ANATOMY AND PHYSIOLOGY

BS PSYCHOLOGY 3
1st Semester | A.Y. 2023-2024

INTRODUCTION TO ANATOMY AND PHYSIOLOGY 2. Phylogeny – study of development of a

group/race.
Zoology – Study of animals, their behavior, their
physiology and evolution, as well as their interactions with 3. Evolution – origin and differentiation of animal
each other and with their environment. life.
4. Economic Zoology – study of the economic
BRANCHES OF ZOOLOGY value of animals.
A. Structural Zoology
1. Morphology – study of animal form and G. Medical Zoology
structure 1. Parasitology – study of parasites.
2. Anatomy – study of the different structures of 2. Pathology – study of abnormal structures and
an organism. nature and symptoms.
Ex. Digestive system of a frog.
3. Histology – study of tissues SUBDIVISIONS OF PHYSIOLOGY
Ex:
*skeletal muscle – not interconnected A. According to type of organism involved
cardiac muscle – interconnected. 1. Animal Physiology
2. Plant Physiology
B. Developmental Zoology
1. Embryology – study of the growth and B. According to the organizational level
development of fertilized egg. 1. Molecular Physiology
2. Ontogeny – study of the development of an 2. Cellular Physiology
individual.
3. Genetics – study of heredity and variation. C. According to specific or systemic function
1. Neurophysiology
C. Functional Zoology 2. Respiratory physiology
1. Animal Physiology – study of living process or 3. Cardiovascular physiology
function of an animal.
2. Ethology – study of animal behavior in ATTRIBUTES OF LIFE CONSIDERED MOST
response to stimulus. IMPORTANT IN HUMANS

D. Systematic Zoology/Taxonomy 1. Responsiveness

1. Protozoology – study of one celled organism.
2. Entomology – study of insects.
3. Conchology – study of shells.
4. Malacology – study of mollusks, soft bodied
organism.
5. Ichthyology – study of fishes.
6. Herpetology – study of reptiles.
7. Ornithology – study of birds.
8. Mammalogy – study of mammals.
9. Helminthology – study of worms.
10. Apiculture – study of honeybees.
11. Anthropology – study of man.
12. Carcinology - study of crustaceans.
● Or irritability
● Permits an organism to sense, monitor, and
respond to changes in its external
environment.
● Example: Withdrawing from a painful stimulus,
such as a pinprick.
2. Conductivity
● Capacity of living cells and tissues to
selectively transmit or propagate a wave of
excitation from one point to another within the
body.
● Highly developed in nerve and muscle cells.

3. Growth
E. Distributional Zoology ● Occurs as a result of a normal increase in size
1. Zoogeography – distribution of animals on earth or number of cells.
surface. ● It produces an increase in size of the individual,
2. Ecology – relationship between organisms with
or of a particular organ or part.
their environment.
4. Respiration
F. Historical Zoology
1. Paleontology – study of fossils and past life.
 ● Involves process that result in the absorption, movement muscles, posture, heat
transport, utilization, or exchange if tendons production
respiratory gases between an organism and its
Communicati Nervous Brain, Control and
environment. on, control, spinal cord, regulation of
● The exchange of gases may occur between the and nerves, other
blood and individual body cells (internal integration sensory systems,
respiration) or between the blood and air in the organs sensation,
lungs (external respiration). memory

Communicati Endocrine Pituitary Control and

5. Digestion on, control, glands, regulation of
● Process by which complex food products are and adrenals, other
broken down into simpler substances that can integration pancreas, systems.
be absorbed and used by individual cells. thyroid,
parathyroid
6. Absorption
Transportatio Cardiovascular Heart, Exchange
● The movement of digested nutrients through
n and arteries, and transport
the wall of the digesting tube and into the body defense veins, of materials
fluids for transport to cells for use. capillaries

7. Secretion Transportatio Lymphatic Lymph Immunity,

● Production and delivery of specialized n and nodes, fluid balance.
defense
substances, such as digestive juices and
hormones for diverse body functions. Respiration, Respiratory Lungs, Gas
● Happens inside the body. nutrition, and bronchial exchange,
excretion tree, acid-base
8. Excretion trachea, balance.
● Removal of waste products produced during larynx,
nasal cavity
body functions, including the breakdown and use
of nutrients in the cell. Respiration, Digestive Stomach, Breakdown
● Happens outside the body. nutrition, and small and and
excretion large absorption of
9. Circulation intestines, nutrients,
● Movement of body fluids and many other esophagus, elimination of
liver, wastes
substances, such as nutrients, hormones, and mouth,
waste products, from one body area to another. pancreas

