Dr.

Venky’s Exam Oriented Physiology

Dr. Venky’s
Exam Oriented Physiology

Paper I

Dr. R. Venkatesan M.D

Associate Professor,
Department of Physiology,
Government Medical College,
Pudukkottai, Tamil Nadu, India.

For bulk or retail purchase: Contact Phone no. 7010003512, 7402277812 or

Mail to: arvees99@yahoo.co.in
 Dr. Venky’s Exam Oriented Physiology
Sample Five or 4 Mark answers:
1. Hemolytic disease of the newborn or Rh
incompatibility:
When an Rh-ve mother carries an Rh+ve fetus, the
first child usually escapes from hemolytic disease
because the mixing of the mother’s and fetal blood
normally occurs only during the time of delivery
and only after this mixing the mother would
produce anti Rh antibodies against the fetal Rh
antigen, so the first child escapes. Anti-Rh
antibodies develop slowly after mixing, reaching
the maximum concentration in about 2 to 4
months. Mixing of 0.5 ml of Rh+ve blood with
Rh-ve blood is enough to stimulate antibody
formation.
Now once again if the same mother (sensitized
mother) becomes pregnant with another Rh+ve
fetus, anti Rh antibodies (IgG) which were already
formed in the mother after the birth of the first
child would cross the placenta and attack the
Rh+ve fetal RBCs causing agglutination and
hemolysis. This disease is called hemolytic disease
of the newborn.
Severity of the disease increases with each
subsequent pregnancy.
Let us suppose that an Rh-ve mother was
transfused with an Rh+ve blood before she became
pregnant, i.e. she is already sensitized. Now even
the first fetus would be affected by hemolysis if
that fetus is Rh+ve because mother’s blood would
already have formed anti Rh antibodies against
those transfused Rh+ve RBCs. So an Rh–ve
woman must never be transfused with an Rh+ve
blood if she wants to have children in the future.
Clinical features:
The antigen antibody reaction and subsequent
hemolysis is responsible for various manifestations
of Rh incompatibility.
1. Erythroblastosis foetalis:
Anti Rh antibodies attack Rh positive Fetal Red
Blood Cells

Agglutination and hemolysis of the fetal RBCs
cause anemia;

The hematopoietic tissue of the infant tries to
replace the hemolysed RBCs rapidly

Many early nucleated forms of red blood cells
(erythroblasts), are released from the baby’s bone
marrow into blood,

Erythroblastosis foetalis
The severe anemia caused by hemolysis is
usually the cause of death.
2. Hydrops foetalis: (Hydrops=>water)
Hydrops foetalis is nothing but accumulation of
fluid or edema, in at least two fetal compartments.
It can occur in any of pleural space, pericardial
space, peritoneal space, scalp and subcutaneous
tissue.
Severe anemia due to hemolysis leads to poor
oxygen delivery to tissues. So to improve oxygen
delivery heart would pump excessively, finally
leading to heart failure and edema. Edema is one
of the features of heart failure.
3. Icterus gravis Neonatorum (Icterus=> Jaundice;
gravis=>during pregnancy;
Neonatorum=>neonate)
Lysis of red blood cells releases hemoglobin into
the blood, fetal macrophages convert the
hemoglobin into bilirubin, which causes jaundice
seen at birth. If jaundice is not present at birth, it
develops very quickly within 24 hours
4. Kernicterus:
Many children who escape death exhibit
permanent mental impairment or damage to motor
areas of the brain, particularly basal ganglia,
because of precipitation of bilirubin in the
neuronal cells and their subsequent destruction, a
condition called kernicterus.
 Dr. Venky’s Exam Oriented Physiology
Management: Treatment & Prevention
Treatment:
Exchange transfusion:
Mother’s anti Rh antibodies continue to be present
in the neonate for upto 1 to 2 months after birth, so
they will keep on destroying neonate’s Rh positive
RBCs during that time, so replacing the neonate’s
Rh positive blood with Rh negative blood prevents
agglutination. This replacement is called Exchange
transfusion.
About 400 milliliters of Rh-negative blood is
infused over a period of 90 minutes or more, while
at the same time the neonate’s own Rh-positive
blood is being removed.
This procedure may need to be repeated several
times during the first few weeks of life, mainly to
prevent hemolysis and to keep the bilirubin level
low, thereby preventing kernicterus.
By the time these transfused Rh-negative cells are
replaced with the infant’s own Rh-positive cells
from its bone marrow, a process that requires 6 or
more weeks, the anti- Rh antibodies that had come
from the mother will have been destroyed.
Prevention:
An anti-D antibody is administered to the
expectant Rh-ve mother, starting at 28 to 30 weeks
of gestation.
The anti-D antibody is also administered to Rh-
negative women who deliver Rh-positive babies
within 72 hours after delivery to prevent
sensitization of the mothers to the D antigen.
This greatly reduces the risk of developing large
amounts of antibodies against D antigen during
the second pregnancy.
The anti-D antibody destroys the Rh positive fetal
RBCs which enter the mother during delivery and
thereby inhibits antigen-induced B lymphocyte
antibody production in the mother.
2. Physiology of vomiting
Definition:
Vomiting is a process by which the upper
gastrointestinal tract removes its contents when
any part of the upper GI tract becomes excessively
irritated, over distended, or even over excitable.
This happens by means of reverse peristalsis.
Antiperistalsis, the Prelude to Vomiting:
Antiperistalsis means peristalsis toward oral
direction. Excessive gastrointestinal irritation or
overdistention provide an especially strong
stimulus for vomiting and stimulates
antiperistalsis many minutes before vomiting
appears.
This begins in the ileum and pushes small
intestinal contents all the way back to the
duodenum and stomach within 3 to 5 minutes at a
rate of 2 to 3 cm/sec. Then, as these upper portions
of the gastrointestinal tract, especially the
duodenum, become overly distended, this
distention becomes the exciting factor that initiates
the actual vomiting act.
Vomiting centers:
The vomiting center consists of various scattered
groups of neurons in the reticular formation of
the medulla that controls the different components
of the vomiting act.
Afferents:
Impulses are relayed from the mucosa of upper
GIT to the medulla through visceral afferent
pathways in the sympathetic nerves and vagi.
Efferents:
Motor impulses that cause the actual vomiting are
transmitted from the vomiting center through 5th,
7th, 9th, 10th, and 12th cranial nerves to the upper
gastrointestinal tract, through vagal and
sympathetic nerves to the lower gastrointestinal
tract, and through spinal nerves to the diaphragm
and abdominal muscles.
 Dr. Venky’s Exam Oriented Physiology
Chemoreceptor trigger zone:
Chemoreceptor trigger zone is a small area made
up of chemoreceptors, located bilaterally on the
floor of the fourth ventricle. This area lies in area
postrema, a V-shaped band of tissue on the lateral
walls of the fourth ventricle near the obex. This
structure is one of the circumventricular organs
and is not protected by the blood–brain barrier.
Electrical stimulation of this area and
administration of certain drugs, including
apomorphine, morphine, and some digitalis
derivatives, can directly stimulate this
chemoreceptor trigger zone and initiate vomiting.
Act of Vomiting:
Once the vomiting center has been sufficiently
stimulated and the vomiting act has started, the
following sequence of events takes place:
A deep breath

