AMELOGENESIS

DR. YUSRA JAMIL

ASST. PROFESSOR (ORAL BIOLOGY)
Learning Outcomes
• Define Amelogenesis

• Enumerate different morphological and functional phases/stages which an

ameloblasts passes through during amelogenesis
• Classify enamel proteins secreted by ameloblasts during secretory and maturation
phases
• What are the main functions of important enamel proteins
Amelogenesis
• Process by which enamel is formed incrementally by ameloblasts is
known as Amelogenesis.
• Two step process:

Secretory phase (organic matrix formation): Initially the enamel

formed is only partially mineralized to about 30%.
Maturation phase (Mineralization): After full thickness of enamel layer
has been formed, organic matrix and water is gradually removed;
minerals are added and crystals grow wider and thicker to attain greater
than 96% mineral content.
Stages/Phases of Amelogenesis

Amelogenesis has been described in as many as six phases but generally is

subdivided into three main functional stages referred to as the:

1. Presecretory stage (Morphogenetic phase, Organization and

histodifferentiation phase)

2. Secretory Stage

3. Maturation Stage (Transition Phase and maturation Proper, protection phase)

Presecretory stage
(Morphogenetic phase, Organization and histodifferentiation phase)

 The presecretory stage includes all activities of the future ameloblast before the
secretion of the main component of the enamel matrix.
This stage has two principal features:

1. Differentiation of the pre-ameloblasts

2. Formation and subsequent resorption of a basal lamina.
Morphogenetic Phase
• Early bell stage
• Shape of crown determined
• Basal lamina present
• Cuboidal/low columnar cells of IEE. They are uniform in length
and arranged in a single row
• Large central nucleus
• Mitotic activity present in IEE Proximal end
• Proximal junctional complex
• present (proximal end - towards the stratum intermedium)
• poorly developed Golgi elements in the proximal portion of the
cells (facing the stratum intermedium),
• Mitochondria and other cytoplasmic components evenly
scattered throughout the cell Proximal junctional
complex

Distal end
Histodifferentiation Phase
• Late bell stage
• Mitosis ceases
• Tall columnar cells (40 μm long, 5μm wide)
• Proximal located nucleus (Polarized)
• Distal located RER and Golgi complex
• Basal lamina disintegrates
• Distal Junctional complex appears.
• Tightly hold the ameloblasts and determine at different stages that what may,
and may not, pass between them to enter or leave the enamel.
• Secretion of enamel and dentine proteins (transient) -

Distal
junctional
complex
• The Ameloblast becomes a polarized cell, with the majority of its
organelles like Golgi complex and RER situated in the cell body
distal to the nucleus (supranuclear cytoplasm) Proximal junctional
complex
• Mitochondria cluster in the infranuclear compartment
(proximally), with only a few scattered through the rest of the
cell

Distal
junctional
complex
Secretory phase
At late bell stage of tooth development
Ameloblast cells present as Taller columnar cells (50μm long, 5-10 μm wide)
Electron microscope E/M:
Golgi apparatus; developed and condensed occupying a major part of the
central core
Mitochondria clustered in the proximal region
RER and vesicles increased in number reflecting their intense synthetic
and secretory activities.
Cell attachment.. Proximal and distal junctional complexes
The cells acquire intense synthetic and secretory activity

• mRNA for enamel proteins are translated by rough endoplasmic

reticulum Modified by Golgi complex packed into
secretory granules
• These granules migrate to distal extremity of the cell, into Tomes Process

• Enamel proteins and water (organic matrix) are secreted through

secretory vesicles at the distal end of the cells against the newly formed
mantle dentin.
• This matrix is immediately mineralized by deposition of hydroxy apatite
crystals
• So an un-mineralized enamel matrix is never seen in enamel,
mineralization is 30% at this stage.
• Initially crystallites of hydroxy apatite are thin (1.5 nm thick),
needle like and much smaller as compared to mature enamel
crystals
• Enamel thickness completely formed during this phase.
• Ameloblasts as they move away from the forming enamel
develop Tomes’ process at the distal secretory end (i.e. towards
the enamel)
• Initially the tomes’ process of ameloblast comprise only of
proximal portion. Thus initial thin layer of enamel doesn’t
contain enamel rods (aprismatic enamel).
• As the ameloblasts migrate away, they develop the distal
portion of tomes’ process.