10. Reproduction Respiration, Urinary Kidneys, Excretion of

● Formation of a new individual and also the nutrition, and ureter, wastes, fluid
formation of new cells in the body to permit excretion bladder, and
urethra electrolyte
growth, wound repair and replacement of dead or
balance, acid-
aging cells on a regular basis. base balance.
● Example: Cytokinesis
Reproduction Reproductive Males: Reproduction,
and Testis, vas continuity of
DIFFERENT BODY SYSTEMS development deferens, genetic
prostate, information,
seminal nurturing of
Functional Body Principal Primary
vesicle, offspring
Category System Organs Functions
penis
Support and Integumentary Skin Protection,
movement temperature,
regulation, Females:
sensation Ovaries,
fallopian
Support and Skeletal Bones, Support, tube,
movement Ligaments protection, uterus,
movement, vagina,
mineral and breasts
fat storage,
blood
production

Support and Muscular Skeletal Movement,

 ● Oblique Plane

A plane that is any type of

angle other than horizontal
or vertical angle.

THE LANGUAGE OF ANATOMY

DIRECTIONAL TERMS
The purpose of understanding the language of anatomy is
to easily locate the body parts. Superior and Inferior

● Anatomical Planes ● Superior – Above; toward the head

● Directional Terms Ex: Skull
● Body Parts and Regions ● Inferior – Below; away from the head
● Subdivisions of Abdomen Ex: Floor

ANATOMICAL PLANES
Example:

Head is superior to the torso.

Torso is inferior to the head.

Heart is superior to the liver.

(Frontal Plane) Liver is inferior to the heart.

● Transverse Plane – Divides the body into lower and

upper portion.

● Frontal/Coronal Plane – Divides the body into front Anterior and Posterior
and back
✔ Frontal – Front ● Anterior – Front;
✔ Coronal – Back toward the front of the
body
● Sagittal Plane – Divides the body into left and right ● Posterior – Back;
portion. toward the back of the
Types of Sagittal Plane body
✔ Midsagittal Plane – Divides left and right equally.
✔ Parasagittal Plane – Divides left and right Example:
(Unequal)
Frontal lobe is anterior to the occipital lobe. ● Distal – Away from the origin
Distal – Distant
Occipital lobe is posterior to the frontal lobe.

Medial and Lateral

Example:
Midline – Imaginary vertical Ankle is proximal to the foot.
line down middle of body Knee is proximal to the
Midline – Middle ankle.
Hip is proximal to the knee.
● Medial – Toward the
midline
● Lateral – Toward the Knee is distal to the hip.
side of the body. Ankle is distal to the knee.
Foot is distal to the ankle.

Superficial and Deep

Example:
● Superficial – Closer to
Nose is medial to the eyes. the surface of the body.
Superficial – surface
Eyes are lateral to the nose.
● Deep – Away from the
surface of the body
Arms are lateral to the torso.

Torso is medial to the arms.

Example:

Skin is superficial to the ribs.

Ribs are superficial to the lungs.

Lungs are deep to the ribs.

Ribs are deep to the sky.

Ipsilateral and Contralateral Unilateral and Bilateral

● Unilateral – Involving one side of

● Ipsilateral – On the same side of
the body.
the body Uni – one
● Bilateral – Involving both sides of
“Ipsi” - Same
the body.
Bi – Two

● Contralateral – On opposite
sides of the body QUADRANTS OF ABDOMEN
“Contra” – Opposite

Proximal and Distal

● Proximal – Toward the

trunk; near the origin
Proximal – Proximity
 ✔ Urinary Bladder, Sigmoid Colon, Female
Reproductive Organ/Male Reproductive Organ