Raising of the hyoid bone, larynx pulls and opens
the upper esophageal sphincter

Closing of the glottis occurs to prevent vomitus to
flow into the lungs
 d). Small amounts of ATP are required for
Lifting of the soft palate closes the posterior nares
 muscle fiber membrane to maintain appropriate
Strong downward contraction of the diaphragm
along with contraction of abdominal wall muscles
squeezes stomach and increases intragastric
pressure
 4 millimolar, this amount can support contraction
The lower esophageal sphincter relaxes
completely, allowing expulsion of the gastric
contents upward through the esophagus.
Mechanism of motion sickness:
Rapidly changing direction or changing rhythm of
motion of the body stimulate receptors in the
vestibular labyrinth of the inner ear, and from here
impulses are transmitted mainly to the brain stem
vestibular nuclei which in turn transmits the
impulses into the cerebellum.CTZ then receives
information from the cerebellum and finally sends
it to the vomiting center to cause vomiting.
Pathway:
Vestibular labyrinth → Brain stem vestibular
nuclei→ Cerebellum→ CTZ→ Vomiting centers.
3. Energy source for muscle contraction
ATP is the immediate source of energy for skeletal
muscle contraction. ATP is hydrolyzed to ADP &
inorganic phosphate with release of about 7.3 kcal
of energy.
Functions of ATP:
a). Most of the ATP is required for cross-bridge
movement during muscle contractions.
b). Binding of ATP to myosin breaks the actin-
myosin interactions and allows cross-bridge cycle
to continue.
c). ATP provides energy to SERCA to transport
calcium ions back into sarcoplasmic reticulum &
also provides energy to Calcium ATPase pump
which pumps Ca2+ back into ECF and thereby
initiates relaxation.
pumping sodium and potassium ions through the
ionic environment for propagation of muscle fiber
action potentials.
Sources of ATP:
There is very little storage of ATP in muscle-about
for only 1 to 2 seconds at most. When contraction
begins, energy is provided by the following three
sources depending upon the duration of muscular
activity.
a). Phosphocreatine
b). Glycolysis
c). Oxidative phosphorylation
a). Phosphocreatine:
 Dr. Venky’s Exam Oriented Physiology
Phosphocreatine is the first source of energy that is
used to from ATP. It carries a high-energy
phosphate bond similar to the bonds of ATP but
the phosphate bond of phosphocreatine has a
slightly higher amount of free energy than that of
each ATP bond.
The combined energy of both the stored ATP and
the phosphocreatine in the muscle is capable of
causing maximal muscle contraction for only 5 to 8
seconds. Ex. activities like 100m sprint, jumping,
weight lifting, diving etc.
Lohmann reaction:
Energy released during this reaction is used for
ATP synthesis.
CP + ADP ATP+C
During recovery period concentration of creatine
phosphate is restored back to normal level by the
reversal reaction. ATP is used to immediately form
ADP and CP
Resynthesis of creatine phosphate:
ATP+C CP+ADP
b). Glycolysis:
The second important source of energy, which is
used to reconstitute both ATP and
phosphocreatine, is “glycogenolysis” of glycogen
previously stored in the muscle cells. Rapid
enzymatic breakdown of the glycogen to pyruvic
acid and lactic acid liberates energy that is used to
convert ADP to ATP and also to re-form the stores
of phosphocreatine. This provides energy for
activities like 400m running, 100m swimming, etc.
Advantages of glycolysis:
1. The glycolytic reactions can occur even in the
absence of oxygen, so that muscle contraction can
occur even when oxygen delivery from the blood is
not available.
2. The rate of formation of ATP by glycolysis is
about 2.5 times as rapid as ATP formation in
oxidative metabolism.
Limitation of glycolysis:
So many end products of glycolysis accumulate in
muscle cells, therefore glycolysis loses its
capability to sustain maximum muscle contraction
after about 1minute.
c). Oxidative metabolism:
The third and final source of energy is oxidative
metabolism. This means combining oxygen with
the end products of glycolysis and with various
other cellular foodstuffs to liberate ATP. More
than 95 percent of all energy used by the muscles
for sustained, long term contraction is derived
from this source. Ex. marathon
For extremely long-term maximal muscle
activity—over a period of many hours—by far the
greatest proportion of energy comes from fats, but
for periods of 2 to 4 hours, as much as one half of
the energy can come from stored carbohydrates.
4. Vasa recta / Countercurrent exchanger
mechanism in kidney
The capillaries draining the tubules of the cortical
nephrons form a peritubular network, whereas the
efferent arterioles from the juxtamedullary
nephrons drain not only into a peritubular
network, but also into vessels that form hairpin
shaped loops called the vasa recta.
These vessels descend into the medulla in parallel
with the loops of Henle and then loop back along
with the loops of Henle and return to the cortex
before emptying into the venous system.
The descending vasa recta have a non-fenestrated
endothelium that contains a facilitated transporter
for urea, and the ascending vasa recta have a
fenestrated endothelium, consistent with their
function in conserving solutes.
Function:
Countercurrent multiplier (Loop of Henle) traps
solutes in the renal medulla and creates
hyperosmolarity in the renal medulla. This is
necessary for the production of concentrated urine.
Vasa recta preserves the hyperosmolarity of the
renal medullary interstitium, therefore it also
 Dr. Venky’s Exam Oriented Physiology
plays an important role in allowing the kidneys to
form concentrated urine.
Without vasa recta, the solutes trapped into the
renal medulla by the countercurrent multiplier
system would be rapidly dissipated.
Two special features of the renal medullary blood
flow contribute to the preservation of the high
solute concentrations:
1. Low medullary blood flow:
The medullary blood flow is low, accounting for
less than 5 per cent of the total renal blood flow.
This sluggish blood flow is sufficient to supply the
metabolic needs of the tissues but helps to
minimize solute washout from the medullary
interstitium.
2. The vasa recta serve as countercurrent
exchangers:
The vasa recta serve as countercurrent exchangers,
by doing so they minimize washout of solutes
from the medullary interstitium
Mechanism of operation of vasa recta as
countercurrent exchangers:
The vasa recta, like other capillaries, are highly
permeable to solutes in the blood, except for the
plasma proteins.
Descending limb of vasa recta:
As blood descends in the descending limb toward
the papillae, it becomes progressively more
concentrated, due to two events:
1). Solutes enter the vasa recta from the renal
medullary interstitium and
2). Water leaves from the vasa recta and enters the
interstitium.
By the time the blood reaches the tips of the vasa
recta, it has a concentration of about 1200
mOsm/L, the same as that of the medullary
interstitium.
Ascending limb of vasa recta:
As blood ascends back in the ascending limb
toward the cortex, it becomes progressively less
concentrated due to two events:
1). Solutes diffuse back out into the medullary
interstitium from vasa recta and
2). Water moves from the interstitium into the vasa
recta.
This sequence of events maintains the
hyperosmolarity of the renal medullary
interstitium constant, thereby helping the kidney
to produce concentrated urine.
5. Leptin
Several hormones are known to be derived from
the adipose tissue, since they are cytokines they are
commonly termed as adipokines. Known
adipokines include leptin, adiponectin, and
resistin. The trophoblast cells and amnion cells also
secrete leptin and moderate amounts of this satiety
hormone enter the maternal circulation. Some also
enter the amniotic fluid. Its function in pregnancy
is not known.
Functions of Leptin:
Leptin has a variety of roles ranging from food
intake to puberty. Effects of leptin include:
1). Leptin and regulation of food intake:
Leptin and ghrelin are peripheral factors that are
critical regulators of food intake, they act in a
reciprocal manner to each other. Both activate their
receptors in the hypothalamus that initate
 Dr. Venky’s Exam Oriented Physiology

