3 types of solutions

● Hypotonic
> hypo[less]+tonic[solute]

> less solute, thus more water

> cell has more solute and less water

> water moves from solution to cell (expand and burst)

● Hypertonic
> hyper[high]+tonic[solute]

> more solute, thus, less water

> cell has less solute and more water

> water moves from cell to solution (shrink)

● Isotonic
> concentration of solute and solvent is the same throughout the sides,
thus, no net movement (no gradient)

○ Facilitated Diffusion
> movement of large lipid-insoluble (hydrophilic, polar) substances across the
membrane through the help of transmembrane proteins

> specificity, competition, and saturation

Active Membrane Transport

> requires energy (ATP) for substances to move against the gradient or from low to high
concentration
 ○ Active Transport
> transport of inorganic or ionic substances through ATP-powered pumps (require
energy) from high to low concentration or vice versa

> ex.: In the ECF, Na is higher and K is lower which means in ICF, Na is lower and K
is higher. In a sodium-potassium pump, K moves to ICF (low to high) and Na moves to
ECF (low to high)

> from ICF, sodium attaches to ATP pump, when ATP binds to pump and breaks
down, it undergoes a conformational change which pumps sodium to ECF

> K attaches to the pump from ECF, when phosphate is released, it goes back to its
original shape, thus, releasing the K to ICF

note: for every ATP, Na moves to ECF and K moves from ECF back to ICF

○ Secondary Active Transport

> movement of organic or ionic substances (glucose and Na) along and against the
concentration gradient

> ex.: when Na accumulates in the ECF, it moves down to its gradient which creates
energy for Glucose to move inside the cell (against the gradient)

Vesicular Transport
> transport of large substances across the membrane > requires ATP

○ Endocytosis
> moves substances from outside to inside the cell

■ Phagocytosis
> phago (to eat) > cell-eating > ex.: macrophage (a wbc) finds a streptococcus
(a bacterium) > strep attaches to macro receptors > macro extends pseudopods
across the strep to envelope > vesicle is formed then separated from the
membrane (phagosome) > phagosome meets lysosome > lysosome digests
phago with its digestive enzymes > leftovers are expelled

note: phagocyte is an immune cell

■ Pinocytosis
> cell drinking > membrane engulfs random molecules and fluid from ICF
and delivers it deep into the cytosol where it is released

■ Receptor-Mediated Endocytosis
> are special receptors that carry specific into the cell to increase cell uptake
on these specific substances

> ex. LDL (low-density lipoprotein) receptor is found in clathrin-coated pits in

the cell membrane > LDL bind to the receptors > pseudopods form then
clathrins link up around it and gets released back to the membrane when
vesicle separates from the membrane > endosome engulfs the vesicle and
 separated LDL from the receptor > 2 vesicles form for LDL and receptor >
LDL goes to the lysosome for digestion > receptor goes back to membrane

> when LDL receptor is low, cholesterol uptake of the cell is low thus, cells
produce more cholesterol inside (hypercholesterolemia) when cholesterol
accumulates it blocks blood vessels (Atherosclerosis) which causes heart
attack or stroke

○ Exocytosis
> ICF substances expelled out of the cell

○ > ex.: Golgi apparatus packs proteins, lipids, and hormones from the endoplasmic
reticulum through a vesicle > vesicle is transported through cytoskeleton to the
membrane > vesicular membrane fuse with cell membrane > vesicular contents rupture
to the ECF

Cell Junctions
> cells need to connect and communicate with each other through different types of junctions

Tight Junctions
> holds cell very tightly where waters and ions can't pass through with the help of proteins

> ex. bladder, intestine, stomach, kidney, etc.