9. Left Iliac
✔ Descending colon, sigmoid colon

SUBDIVISIONS OF ABDOMEN

1. Right Hypochondriac
✔ Liver, Gallbladder, Right Kidney, Small Intestine

2. Epigastric Region
✔ Stomach, Liver, Pancreas, Duodenum, Spleen,
Adrenal Glands

3. Left Hypochondriac
✔ Spleen, Colon, Left Kidney, Pancreas

4. Right Lumbar
✔ Gallbladder, Liver, Right Colon

5. Umbilical Region
✔ Umbilicus (navel), Parts of the small intestine,
Duodenum

6. Left Lumbar
✔ Descending colon, Left Kidney

7. Right Iliac
✔ Appendix, Cecum

8. Hypogastric Region

BIOMOLECULES: INTRODUCTION
● Carbohydrates
● Protein
● Lipids
● Nucleic Acids
CARBOHYDRATES
Carbohydrates
● Biological molecules consisting of CARBON (C),
HYDROGEN (H), and OXYGEN (O) atoms.
● They serve as sources and storage of energy.
● Some serve as the backbone of other biological
molecules.
*Combining carbohydrates together always undergo
dehydration synthesis
*Glycocidic bond – bond of carbohydrates
THREE MAJOR GROUPS OF CARBOHYDRATES
1. Monosaccharides - *Saccharine – sweet
● Are the simplest units of carbohydrates and
the simplest form of sugar.
● They are the building blocks of more complex
carbohydrates such as disaccharides and
polysaccharides.
● Physically, they are usually colorless, can
dissolve in water, and have the appearance of a
crystal-like substance.
Examples of Monosaccharide:
● Glucose – Blood sugar; dextrose
Example: Molasse
● Fructose – Fruit sugar
Example: Cherries
*Not all fruits have fructose e.g. apple
● Galactose – Sugar in RNA
Example: Yogurt
✔ Ribose - sugar in RNA
✔ Deoxyribose – sugar in DNA
2. Disaccharides
● A carbohydrate which is formed when
monosaccharides (simple sugars) undergo a
dehydration synthesis reaction which involves
the elimination of a small molecule, such as
water, and the combination of two
monosaccharides.
Examples of Disaccharides:
● Sucrose - glucose and fructose; the common
table sugar; usually obtained from sugarcane and
sugar beets.
● Lactose - glucose and galactose; milk sugar
● Maltose - two glucose molecules, malt sugar; the
sugar in beer and apples
3. Polysaccharides
● Most carbohydrates found in nature occur as
polysaccharides, polymers of medium to high
molecular weight.
● Polysaccharides, also called glycans, differ from
each other in:
✔ identity of their recurring monosaccharide
units,
✔ lengths of their chains, in the types of bonds
linking the monosaccharide units, degree of
branching.
● Homopolysaccharides contain only a single
monomeric species whereas
heteropolysaccharides contain two or more
different kinds.
● Unlike proteins polysaccharides generally do
not have defined molecular weights. This is
because polysaccharides are not synthesized
from a template. Instead, there is no specific
stopping point for the enzymes involved in their
biosynthesis.
EXAMPLES OF CARBOHYDRATES
1. Starches
● Starch is a storage homopolysaccharide of D
glucose residues that is found in the
cytoplasm of plant cells. It is extensively
hydrated because it has many exposed hydroxyl
groups available to hydrogen-bond with water.
● Starches consist of two types of polymers called
amylose and amylopectin.
● Amylose is a linear polymer of D glucose residues
that all are connected via (a 1-4) linkages. The
molecular weights of amylose chains vary from a
few thousand to more than a million.
● Amylopectin is a branched polymer of D glucose
residues that can weigh up to 200 million Da. The
glycosidic linkages between D glucose residues
in amylopectin chains are also (a1-4).
2. Glycogen
 ● Glycogen is the main storage polysaccharide
occurring in animal cells. Its structure is very
similar to amylopectin.
● It is especially abundant in hepatocytes of the
liver where it may constitute as much as 7% of
the wet weight of the tissue. Slightly less
glycogen (about 2% by wet weight) is stored in
skeletal muscle cells.