signaling pathways leading to changes in food Experimental evidence:

intake.
Leptin is a satiety-producing hormone secreted by
fat cells. Leptin produced by the adipose tissue
signals the status of the fat stores in the body. As
adipocytes increase in size, they release greater
quantities of leptin and this tends to decrease food
intake, partly by increasing the expression of other
anorexigenic factors in the hypothalamus such as
pro-opiomelanocortin (POMC), cocaine- and
amphetamine regulated transcript (CART),
neurotensin, and corticotrophin releasing hormone
(CRH).
2). Leptin and diabetes:
Deficient sensing of leptin in the cells of the
hypothalamus that regulate satiety is one of the
causes of hyperphagia in diabetes. The feeding
area of the hypothalamus is not inhibited and thus
satiety is not sensed, so food intake is increased.
Leptin also decreases insulin resistance.
sa). Obese ob/ob mice that cannot make leptin are
infertile, and their fertility is restored by injections
of leptin.
b). Leptin treatment also induces precocious
puberty in immature female mice.
5). Leptin and Bone mass:
Intracerebroventricular administration of leptin
has been shown to decrease bone formation. This
finding is consistent with observations that obesity
protects against bone loss and that most obese
humans are resistant to the effects of leptin on
appetite. Thus, there may be neuroendocrine
regulation of bone mass via leptin.
6). Metabolic rate:
Leptin also stimulates the metabolic rate.

3). Leptin and body weight:

Body weight generally increases at a slow but

steady rate throughout adult life. Decreased
physical activity is undoubtedly a factor in this
increase, but decreased sensitivity to leptin may
also play a role.

4). Leptin and puberty:

A critical body weight must normally be reached

for puberty to occur. Thus, for example, young
women who engage in strenuous athletics lose
weight and stop menstruating, as do girls with
anorexia nervosa. If these girls start to eat and gain
weight, they menstruate again, that is, they “go
back through puberty.”