Desmosomes
> connects cell through cadherins (proteins) that extends to the cytoskeleton

> waters and ions can pass through for flexibility and reduced pressure

> skin, heart muscle, and intestine

Gap Junctions
> creates a connection between cells (connexon) for intercellular communication (ions and
molecules pass through or spread action potential)
Plasma Membrane/Cell Membrane

> Transparent fluid barrier that separates the cell from its environment > Semi-permeable/selectively
permeable - allows only specific substances or molecules to enter the cell > Lipid-soluble/non-polar
molecules can easily pass while polar molecules cannot > ECF (extracellular fluid) - high levels of
sodium - low level of potassium + calcium a + chloride ions > ICF (intracellular fluid) - high levels of
potassium - low levels of sodium +enzymes +proteins +glycogen + potassium ions Fluid-Mosaic Model -
represents the biological structure of a plasma membrane along its components that determine its fluid-
like nature

Membrane Lipids
> Polar heads oriented to face the ICF and ECF > Nonpolar

Phospholipid
> Hydrophilic, polar head (phosphate group + R (choline) > Hydrophobic, non-polar tail
composed of two fatty acids (saturated and unsaturated)

Cholesterol
> Maintains fluidity of the phospholipid bilayer: 1) preventing it to solidify in low temperatures by
pushing them apart and 2) preventing it to be too fluid in high temperatures by holding the
phospholipids together.
 Fluid-mosaic model
> Explains that the plasma membrane is fluid-like (like a dense liquid) and is neither static nor
rigid > Flexible, thus, can change shape and composition through time

Membrane Proteins and their Functions

> Integral proteins - proteins that are embedded within the phospholipid bilayer > Peripheral proteins -
proteins that attach to either the inner or outer surfaces of the bilayer > Surface proteins - proteins that lies
on inner or outer cell surface

Marker Molecules
Helps the cell recognize other cells (Carbohydrate) Glycoprotein - carbohydrate attached to
protein Glycolipids - carbohydrates attached to lipid Ex. 1. sperm cell recognizing oocyte 2.
white blood cells recognizing foreign invaders (distinguishing bacteria from donor cells)

Attachment Proteins

○ Cadherins
> Proteins that attach to the protein of another cell

○ Integrins
> Proteins that attach with other molecules from inside and outside the cell

Transport Proteins
> Integral proteins that extend from each side of the membrane (act as a passageway of
substances) Three common characteristics: a) Specificity - substances can only enter through a
protein specific to the substance b) Competition - substances with the same shape bind to a
common protein (substances in higher concentration are transported at a faster rate) c) Saturation -
substances that get transported are limited by the number of transport proteins.

○ Channel Proteins
> solutes don't bind to channel proteins

■ Leak Ion Channels

A Passive Transport Protein > always open for transport of specific substances

■ Gated Ion Channels

● Ligand Gated Ion Channel

> Ligand (chemical signal) binds with the protein receptor to open

● Voltage-Gated Ion Channel

> Gates open in response to change in membrane potential

○ Carrier Proteins
> Proteins bind to protein receptor which triggers conformational change

■ Uniport
> Carries one specific substance at a time
 ■ Symport
Cotransport > Transports two different substances together in the same
direction

■ Antiport
Counter-transport > transports one substance to a different side, then transport a
different substance back to the first side

○ ATP-Powered Pumps
> Have 2 binding sites > One for the ion to be transported and one for ATP which will
release energy to fuel the transport

Receptor Proteins
> Proteins with exposed specific receptors wherein chemical signals (or other substances) bind to
initiate a response > can be membrane proteins or glycoproteins

○ Receptor Linked to Channel Proteins

> channel proteins have an exposed receptor wherein chemical signals bind to change

○ Receptors Linked to G Protein Complexes

> the receptor site of a protein binds with a chemical signal which causes the G protein
complex to bind to the protein. > the guanosine diphosphate from the a subunit of the
complex will then be replaced with guanosine triphosphate (activation) > the g-complex
leaves the protein and the a subunit will then dissociate from the complex to be used for
cell

Enzymes
> are integral proteins that catalyze chemical reactions from the inner or outer surface of the cell >
are either always active or activated by G protein complexes

Movement Through the Plasma Membrane

Passive Membrane Transport

> does not require energy (substance moves along the concentration gradient which allows
substances to move from high to low concentration) > collisions from concentrated area creates
energy

○ Diffusion
> movement (high-to-low concentration) of lipid-soluble substances directly through the
phospholipid bilayer to the opposite side of the membrane > small polar molecules can
diffuse (ex. water) > water diffusion is called osmosis