● Glycogen molecules occur in large granules that
can be observed in the cytoplasm of cells by
electron microscopy. A single glycogen molecule
can weigh several million Da. Like amylopectin,
glycogen molecules have many nonreducing
ends at the ends of the branches, but only one
reducing end. The enzymes of glycogen
metabolism build up and break down glycogen to
glucose units at the nonreducing ends of the
molecule. Simultaneous reactions at the many
nonreducing ends speed up the metabolism of
the polysaccharide.
3. Cellulose
● Linear homopolysaccharide composed
exclusively of D glucose units held together in
(B1-4) linkages. A single chain of cellulose can
contain 10-to-15,000 residues. They are insoluble
in water and form tough fibers.
● Cellulose is found in the cell walls of plants,
particularly in stalks, stems, trunks, and the
woody portions of the plant bod. Cellulose
constitutes much of the mass of wood, and
cotton is almost pure cellulose.
● Vertebrate animals lack hydrolvtic enzymes
(cellulases) that can cleave the (B1-4) linkages
between glucose units in cellulose. These
enzymes are produced by many cellulolytic
microorganisms. These microorganisms, such
as Trichonympha, a symbiotic protist that
resides in the termite gut allow the host to
derive energy from the glucose units stored in
cellulose Similarly cellulases produced by
microorganisms living in the rumens of cattle,
sheep, and goats allow these animals to obtain
energy, from cellulose present in soft grasses
in the diet.
4. Chitin
● Chitin is a linear homopolysaccharide
composed of N-acetylglucosamine residues in
(B1-+4) linkage. The only chemical difference
from cellulose is the replacement of the
hydroxyl group at C-2 with an acetylated
amino group.
● It also forms extended fibers similar to those
of cellulose. Like cellulase, chitin cannot be
digested by enzymes found in vertebrates.
● Chitin is the principal component of the hard
exoskeletons of nearly a million species of
arthropods- insects, lobsters, and crabs, for
example-and is probably the second most
abundant polysaccharide in nature.
LIPIDS (BIOLOGICAL ROLES & BUILDING BLOCKS)
● Substances composed of the element Carbon,
Hydrogen, and Oxygen with less oxygen than
carbohydrates.
● The larger content of hydrogen allows a greater
degree of oxidation.
*For lipids, the process involved is oxidation/reduction
reaction
Oxidation – Addition/acceptance of electrons (becomes
negatively charged)
Reduction – Removal/donation of electrons (becomes
positively charged)
*Ester bond – Putting lipids together.
BIOLOGICAL ROLES OF LIPIDS
1. They serve as the highest energy-giving foods in
the body.
*Gives more energy than carbohydrates
2. They act as insulators by protecting animals from
extreme cold.
*Animals have additional insulators e.g. polar
bears
3. They serve as a constituent of the protoplasm of
living cells.
*Everything we find within the cell
Cytoplasm – outside the nucleus
Karyoplasm – within the nucleus
4. In the form of phospholipids, they form a part of the
structure of the cell membrane.
*Cell membrane – cell transport
5. They serve as a building block of many steroids.
BUILDING BLOCKS OF LIPIDS
1. Fatty acids – are long-chain hydrocarbons with a
carboxyl group at one end.
✔ Fatty acids are attached to the glycerol molecule
by ester bonds. The number of fatty acids
attached to the glycerol molecule determines the
type of lipid.
Example:
● If there are three fatty acids attached, the lipid
is called a triglyceride.
● Two fatty acids attached; the lipid is called a
diglyceride.
● If there is one fatty acid attached, the lipid is
called a monoglyceride.
2. Glycerol – is a 3-carbon compound with a hydroxyl
group attached to each carbon. Example:
✔ Act as the backbone of the lipid molecule. Sphingomyelin – helps maintain the right shape of
the lungs of the fetus.