Leptin appears to be the link between body weight

and puberty. However, the way that leptin fits into
the overall control of puberty remains to be
determined.
 Dr. Venky’s Exam Oriented Physiology
Two Mark Or 3 Mark Answers:
1. Apoptosis/Cell suicide
Apoptosis is nothing but programmed cell death.
There are 100 trillion cells in the body. The total
number of cells is regulated not only by controlling
the rate of cell division but also by controlling the
rate of cell death. When cells are no longer needed
or become a threat to the organism, they undergo a
suicidal programmed cell death called apoptosis.
Mechanism:
Apoptosis is initiated by activation of a family of
proteases called caspases. These enzymes are
synthesized and stored in the cell as inactive
procaspases.
The mechanisms of activation of caspases are
complex, but once activated, the enzymes cleave
and activate other procaspases, triggering a
cascade that rapidly breaks down proteins within
the cell.
Activation of procaspases → Formation of active
caspases → Activates more Procaspases
Once specific proteolytic cascade is activated,
caspases cause the cell to shrink and condense,
disassemble the cytoskeleton, and alter the cell
surface. After these changes happen, a neighboring
phagocytic cell, such as a macrophage, can attach
to the cell membrane and digest the cell.
Necrosis:
In contrast to programmed death, cells that die as a
result of an acute injury usually swell and burst
due to loss of cell membrane integrity, a process
called cell necrosis.
Balance between apoptosis and new cell
formation:
Programmed cell death, is precisely balanced with
the formation of new cells in healthy adults. If
apoptosis is excessive the body’s tissues would
shrink, if is decreased the body’s tissues grow
excessively.
A tremendous amount of apoptosis occurs in
tissues that are being remodeled during
development. Even in adult humans, billions of
cells die each hour in tissues such as the intestine
and bone marrow and are replaced by new cells
2. Clot Retraction
Once a fibrin clot is formed, within another 5- 30
minutes the clot retracts to 40% of its original
volume releasing a fluid in the process. This fluid
expressed is called serum. It lacks fibrinogen and
other clotting factors because they are consumed
during clot formation, in this way, serum differs
from plasma. Therefore, serum cannot clot because
it lacks these factors.
Role of platelets:
Platelets are necessary for clot retraction to occur.
This is due to the contraction of thrombosthenin
protein, actin, and myosin molecules present in
the platelets which finally shortens the fibrin
threads. The contraction is activated and
accelerated by thrombin as well as by calcium ions
released from calcium stores in the mitochondria,
endoplasmic reticulum, and Golgi apparatus of the
platelets. So if platelet count decreases clot
retraction becomes poor.
As the clot retracts, the edges of the broken blood
vessel are pulled together, thus contributing still
further to the ultimate state of hemostasis.
Significance of clot retraction:
The significance of clot retraction is that the
retracted clot is more solid, elastic and stronger
and it plugs the hole in the vessel much better than
a non-retracted clot.
Furthermore, platelets entrapped in the clot
continue to release procoagulant substances, one of
the most important of which is fibrin-stabilizing
factor, which causes more and more cross-linking
bonds between adjacent fibrin fibers and stabilizes
the clot further.
 Dr. Venky’s Exam Oriented Physiology
3. Why can’t cardiac muscle be tetanized and
fatigued?
Cardiac muscle cannot be tetanized because:
The normal refractory period of the ventricle is
0.25 to 0.30 second, the refractory period of atrial
muscle is about 0.15 second.
Compared to skeletal muscles, cardiac muscle has
a prolonged refractory period. Therefore, more
than half of the contractile response is over during
absolute refractory period itself. This makes
summation impossible in cardiac muscle, hence
cardiac muscle cannot be tetanized.
Cardiac muscle does not become fatigued
because of the following factors:
1. The build-up of lactic acid plays a major role in
the development of muscle fatigue. This happens
during anaerobic metabolism. Heart normally
works almost under complete aerobic
metabolism with no accumulation of lactic acid.
However, under ischemic conditions, cardiac
muscle can also use anaerobic glycolysis for energy
which accounts for about a meagre 1% of
metabolism.
2. Rich blood supply of about 250 ml/min provides
heart with plentiful of nutrients and oxygen. So
cardiac muscle need not switch to anaerobic
metabolism to produce ATP.
3. Cardiac myocytes have plenty of mitochondria
when compared to skeletal muscle which
continuously produce ATP to supply energy for
contraction.
4. Under resting conditions, cardiac muscle
normally consumes fatty acids to supply most of
its energy instead of carbohydrates. About 70 per
cent of the energy is derived from fatty acids.
5. Cardiac myocytes have a large amount of
myoglobin which stores oxygen.
All these factors prevent the cardiac muscle from
becoming fatigued throughout its entire life time.
4. Role of ATP in muscle contraction and
relaxation
ATP is the immediate source of energy for skeletal
muscle contraction. ATP is hydrolyzed to ADP &
inorganic phosphate with release of energy - 7.3
kcal. This energy is used to carry out various
processes during muscle contraction and
relaxation.
Role of ATP in muscle contraction:
Before contraction begins, the heads of the cross
bridges bind with ATP. The ATPase activity of the
myosin head immediately cleaves the ATP but
leaves the cleavage products, ADP plus phosphate
ion, bound to the head.
This energy released is used to alter the position of
mysoin head in such a way that it becomes
perpendicular to the actin filament, but is not yet
attached to the actin.
Power stroke:
When a myosin heads binds to the active site of
actin, this attachment simultaneously causes
profound changes in the intramolecular forces
between the head and arm of its cross-bridge. The
new alignment of forces causes the head to tilt
toward the arm and to drag the actin filament
along with it. This tilt of the head is called the
power stroke.
The energy that activates the power stroke is the
energy already stored, like a “cocked” spring, by
the conformational change that occurred in the
head when the ATP molecule was cleaved earlier.
Thus the ATP provides energy to perform power
stroke during muscle contraction.
Role of ATP in relaxation:
Once the head of the cross-bridge tilts, this allows
release of the ADP and phosphate ion that were
previously attached to the head. At the site of
release of the ADP, a new molecule of ATP binds.
This binding of new ATP causes detachment of the
head from the actin.
Restoring calcium level in sarcoplasm:
 Dr. Venky’s Exam Oriented Physiology

After contraction is over, ATP is required to pump 1 liter of food. The food often becomes putridly
the calcium ions from the sarcoplasm into the infected during long periods of esophageal stasis.
sarcoplasmic reticulum via SERCA. The infection may also cause ulceration of the
esophageal mucosa, sometimes leading to severe
ATP is also used by calcium ATPase present in the
substernal pain or even rupture and death.
sarcolemma to pump calcium ions from
sarcoplasm to ECF so that the calcium level in Treatment:
sarcoplasm is brought back to precontraction state.
1. It can be treated by pneumatic dilation of the
5. Achalasia cardia sphincter by means of a balloon inflated at the end
of a swallowed esophageal tube.
Achalasia means failure to relax. Cardia refers to
2. Antispasmodic drugs which relax smooth
opening of the lower end of the esophagus into
muscles can also be helpful.
stomach. Achalasia Cardia is a pathological
3. Incision of the esophageal muscle (myotomy) is
condition in which food fails to pass from
also useful.
esophagus into stomach, therefore it accumulates
4. Inhibition of acetylcholine release by injection of
in the lower end of the esophagus resulting in
botulinum toxin into the LES is also effective and
massive dilatation.
this gives relief that lasts for several months.
Pathophysiology:

Achalasia Cardia is due to increased resting tone of

the smooth muscles of the lower esophageal
sphincter (LES) leading to their incomplete
relaxation during swallowing.

The basic underlying pathology is that the

myenteric plexus of the esophagus is deficient in
the lower two thirds of the esophagus and the
release of nitric oxide and vasoactive intestinal
peptide is defective. These are normally required
for relaxation of GI smooth muscle, hence their
deficiency leads to increased tone.

In other words, the myenteric plexus has lost its

ability to transmit a signal to cause “receptive
relaxation” of the lower esophageal sphincter as
food approaches this sphincter during swallowing.

Over months and years, the esophagus becomes

tremendously enlarged that it can hold as much as
 Dr. Venky’s Exam Oriented Physiology

VIVA Answers: 5. Catch up growth

In children, following illness or starvation, a period

1. Define Homeostasis of increased growth takes place during which the
growth rate is greater than normal. This
Maintenance of nearly constant conditions in the accelerated growth usually continues until the
internal environment of our body is called previous growth curve is reached, then slows to
homeostasis. The term homeostasis was coined by normal. This period of accelerated growth is called
American physiologist W.B. Cannon. as catchup growth. The mechanisms that bring
about and control catch-up growth are unknown.
Essentially all organs and tissues of the body
perform various physiological functions to
maintain this internal environment. For example,
the lungs provide oxygen to the extracellular fluid
to replenish the oxygen used by the cells, the
kidneys maintain constant ion concentrations, and
the gastrointestinal system provides nutrients etc.

2. How does a person with “A blood group” have

“antibodies against B antigens” and vice versa?.

Antigens very similar to A and B are common in

intestinal bacteria and possibly in foods to which
all newborn individuals are exposed. Therefore,
infants rapidly develop antibodies against those
antigens which are not present in their own red
blood cells.