○ Osmosis
> movement of water from high to low concentration (requires aquaporins)

■ Tonicity
> behavior of cells when placed in a solution (shrink or expand and burst) > 3
types of solutions

● Hypotonic
> hypo[less]+tonic[solute] > less solute, thus more water > cell has more
 solute and less water > water moves from solution to cell (expand and
burst)

● Hypertonic
> hyper[high]+tonic[solute] > more solute, thus, less water > cell has
less solute and more water > water moves from cell to solution (shrink)

● Isotonic
> concentration of solute and solvent is the same throughout the sides,
thus, no net movement (no gradient)

○ Facilitated Diffusion
> movement of large lipid-insoluble (hydrophilic, polar) substances across the
membrane through the help of transmembrane proteins > specificity, competition, and
saturation

Active Membrane Transport

> requires energy (ATP) for substances to move against the gradient or from low to high
concentration

○ Active Transport
> transport of inorganic or ionic substances through ATP-powered pumps (require
energy) from high to low concentration or vice versa > ex.: In the ECF, Na is higher and
K is lower which means in ICF, Na is lower and K is higher. In a sodium-potassium
pump, K moves to ICF (low to high) and Na moves to ECF (low to high) > from ICF,
sodium attaches to ATP pump, when ATP binds to pump and breaks down, it undergoes
a conformational change which pumps sodium to ECF > K attaches to the pump from
ECF, when phosphate is released, it goes back to its original shape, thus, releasing the K
to ICF note: for every ATP, Na moves to ECF and K moves from ECF back to ICF

○ Secondary Active Transport

> movement of organic or ionic substances (glucose and Na) along and against the
concentration gradient > ex.: when Na accumulates in the ECF, it moves down to its
gradient which creates energy for Glucose to move inside the cell (against the gradient)

Vesicular Transport
> transport of large substances across the membrane > requires ATP

○ Endocytosis
> moves substances from outside to inside the cell

■ Phagocytosis
> phago (to eat) > cell-eating > ex.: macrophage (a wbc) finds a streptococcus (a
bacterium) > strep attaches to macro receptors > macro extends pseudopods
across the strep to envelope > vesicle is formed then separated from the
membrane (phagosome) > phagosome meets lysosome > lysosome digests phago
with its digestive enzymes > leftovers are expelled note: phagocyte is an
immune cell
 ■ Pinocytosis
> cell drinking > membrane engulfs random molecules and fluid from ICF and
delivers it deep into the cytosol where it is released

■ Receptor-Mediated Endocytosis
> are special receptors that carry specific into the cell to increse cell uptake on
these specific substances > ex. LDL (low-density lipoprotein) receptor is found
in clathrin-coated pits in the cell membrane > LDL bind to the receptors >
pseudopods form then clathrins link up around it and gets released back to the
membrane when vesicle separates from the membrane > endosome engulfs the
vesicle and separated LDL from the receptor > 2 vesicles form for LDL and
receptor > LDL goes to lysosome for digestion > receptor goes back to
membrane > when LDL receptor is low, cholesterol uptake of cell is low thus,
cells produce more cholesterol inside (hypercholesterolemia) when cholesterol
accumulates it blocks blood vessels (Atherosclerosis) which causes heart attack
or stroke

○ Exocytosis
> ICF substances expelled out of the cell > ex.: Golgi apparatus packs proteins, lipids,
and hormones from the endoplasmic reticulum through a vesicle > vesicle is transported
through cytoskeleton to the membrane > vesicular membrane fuse with cell membrane >
vesicular contents rupture to the ECF

Cell Junctions
> cells need to connect and communicate with each other through different types of junctions

Tight Junctions
> holds cell very tightly where waters and ions can't pass through with the help of proteins > ex.
bladder, intestine, stomach, kidney, etc.

Desmosomes
> connects cell through cadherins (proteins) that extends to the cytoskeleton > waters and ions can
pass through for flexibility and reduced pressure > skin, heart muscle, and intestine

Gap Junctions
> creates a connection between cells (connexon) for intercellular communication (ions and
molecules pass through or spread action potential)