KINDS OF LIPIDS 4. Waxes

1. Phospholipids (or phosphoglycerides)
● Are the most common form of lipids.
● They are important members of the plasma
membrane as well as other biological
membranes.
*Phospholipids – Important part of the cell
membrane
Cell membrane  Hydrophobic – Regulation
Hydrophilic – Water can easily
pass the heads
Examples:
● Lecithin - found in egg yolk, brain, yeast, and
liver. It acts as an emulsifier.
*Emulsifier – breaks down fat into smaller
molecules.
● Cephalin – also found in brain tissue.
● Are composed of long-chain fatty acids linked to
chain glycerol.
● They are used as lubricants, polishers, and
ointments.
● They also serve to protect the surfaces of some
leaves and fruits.
● Example: Banana leaves, Gabi leaves, Apples
Cuticle – Protective layer; it contains cutin, a
waxy substance.
*Phospholipids, glyceride, sphingolipids, waxes are
saponifiable
5. Terpenes
● Do not contain fatty acids but they are considered
as lipids because they are insoluble in water.
*Non-saponifiable – insoluble in water

2. Glycerides Examples:
● Commonly found in nuts, meat, and milk. ● Chlorophyll – the green pigment in plants which
● They may be liquid (oil), or solid (lard, butter, is needed in photosynthesis.
margarine). ● Carotene – an orange pigment found in some
● Oils are composed of unsaturated fatty acids. plants.
● It can be saturated and unsaturated ● Vitamins A, E, and K – are fat-soluble vitamins.
● Coenzyme Q – involved in cellular respiration.
Unsaturated – Mostly solids
✔ Double bonds – hydrogen and carbon 6. Steroids
✔ Contain carbons in the fatty acids. ● Like terpenes, they have no fatty acids but are
✔ Foods rich in unsaturated fatty acid also considered lipids.
o Solids are composed of unsaturated fatty *In sports field, steroids are controversial, it is also
acids. non-saponifiable
o Avocado
o Salmon Examples:
o Mackerel ● Cholesterol - helps regulate the fluidity in cell
o Tuna membranes and therefore aids in the transport of
o Canola oil materials.
● Bile salt - is an emulsifier in the digestive system.
Saturated – Liquids It breaks fat into smaller globules thus hastening
✔ It can easily bend because of the absence of digestion.
some hydrogen. ● Sex hormones like estrogen and androgens.
✔ Can easily break through spaces/easier to
digest.
✔ Food rich in saturated acids PROTEINS
o Red meat
o Butter Proteins
o Cream ● The most abundant organic compounds in living
o Mayonnaise cells.
o Skin on poultry, such as chicken and duck ● They are the fundamental constituents of the
o Hot chips (fries) protoplasm of the cell.
o Palm oil ● They are made up of carbon, hydrogen, oxygen and
o Ice-cream nitrogen.
● Building blocks is amino acids
3. Sphingolipids
● Are found in the brain, lungs, and nerve tissue.
 PARTS OF AN AMINO ACID 5. Albumin – for osmotic regulation
Example:
1. Central Carbon Atom ● Serum Albumin – maintains osmotic
2. Amino Group (NH2) concentration of blood
3. Carboxyl Group (COOH)
4. Hydroxyl Atom (OH) 6. Repressor – for regulation of gene action
5. Radical Group – nagbabago; to distinguish the Examples:
differences in the types of amino acids (like each type Lac Repressor – regulates transcription
of amino acids has different radical group?) *Regulation of proteins that are responsible for
lactose
*Central carbon atom, amino group, carboxyl group
and hydroxyl group are permanent parts of amino 7. Hormones – for regulation of body functions
acid. These are all reactive and usually donate Examples:
hydrogen. ● Insulin – controls blood glucose levels
● Vasopressin - increase water retention by kidney
● Oxytocin – regulates milk production
BIOLOGICAL ROLES OF PROTEINS
8. Globins – for the transport throughout the body
1. Proteins are essential in building and repairing Examples:
body cells and tissues. ● Hemoglobin – transports oxygen and carbon
dioxide in blood
2. All enzymes are proteins, and they aid in speeding ● Myoglobin – transports oxygen and carbon
up almost all chemical reactions in the body.
dioxide in muscles
3. Proteins bring about individual differences. We all
9. Ion-Binding - for storage
look different because each of us is made up of
Examples:
different proteins.
● Ferritin – stores iron, especially in spleen
*We are made up of 21 occurring amino acids.
● Casein – stores in iron in milk
4. Proteins serve as transport molecules, reserve
food, and provide protection as antibodies. 10. Muscle – for contraction
Example:
CLASSIFICATION OF PROTEINS ● Myosin and Actin - for contraction of muscle
fibers
1. Fibers – for structure 11. Immunoglobulins – for defense
Examples: Example:
● Collagen – in cartilage ● Antibodies – mark foreign proteins for
● Keratin - in hair and color elimination
● Fibrin – for blood clotting.
12. Toxins – for defense
2. Enzymes – for metabolism Example:
Examples: ● Snake venom – blocks nerve function
● Amylase – cleaves starch/breakdown
polysaccharide into disaccharide.
● Proteases – breakdown of proteins STRUCTURE OF PROTEINS
● Polymerases – produces nucleic acids
● Lipases – breakdown of lipids ● Primary Structure
● A string of amino acids connected by peptide
3. Channels – for membrane transport / do not change bonds between the amino group and the
structure carboxyl group.
Examples:
● Protein Pump – Chemiosmosis (proton of ● Secondary Structure
hydrogen) ● Brought about by hydrogen bonds (result of
● Sodium Potassium Pump – for excitable hydrogen bonding).
membranes (skeletal muscle and cardiac muscle)
● Tertiary Structure
4. Cell Surface Antigens – for cell recognition (to ● Brought about by interactions among the R
identify bacteria from?) groups.
Example:
● ABO Blood – identify red blood cell ● Quaternary Structure
 ● Brought about by interaction between  Pyrimidines: cytosine (C), thymine (T) and Uracil
polypeptides. (U)