Thus, type A blood group individuals develop

anti-B antibodies, type B individuals develop anti-
A antibodies, type O individuals develop both, and
type AB individuals develop no antibodies.

3. Fenn effect

When a muscle contracts, work is performed and

energy is required. Large amounts of ATP are
cleaved to release energy during the contraction
process; the greater the amount of work performed
by the muscle, the greater the amount of ATP that
is cleaved. This is called as the Fenn effect.

4. Wolff –Chaikoff effect

In normal individuals, administration of large

doses of iodide has an inhibitory effect on hormone
production. Iodide act directly on the thyroid
gland to produce a mild and transient inhibition of
organic binding of iodide, eventually resulting in
inhibition of thyroid hormone synthesis. This
inhibition is known as the Wolff –Chaikoff effect.
 Dr. Venky’s Exam Oriented Physiology

Essay Answers: a single type of membrane receptor. The second

messenger does the rest.
1. Second messenger system

Second messengers are molecules that relay signals

received at receptors on the cell surface or cytosol
or nucleus - such as the arrival of protein
hormones, growth factors, etc. - to target molecules
inside the cell. These are intracellular mediators.
This is one of the means by which hormones exert
their intracellular actions.

Many ligands in the ECF bind to receptors on the

surface of cells and trigger the release of
intracellular mediators such as cAMP, IP3, and
DAG which initiate changes in cell function.
Consequently, the extracellular ligands are called
“first messengers” and the intracellular mediators
are called “second messengers.”

Second messengers bring about many short-term

changes in cell function by altering enzyme
Stimulatory G protein (Gs):
function, triggering exocytosis, and so on, but they
also can lead to the alteration of transcription of Binding of the hormones with the receptor allows
various genes. coupling of the receptor to a G protein. If the G
protein stimulates the adenylyl cyclase–cAMP
There are four major second messenger systems:
system, it is called a Gs protein, denoting a
• Adenylyl Cyclase–cAMP Second stimulatory G protein.
Messenger System
Stimulation of membrane bound enzyme adenylyl
• The Cell Membrane Phospholipid cyclase, by the Gs protein then catalyzes the
Second Messenger System conversion of a small amount of cytoplasmic
adenosine triphosphate (ATP) into cAMP inside
• Calcium-Calmodulin Second Messenger the cell. This then activates cAMP-dependent
System
protein kinase, which phosphorylates specific
• Guanylyl Cyclase–cGMP Second proteins in the cell, triggering biochemical
Messenger System reactions that ultimately lead to the cell’s response
to the hormone.
Adenylyl Cyclase–cAMP Second Messenger
System: Inhibitory G protein (Gi):

One of the means by which hormones exert
intracellular actions is to stimulate formation of the
second messenger cyclic Adenosine Mono
Phosphate (cAMP) inside the cell membrane.
The cAMP then causes subsequent intracellular
effects of the hormone. Therefore, the only direct
effect that the hormone has on the cell is to activate
If binding of the hormone to its receptors is
coupled to an inhibitory G protein (denoted Gi
protein), adenylyl cyclase will be inhibited,
reducing the formation of cAMP and ultimately
leading to an inhibitory action in the cell.
Thus, depending on the coupling of the hormone
receptor to an inhibitory or a stimulatory G
protein, a hormone can either increase or decrease
 Dr. Venky’s Exam Oriented Physiology

the concentration of cAMP and phosphorylation of

key proteins inside the cell

Cascading effect:

Once cAMP is formed inside the cell, it usually

activates a cascade of enzymes.

First one enzyme is activated, which activates a

second enzyme, which activates a third, and so
forth. The importance of this mechanism is that
only a few molecules of activated adenylyl cyclase
immediately inside the cell membrane can cause
many more molecules of the next enzyme to be
activated, which can cause still more molecules of
the third enzyme to be activated, and so forth.
In this way, even the slightest amount of hormone
acting on the cell surface can initiate a powerful
cascading amplifying effect on the entire cell.
Diversity of functions:
Increases or decreases in cAMP produce different
functions in different target cells. This is due to the
presence of different set of enzyme systems in
different cells.
Ex. A thyroid cell stimulated by cAMP forms the
metabolic hormones thyroxine and
triiodothyronine, whereas the same cAMP in an
adrenocortical cell causes secretion of the
adrenocortical steroid hormones. In epithelial cells
of the renal tubules, cAMP increases their
permeability to water.
The cell membrane phospholipid second
messenger system:
Some hormones activate transmembrane receptors
that activate the enzyme phospholipase C attached
to the inside projections of the receptors.
This enzyme catalyzes the breakdown of some
phospholipids in the cell membrane, especially
phosphatidyl inositol biphosphate (PIP2), into
two different second messenger products: inositol
triphosphate (IP3) and diacylglycerol (DAG).
Inositol triphosphate - IP3:
The IP3 mobilizes calcium ions from mitochondria
and the endoplasmic reticulum, and the calcium
ions then have their own second messenger effects,
such as smooth muscle contraction and changes in
cell secretion.
Diacylglycerol:
DAG, the other lipid second messenger, activates
the enzyme protein kinase C (PKC), which then
phosphorylates a large number of proteins, leading
to the cell’s response.
Further, the lipid portion of DAG is arachidonic
acid which is the precursor for the prostaglandins
and other local hormones that cause multiple
effects in tissues throughout the body.
Calcium-Calmodulin second messenger system:
This second messenger system operates in
response to the entry of calcium into the cells.
Calcium entry may be initiated by:
(1) Changes in membrane potential that open
calcium channels (voltage gated channels) or
(2) A hormone interacting with membrane
receptors that open calcium channels (ligand gated
channels) or
(3). Stretch sensitive calcium channels
 Dr. Venky’s Exam Oriented Physiology
On entering a cell, calcium ions bind with the
protein calmodulin. This protein has four calcium
sites, and when three or four of these sites have
bound with calcium, the calmodulin changes its
shape and initiates multiple effects inside the cell,
including activation or inhibition of protein
kinases.
Activation of calmodulin-dependent protein
kinases causes, via phosphorylation, activation or
inhibition of proteins involved in the cell’s
response to the hormone. For example, one specific
function of calmodulin is to activate myosin
kinase, which acts directly on the myosin of
smooth muscle to cause smooth muscle
contraction.
Calcium concentration:
The normal calcium ion concentration in most cells
of the body is 10-8 to 10-7 mol/L, which is not
enough to activate the calmodulin system. But
when the calcium ion concentration rises to 10-6 to
10-5 mol/L, enough binding occurs to cause all the
intracellular actions of calmodulin.
This is almost exactly the same amount of change
in calcium ion concentration that is required in
skeletal muscle to activate troponin C, which
causes skeletal muscle contraction. Troponin C is
similar to calmodulin in both function and protein
structure.
Guanylyl Cyclase–cGMP Second Messenger
System:
Guanylyl cyclases are a family of enzymes that
catalyze the formation of cyclic guanosine
monophosphate (cyclic GMP or cGMP). They
exist in two forms:
One form has an extracellular amino terminal
domain that is a receptor, a single transmembrane
domain, and a cytoplasmic portion with guanylyl
cyclase catalytic activity. Several such guanylyl
cyclases have been characterized.
One form of guanylyl cyclase is soluble, contains
heme, and is not bound to the membrane. There
appear to be several isoforms of the intracellular
enzyme. They are activated by nitric oxide (NO)
and NO-containing compounds.
Physiological significance:
1. cGMP is important in vision in both rod and
cone cells.
2. cGMP-regulates ion channels, and
3. cGMP activates cGMP-dependent kinase,
producing a number of physiologic effects like
smooth muscle relaxation which brings about
penile erection.
4. Two forms of guanylyl cyclases acts as receptors
for atrial natriuretic peptide (ANP), and a third
form binds an Escherichia coli enterotoxin and the
gastrointestinal polypeptide guanylin.
 Dr. Venky’s Exam Oriented Physiology