Pentose Sugars
 There are two related pentose sugars:
PROTEIN DENATURATION
 RNA contains ribose.
Protein Denaturation  DNA contains deoxyribose.
● The destruction of the quaternary tertiary structure of • The sugars have their carbon atoms numbered with
proteins. primes to distinguish them from the nitrogen bases.
There are two related pentose sugars:

Examples of Protein Denaturation:

● Frying of boiling of an egg PRIMARY STRUCTURE OF NUCLEIC ACIDS
● Ironing or curling of your hair.
● Alcohol cuts to denature proteins in bacteria.  The primary structure of a nucleic acid is the
nucleotide sequence.
● Cooking food to denature proteins in bacteria
 The nucleotides in nucleic acids are joined by
phosphodiester bonds.
 The 3’-OH group of the sugar in one nucleotide
NUCLEIC ACIDS
forms an ester bond to the phosphate group on the
5’-carbon of the sugar of the next nucleotide.
Nucleic Acids
 Nucleic acids are molecules that store information
for cellular growth and reproduction.
 There are two types of nucleic acids:
 Deoxyribonucleic acid (DNA) and ribonucleic
acid (RNA).
 These are polymers consisting of long chains of
monomers called nucleotides.
 A nucleotide consists of a nitrogenous base, a
pentose sugar and a phosphate group:

Example of RNA Primary Structure

 In RNA, A, C, G and U are linked by 3’ -5’ ester bonds
between ribose and phosphate.

Nitrogen Bases
 The nitrogen bases in nucleotides consist of two
general types:
 Purines: adenine (A) and guanine (G)
  The pentose sugar in RNA is ribose, in DNA it's
deoxyribose
 In RNA, uracil replaces the base thymine (U pairs
with A)
 RNA is single stranded while DNA is double
Example of DNA Primary Structure stranded.
 In DNA, A, C, G and T are linked by 3’ -5’ ester bonds
 RNA molecules are much smaller than DNA
between deoxyribose and phosphate.
molecules.
 There are three main types of RNA:
 ribosomal (rRNA), messenger (mRNA) and
transfer (tRNA)

TYPES OF RNA
Type Abbreviation Percentage Functions
Ribosomal rRNA 75 Major component of
the cell
Messenge mRNA 5-10 Carries information
r for protein synthesis
from the DNA in the
nucleus to the
ribosomes
Transfer RNA 10-15 Brings amino acids
to the ribosomes for
protein synthesis

SECONDARY STRUCTURE: DNA DOUBLE HELIX *Ribosomes are the sites of

proteins: It is made up of
 In DNA, there are two strands of nucleotides that small subunit and large
wind together in a double helix. subunit
 The strands run in opposite directions
 The bases are arranged in step-like pairs
 The base pairs are held together by hydrogen
bonding Example of
 The pairing of the bases from the two strands is very Transfer RNA
specific.
 The complementary base pairs are A-T and G-C
 Two hydrogen bonds form between A and T
 Three hydrogen bonds form between G and C FIVE DIFFERENCES BETWEEN RNA AND DNA
 Each pair consists of a purine and a pyrimidine,
so they are the same width, keeping the two 1. Sugar in RNA is ribose instead of deoxyribose.
strands at equal distances from each other. 2. RNA is single stranded.
3. RNA contains Uracil instead of Thymine.
Base Pairing in the DNA Helix 4. RNA is disposable.
5. RNA can be outside the nucleus, DNA can’t.

If you are going from DNA to RNA - what nitrogenous

base would pair with Adenine?
DNA: C A G T T A
RNA: G U C A A U

THE CENTRAL DOGMA

Replication  Transcription  Translation

DNA REPLICATION
RIBONUCLEIC ACID (RNA)
 DNA replication involves several processes:
 RNA is much more abundant than DNA.  First, the DNA must uncoil and be unwound,
 There are several important differences between separating the two strands.
RNA and DNA:
  The single strands then act as templates for
synthesis of the new strands, which are
complementary in sequence.
 Bases are added one at a time until two new
DNA strands that exactly duplicate the original
DNA are produced.
 The process is called semi-conservative replication
because one strand of each daughter DNA comes
from the parent DNA and one strand is new.
 The energy for the synthesis comes from hydrolysis
of phosphate groups as the phosphodiester bonds
form between the bases.
Semi-conservative
DNA Replication
 During transcription, RNA polymerase moves along the
DNA template in the 3’-5’direction to synthesize the
corresponding mRNA.
 The mRNA is released at the termination point.
Processing of mRNA
 Genes in the DNA of eukaryotes contain exons that
code for proteins along with introns that do not.
 Because the initial mRNA, called a pre-RNA, includes
the noncoding introns, it must be processed before it
can be read by the tRNA.
 While the mRNA is still in the nucleus, the introns are
removed from the pre-RNA.
 The exons that remain are joined to form the mRNA that
leaves the nucleus with the information for the synthesis
of protein.

Removing Introns from mRNA

Direction of DNA Replication

 The enzyme helicase unwinds several sections of
parent DNA.
 At each open DNA section, called a replication fork,
DNA polymerase catalyzes the formation of 5-
3'ester bonds of the leading strand.
 The lagging strand, which grows in the 3'-5' direction,
is synthesized in short sections called Okazaki
fragments. Regulation of Transcription
 The Okazaki fragments are joined by DNA ligase to  A specific mRNA is synthesized when the cell
give a single 3'-5' DNA strand. requires a particular protein.
 The synthesis is regulated at the transcription level:
 Feedback control, where the end products speed
up or slow the synthesis of mRNA.
 Enzyme induction, where a high level of a reactant
induces the transcription process to provide the
necessary enzymes for that reactant.

Regulation of Prokaryotic Transcription

 In prokaryotes (bacteria and archaebacteria),
transcription of proteins is regulated by an operon,
which is a DNA sequence preceding the gene sequence.
TRANSCRIPTION  The lactose operon consists of a control site and the
genes that produce mRNA for lactose enzymes.
 Several steps occur during transcription:
 A section of DNA containing the gene unwinds.
 One strand of DNA is copied starting at the
initiation point, which has the sequence TATAAA.
 An mRNA is synthesized using complementary
base pairing with uracil (U) replacing thymine (T)
 The newly formed mRNA moves out of the nucleus
to ribosomes in the cytoplasm and the DNA re-winds
Lactose Operon and Repressor
RNA Polymerase
 When there is no lactose in the cell, a regulatory gene
produces a repressor protein that prevents the
synthesis of lactose enzymes.
 The repressor turns off mRNA synthesis.

Lactose Operon and Inducer

 When lactose is present in the cell, some lactose
combines with the repressor, which removes the
repressor from the control site.
 Without the repressor, RNA polymerase catalyzes the
synthesis of the enzymes by the genes in the operon.
 The level of lactose in the cell induces the synthesis of
the enzymes required for its metabolism.

TRANSLATION

 A ribosome attaches to the mRNA molecule.

*AUG is the initiation point, initiation codon, signals the starts

of the translations
 percent of the membrane, with the remainder being
proteins.
 While lipids help to give membranes their flexibility,
proteins monitor and maintain the cell's chemical
climate and assist in the transfer of molecules across
the membrane.

MEMBRANE TRANSPORT

 One of the great wonders of the cell membrane is its

ability to regulate the concentration of substances
inside the cell.
 These substances include ions such as Ca 2+, Na+, K+,
and Cl–; nutrients including sugars, fatty acids, and
amino acids; and waste products, particularly carbon
dioxide (CO2), which must leave the cell.

PASSIVE TRANSPORT

 Does not require the cell to expend energy.