2. Define anemia. Describe in detail the functioning bone marrow. Aplastic anemia and
classification and signs and symptoms. Elaborate anemia of chronic diseases are also due to
on iron deficiency anemia. hypoproliferative bone marrow.

Anemia is defined as a reduction in the oxygen 3. Hemolytic anemias:

carrying capacity of blood resulting in inadequate
Hemolytic anemias are due to destruction of RBCs.
O2 supply to tissues. This can be either due to
decreased red blood cells or deficient hemoglobin. They are of two causes, intracorpuscular and
extracorpuscular.
More accurately it is defined as a reduction in the
red cell mass. Intracorpuscular causes: They can be either
congenital or acquired.
Classification:
i) Congenital Abnormalities:
Functional or Etiological or Whitby’s
classification: a. Membrane defects:
Etiologically anemias can be classified into: * Hereditary spherocytosis
1. Hemorrhagic anemias * Hereditary elliptocytosis
2. Anemia due to decreased red cell production:
a. Dyshaemopoietic anemias b. Haemoglobinopathies:
b. Hypoproliferative anemias * Sickle cell anaemia
3. Hemolytic anemias * Thalaseemia
4. Dilutional anemia: Pregnancy, Oliguric renal c. Enzymopathies
failure and volume-overload. 1) Abnormal aerobic glycolysis e.g. G6PD
1. Hemorrhagic anemias: deficiency
2) Abnormal anerobic glycolysis e.g pyruvate
Acute loss of blood: Ex. Road traffic accident and kinase deficiency
Chronic loss of blood: Hook worm infestation, ii) Acquired Abnormalities
excessive menstrual blood loss, hemorrhoids, 1). Paroxysmal nocturnal haemoglobinuria
bleeding peptic ulcer. 2). Vitamin E deficiency