 Substances move from an area of higher
concentration to an area of lower concentration,
CELL MEMBRANE AND TRANSPORT
down the concentration gradient and energetically
favorable.
Cell Membrane
 Depending on the chemical nature of the substance,
 The cell membrane (plasma membrane) is a thin
different process may be associated with passive
semi-permeable membrane that surrounds
transport.
the cytoplasm of a cell.
 Its function is to protect the integrity of the interior
TYPES OF PASSIVE TRANSPORT
of the cell by allowing certain substances into the
cell while keeping other substances out.
Diffusion
 It also serves as a base of attachment for
 A passive process of transport.
the cytoskeleton in some organisms and the cell
 A single substance tends to move from an area of
wall in others. Thus, the cell membrane also serves to
high concentration to an area of low
help support the cell and help maintain its shape.
concentration until the concentration is equal
 Another function of the membrane is to regulate cell
across a space.
growth through the balance of endocytosis and
exocytosis.
 In endocytosis, lipids and proteins are removed
from the cell membrane as substances are
internalized.
 In exocytosis, vesicles containing lipids and
proteins fuse with the cell membrane increasing
cell size.
 The cell membrane is primarily composed of a mix of
proteins and lipids.
 Depending on the membrane’s location and role in the Facilitated Transport
body, lipids can make up anywhere from 20 to 80
 Materials diffuse across the plasma membrane
with the help of membrane proteins.
 A concentration gradient exists that allows these
materials to diffuse into or out of the cell without
expending cellular energy.
 The integral proteins involved in facilitated transport
are collectively referred to as transport proteins, and
they function as either channels for the material or
carriers.
 Another type of protein embedded in the plasma
membrane is a carrier protein. This aptly named
protein binds a substance and, in doing so, triggers a
change of its own shape, moving the bound molecule
from the outside of the cell to its interior.
 Carrier proteins play an important role in the function
of kidneys.
 Glucose, water, salts, ions, and amino acids needed
by the body are filtered in one part of the kidney. This
filtrate, which includes glucose, is then reabsorbed in
another part of the kidney with the help of carrier
proteins.
 Because there are only a finite number of carrier
proteins for glucose, if more glucose is present in the
filtrate than the proteins can handle, the excess is not
re-absorbed and it is excreted from the body in the
urine. In a diabetic individual, this is described as
“spilling glucose into the urine.”
Osmosis
 Osmosis is the movement of water through a
semipermeable membrane according to the
concentration gradient of water across the membrane,
which is inversely proportional to the concentration of
solutes.
 While diffusion transports material across membranes
and within cells, osmosis transports only
water across a membrane and the membrane limits
the diffusion of solutes in the water.
 The aquaporins that facilitate water movement play a
large role in
osmosis, most
prominently in red
blood cells and the
membranes of
kidney tubules.
Osmolarity
 Osmolarity describes the total solute
concentration of the solution.
 A solution with low osmolarity has a greater
number of water molecules relative to the number
of solute particles; a solution with high osmolarity
has fewer water molecules with respect to solute
particles.
 Three terms—hypotonic, isotonic, and
hypertonic—are used to relate the osmolarity of
a cell to the osmolarity of the extracellular fluid
that contains the cells.
1. Hypotonic Solution
Extracellular fluid has lower osmolarity than the
fluid inside the cell, and water enters the cell.
It also means that the extracellular fluid has a
higher concentration of water in the solution
than does the cell. In this situation, water will
follow its concentration gradient and enter the
cell.
2. Hypertonic Solution
As for a hypertonic solution, the extracellular
fluid having a higher osmolarity than the cell’s
cytoplasm.
Therefore, the fluid contains less water than
the cell does. Because the cell has a relatively
higher concentration of water, water will leave
the cell.
3. Isotonic Solution
The extracellular fluid has the same osmolarity as
the cell. If the osmolarity of the cell matches that
of the extracellular fluid, there will be no net
movement of water into or out of the cell, although
water will still move in and out.
ACTIVE TRANSPORT
 Requires the use of the cell’s energy, usually in the
form of adenosine triphosphate (ATP)
 If a substance must move into the cell against its
concentration gradient—that is, if the concentration of the
substance inside the cell is greater than its concentration
in the extracellular fluid (and vice versa)—the cell must
use energy to move the substance.
 Some active transport mechanisms move small-
molecular weight materials, such as ions, through the
membrane. Other mechanisms transport much larger
molecules.
Two mechanisms exist for the transport of small-
molecular weight material and small molecules:

1. Primary active transport moves ions across a

membrane and creates a difference in charge across that
membrane, which is directly dependent on ATP.

2. Secondary active transport describes the movement of

material that is due to the electrochemical gradient
established by primary active transport that does not
directly require ATP.

Carrier Proteins for Active Transport

1. A uniporter carries one specific ion or molecule.
2. A symporter carries two different ions or molecules,
both in the same direction.
3. An antiporter also carries two different ions or
molecules, but in different directions. All of these
transporters can also transport small, uncharged
organic molecules like glucose.

Some examples of pumps for active transport are

 Na+-K+ ATPase, which carries sodium and
potassium ions,
 H+-K+ ATPase, which carries hydrogen and
potassium ions.
*Both of these are antiporter carrier proteins.

Two other carrier proteins are:

 Ca2+ ATPase and H+ ATPase, which carry only
calcium and only hydrogen ions, respectively. Both
are pumps.

One of the most important pumps in animal cells is the

sodium-potassium pump (Na+-K+ ATPase), which
maintains the electrochemical gradient (and the correct
concentrations of Na+ and K+) in living cells.
 The sodium-potassium pump moves K+ into the cell
while moving Na+ out at the same time, at a ratio of
three Na+ for every two K+ ions moved in.