2. Anemia due to decreased red cell production: Extracorpuscular causes: The pathology lies
outside the RBC.
a. Dyshaemopoietic anaemia: There is decreased
Antigen antibody reactions
maturation of red blood cells due to deficiency of
Infection ex. malaria
maturation factors essential for erythropoiesis.
Drugs –quinine, aspirin
i). Mineral deficiency: Iron, zinc, Ni, Mn, copper, Poison – snake venom
Cobalt Hypersplenism
ii). Vitamin deficiency: B12, folic acid, vitamin C& Incompatible blood transfusion
pyridoxine Hemolytic disease of the newborn
iii). Hormonal deficiency: Anemia of renal
4. Dilutional anemia:
diseases, pituitary, thyroid or suprarenal
deficiency. In conditions such as pregnancy, oliguric renal
iv). Protein deficiency failure and volume-overload, plasma volume
increases compared to cellular components of
b. Hypoproliferative anaemia:
blood thereby diluting RBCs.
Hypoproliferative anemia is due to failure of bone
Morphological or Wintrobe’s classification:
marrow. Gamma rays, drugs such as cytotoxic and
sulpha drugs and X rays all damage the bone
marrow. Bone marrow aplasia means lack of
 Dr. Venky’s Exam Oriented Physiology
Anemias can be classified morphologically based
on the average size of the cells and the
hemoglobin concentration into:
1. Macrocytic anemia: Seen in deficiency of
Vitamin B12 and folic acid and pernicious anemia.
2. Normochromic, normocytic anemia: Seen in
acute blood loss, aplastic anemia and all hemolytic
anemias except thalassemia
3. Hypochromic, microcytic anemia: Iron
deficiency anemia and thalaseemia
Severity:
The severity of anemia depends upon the amount
of decrease in hemoglobin.
Mild anemia – Fall in Hb up to 8 gm/dL
Moderate – 8 to 5 gm/dL
Severe – below 5 gm/dL
If the rate of blood loss is more rapid, the
symptoms are also severe, especially in elderly. If
the hemoglobin falls slowly, then this allows time
for haemopoietic compensation with less
symptoms.
Clinical features: Symptoms:
1. Musculo skeletal: Easy fatigability, tiredness
and lassitude.
2. Cardiovascular System:
Angina, dyspnoea, palpitation and intermittent
claudication on exertion are seen. Heart failure
occurs in severe cases and when anemia is present
along with other organic cardiac diseases. Severe
anemia results in high output cardiac failure.
3. Neurological:
Dizziness, fainting, lack of concentration
Blurred or diminished vision
Headache, tinnitus
Paraesthesia in fingers and toes
Insomnia and
Irritability.
4. GIT: Dyspepsia and anorexia
5. Genital: Loss of libido & impotence, menstrual
abnormalities such as amenorrhea.
Signs:
Pallor of the skin and mucous membranes:
Mucous membranes, palms and nail beds look
pale. The colour of the skin is unreliable because it
depends upon the degree of skin pigmentation and
the amount of fluid in the subcutaneous tissues.
Peripheral edema:
Slight edema of the legs can be seen probably due
to increase in the capillary permeability secondary
to hypoxia. It is clearly evident in heart failure.
The cardiovascular system:
There is an increased velocity of blood flow with
decreased viscosity of the blood in addition to
capillary dilation.
Pulse: Tachycardia, bounding pulse
Cardiac examination:
In severe cases, loud heart sounds, S3 over mitral
or tricuspid area, haemic murmur which is an
ejection systolic murmur can all be heard. Haemic
murmur is heard all over the precordium. Jugular
venous pressure is raised.
Fundal changes:
Flame shaped retinal hemorrhages, exudates and
rarely papilloedema can be seen.
Kidney:
Proteinuria and impairment of the concentrating
power of kidneys occur due to anoxia of renal
tubules.
Fever:
Mild fever may occur in severe anemia but other
causes should be excluded.
Iron deficiency anemia:
Iron is the most important component of
hemoglobin, hence lack of iron leads to anemia.
Both RBC count and hemoglobin are lowered.
Iron deficiency anemia is the commonest cause of
anemia in India. This occurs when amount of iron
 Dr. Venky’s Exam Oriented Physiology
loss or physiological requirements exceed
absorption.
Causes of Iron deficiency anemia:
Decreased intake: Poor socioeconomic status,
infants on exclusive milk feed can get anemia
because milk is a poor source of iron.
Increased demand: During pregnancy mother has
to additionally support the fetus, particularly
during the third trimester. Iron is also diverted to
the placenta and the increased maternal red cell
mass. It is also lost with bleeding during child
birth. In infants and adolescents, rapid growth may
overwhelm dietary intake, and result in deficiency.
Increased loss from the body:
Acute loss of blood: Ex. Road traffic accident and
Chronic loss of RBCs: Hook worm infestation,
prolonged menstrual period or excessive loss of
blood during menstruation, hemorrhoids, occult
blood loss from esophagitis, bleeding peptic ulcer
and colorectal malignancy.
Defective utilization: Malabsorption syndromes
Characteristic features of iron deficiency:
Peripheral smear shows microcytic, hypochromic
anemia.
All the RBC indices namely, MCH, MVC and
MCHC are decreased below normal values. It also
shows poikilocytosis (variation in shape)
and anisocytosis (variation in size).
Bone marrow shows normoblastic hyperplasia
Other blood cells are normal.
Nails: Nails become, soft, brittle and spoon shaped
with longitudinal striations called koilonychia.
Tongue becomes inflamed.
Dietary requirement:
Daily requirement of iron for an adult Indian is 20
mg, out of which only about 1-2 mg is absorbed.
Maximum iron absorption is 3.5 mg/day.
Children between 13-15 years need 20-30 mg/day.
Pregnant women need 40 mg/day.
Only Fe2+ (ferrous) form (reduced form) is
absorbed, Fe3+ (ferric) form is not absorbed.
Sources of iron:
Jaggery is rich in iron, other sources include green
leafy vegetables, liver, pulses and cereals.
Management:
Investigations:
Plasma ferritin is a measure of iron stores in
tissues and is the single best test to confirm iron
deficiency. It is a very specific test; a subnormal
level is seen in iron deficiency.
Serum iron and total iron binding capacity
(TIBC) are measures of iron availability. Serum
iron level decreases while total iron binding
capacity increases.
Treatment:
Treatment is based on the severity of anemia. Mild
anemia is treated with oral iron supplements.
Ferrous sulphate 200 mg 3 times daily provides
195 mg of elemental iron per day. This is adequate
and should be continued for 3–6 months to restore
iron stores.
Non-complaint patients and patients with
malabsorption or chronic gut disease may need
parenteral iron therapy. Previously, iron dextran or
iron sucrose was used, but new preparations of
iron isomaltose and iron carboxymaltose have
fewer allergic effects and are preferred. Dosage is
individualized.
Severe anemia needs blood transfusion.
Reticulocyte response:
Reticulocyte response is nothing but an increase in
the reticulocyte count of a person who is treated
for anemia with iron or other supplements. This is
the first response to treatment to be noted in the
blood following nutritional supplements.
Reticulocytes increase by about 25 to 35 % above
normal in peripheral circulation due to excessive
proliferation and release of reticulocytes.
The response occurs within 4- 5 days after starting
treatment with iron. The peak response is seen
between days 7 to 10. It is a measure of the body’s
 Dr. Venky’s Exam Oriented Physiology
response to treatment. Reticulocyte response is
absent or minimal in aplastic anemia.
1. Describe in detail the mechanism of salivary
secretion. Elaborate on its composition,
regulation of secretion and functions.
The first secretion encountered when food is
ingested is saliva. Saliva is produced by three pairs
of salivary glands - the parotid, submandibular,
and sublingual glands - that drain into the oral
cavity.
Salivary secretion is a two-stage process: the first
stage involves the acini, and the second stage
involves the salivary ducts.
The acini secrete a primary secretion that contains
ptyalin and/or mucin and ions. This secretion does
not greatly differ from typical extracellular fluid
i.e. it is isotonic with plasma. As the primary
secretion flows through the ducts, two major active
transport processes take place that markedly
modify the ionic composition of the fluid in the
saliva.
a). Change in Na+, K+, Cl- ion concentrations :
Sodium ions are actively reabsorbed and
potassium ions are actively secreted in exchange
for the sodium in all the salivary ducts. Therefore,
the sodium ion concentration of the saliva becomes
greatly reduced, whereas the potassium ion
concentration becomes increased. However, there
is more sodium reabsorption compared to
potassium secretion, and this creates electrical
negativity of about -70 millivolts in the salivary
ducts; this in turn causes chloride ions to be
reabsorbed passively.
Therefore, the chloride ion concentration in the
salivary fluid falls to a very low level, matching the
ductal decrease in sodium ion concentration. The
ducts are relatively impermeable to water, so the
loss of NaCl renders the saliva hypotonic,
particularly at low secretion rates.
b). Change in Bicarbonate ion concentration:
Bicarbonate ions are secreted by the ductal
epithelium into the lumen of the duct. This is
partly caused by passive exchange of bicarbonate
for chloride ions, and partly from an active
secretory process.
Under resting conditions, the net result of these
transport processes is as follows:
*Concentrations of sodium ions in the saliva - 15
mEq/ L. [1/7th of concentration in plasma],
*Concentrations of chloride ions -15mEq/L [1/10th
of concentration in plasma],
*Concentration of potassium ions - 30 mEq/L. [7
times as great as plasma],
*Concentration of bicarbonate ions - 50 to 70
mEq/L. [2 to 3 times as great as plasma].
During maximal salivation, the salivary ionic
concentrations change considerably because the
rate of formation of primary secretion by the acini
can increase as much as 20-fold. This salivary
secretion then flows through the ducts so rapidly
that the ductal reconditioning of the secretion is
considerably reduced because of availability of less
time for movement of solutes. Therefore, when
copious quantities of saliva are being secreted, the
sodium chloride concentration rises only slightly
[1/2 or 2/3 that of plasma], and the potassium
concentration rises to only four times that of
plasma.
As mentioned earlier, as the rate of secretion
increases, there is less time for NaCl to be extracted
and the tonicity of the saliva rises, but it always
stays somewhat hypotonic with respect to
plasma.
 Dr. Venky’s Exam Oriented Physiology
Composition of saliva is as follows:
Daily secretion: 800 and 1500 milliliters.
pH – 6.8 – 8.0
Enzymes:
Salivary amylase or ptyalin- begins digestion of
carbohydrates
Lingual lipase- Secreted by Ebner’s gland present
on the dorsum of tongue. It becomes active in the
stomach and digests about 10% of neutral fats.
Lysozymes – They are bactericidal in nature
Kallikrein- It is a proteolytic enzyme which is
secreted by activated salivary cells, which in turn
acts as an enzyme to split one of the blood
proteins, an alpha 2-globulin, to form bradykinin
which is a strong vasodilator.
Mucin is a glycoprotein substance which helps
provide lubrication.
Cations: Na+, K+ and Ca2+ ions
Anions: Cl-, HCO3-, phosphates and bromides
IgA – provides local mucosal immunity.
Organic material: Urea, creatinine, uric acid and
amino acids.
Regulation of salivary secretion
The secretion of saliva is controlled by both
sympathetic and parasympathetic neurons. Unlike
their antagonistic activity in most organs, both
systems stimulate salivary secretion, with the
parasympathetic system producing the greater
response. There is no hormonal regulation of
salivary secretion.
a). Parasympathetic control:
The salivary glands are controlled mainly by
parasympathetic nervous signals from the superior
and inferior salivatory nuclei in the brain stem.
The salivatory nuclei are located approximately at
the juncture of the medulla and pons and are
excited by both taste and tactile stimuli from the
tongue and other areas of the mouth and pharynx.
Many taste stimuli, especially the sour taste, elicit
copious secretion of saliva—often 8 to 20 times the
basal rate of secretion. Also, certain tactile stimuli,
such as the presence of smooth objects in the
mouth (ex. pebble), cause marked salivation,
whereas rough objects cause less salivation and
occasionally even inhibit salivation.
Control of salivation from higher centers:
Salivation can also be stimulated or inhibited by
nervous signals arriving to the salivatory nuclei
from higher centers of the central nervous system.
For instance,
Smell or thought or taste or sound of favourite
foods

Stimulation of taste and smell areas of the cerebral
cortex and amygdala

Stimulation of appetite center

Stimulation of salivatory nuclei

Impulses reach salivary glands via otic and
submandibular ganglia

Increased secretion of saliva
When a person smells or eats favorite foods,
salivation is greater than when disliked food is
smelled or eaten. The appetite area of the brain
plays a role in regulation of these effects and is
located close to the parasympathetic centers of the
anterior hypothalamus.
b). Sympathetic control:
Sympathetic stimulation can also increase
salivation but only a slight amount, and much less
so than parasympathetic stimulation. The
sympathetic nerves originate from the superior
cervical ganglia and travel along the surfaces of
the blood vessel walls to the salivary glands.
c). Blood supply to the glands:
Blood supply to the glands is a secondary factor
that also affects salivary secretion, because,
secretion always requires adequate nutrients from
the blood. So, decrease in blood supply leads to
less secretion. Salivation itself directly dilates the
blood vessels. This vasodilator effect is caused by
kallikrein secreted by the activated salivary cells,
 Dr. Venky’s Exam Oriented Physiology
which in turn acts as an enzyme to split one of the
blood proteins, an alpha2-globulin, to form
bradykinin which is a strong vasodilator.
The parasympathetic nerve signals that induce
copious salivation also moderately dilate the blood
vessels.
Functions of saliva:
1). Digestive function:
Carbohydrate digestion by salivary amylase:
The digestive enzyme ptyalin which is an α-
amylase secreted mainly by the parotid glands
hydrolyzes starch into the disaccharide maltose
and other small polymers of glucose that contain 3
to 9 glucose molecules. However, because the food
remains in the mouth only a short time, usually not
more than 5 per cent of all the starches is
hydrolyzed by the time the food is swallowed.
Fat digestion:
About 10 percent of triglycerides is digested in the
stomach by lingual lipase that is secreted by
lingual glands in the mouth and swallowed with
the saliva.
2). Aiding Speech:
Mucus secreted in the saliva lubricates the oral
mucosa and allows for free movement of tongue
and lips, thus saliva helps in pronouncing the
words.
3). Maintenance of Oral Hygiene:
Under basal awake conditions, about 0.5 milliliter
of saliva is secreted each minute. This secretion is
almost entirely made of the mucous type and plays
an important role for maintaining healthy oral
tissues.
Protective function:
The mouth is loaded with pathogenic bacteria that
can easily destroy tissues and cause dental caries.
Saliva helps prevent the deteriorative processes in
several ways.
First, the flow of saliva itself washes away some of
pathogenic bacteria as well as food particles that
provide their metabolic support.
Second, saliva contains several factors that destroy
bacteria. One of these is thiocyanate ions and
another is several proteolytic enzymes—most
important being lysozyme.
Lysozyme:
(a). Attacks the bacteria,
(b). Aids the thiocyanate ions in entering the
bacteria where these ions in turn become
bactericidal, and
(c). Digests food particles, thereby helping further
to remove the bacterial metabolic support.
Third, saliva often contains significant amounts of
antibodies mainly IgA that can destroy oral
bacteria, including some bacteria that cause dental
caries. In the absence of salivation, oral tissues
often become ulcerated and infected, and caries are
frequently present.
Lactoferrin present in saliva binds iron and stops
the multiplication of bacteria.
Saliva contains buffers and proline-rich proteins.
Buffers help relieve heart burns during
regurgitation of gastric juice into esophagus.
Proline-rich proteins bind with toxic substances
such as tannins which are present in many food
substances such as fruits and render them non-
toxic. Further, they maintain oral pH at 7 at which
saliva is saturated with calcium and therefore teeth
don’t lose calcium, thus proline rich proteins
maintain tooth enamel.
4). Appreciation of taste:
Saliva serves as a solvent for the food particles
which stimulate taste buds after getting dissolved
in it.
5). Excretory function:
Saliva excretes many organic and inorganic
substances like iodine, thiocyanate ions, drugs,
alcohol etc.