Interrod enamel

Rod enamel
The shape of the Tomes process of
ameloblasts is responsible for the
prismatic appearance of Enamel

Proximal portion: from junctional

complex to surface of enamel layer.
• result in formation of interrod Proximal portion
of tomes process
enamel

Distal portion: penetrates into and

interdigitates with enamel beyond
initial layer.
• Result in formation of enamel rods
Distal portion
of Tomes
process
• Formation of interrod is always a step ahead as it
delimits the cavity into which rod enamel is
formed.
• Both sites have same composition, but they differ
only in orientation of their crystallites.
• Prismatic enamel (having rods and interrods)
formed making up the bulk of the Enamel
• Final enamel is also aprismatic (i.e. without rods
and inter rods arrangement because of absence of
tomes process)
• It means that prismatic enamel is sandwiched
between aprismatic enamel
Capillaries of Dental follicle come closer to
proximal end of ameloblasts during secretory
phase without disrupting the basal lamina of
outer aspect of enamel organ to form papillary
layer.
Enamel is formed incrementally
Maturation Phase
Amelogenesis is a slow process that takes about 5 years to complete.

 Maturation phase is the longest phase of Amelogenesis.

 It takes about 2/3rd of the time taken in amelogenesis.

• The enamel which is deposited in secretory phase has a high content of water
and enamel proteins (about 70%) and a low content of minerals (about 30%)

• The process that converts this young, immature enamel into fully mineralized and
mature enamel is known as Maturation.

• Crystal growth during the maturation stage occurs at the expense of matrix
proteins and enamel fluid that are largely absent from mature enamel.
Maturation Phase

Can be divided into:

1. Transition Phase
2. Maturation Proper
Transition Phase
 A brief period in which the ameloblasts change from a secretory form
to a maturation form is known as transition phase

• Enamel formative proteins (amelogenins and non amelogenins)

secretion stops
• Withdrawal of tomes’ process.
• Ameloblasts become short and the cell organelles and volume
decreases.
Transition Phase
 Programmed cell death occur known as Apoptosis (in which 25% ameloblasts die in
transition phase and another 25% die in maturation proper = total 50% cells die)

• Apoptosis is defined as programmed cell death without any physical insult, injury, or any
external causative factor. The cell itself sense the need to die and it occurs without any
inflammatory response. The adjacent cells and environment remains unaffected
 Trauma

Necrosis

Cells and organelles swell

Cell lysis and Invasion of

phagocytic cells leading to
Inf lammation
Apoptosis

The Bcl-2 family of proteins, comprising

antiapoptotic and proapoptotic proteins is a
major regulator of apoptosis.
Transition Phase – at the end
• At the end of transition phase and beginning of maturation
proper Basal lamina reforms
• The basal lamina in this case is unique because it lacks Collagen type IV and it is facing a
mineralized surface and attached with it by means of hemidesmosomes which have
laminin-322 proteins (previously known as laminin- 5),and also Amelotin (which is
secreted by ameloblasts)
• No Tomes process is present at the distal end of Ameloblasts. It is flat again
• Microvilli appear on cells of Outer enamel epithelium, Stratum intermedium and Stellate
reticulum
Maturation Proper
• Matrix proteins and water needs to be removed so that space is created for
the growth of the crystals

• During the maturation phase already formed hydroxyapatite crystals (of

secretory phase) grow in width and thickness but new crystals are not
deposited.

• Attachment proteins are only secreted (amelotin and apin) which keeps the
mature ameloblasts and basal lamina attached with the mineralized surface
Maturation Proper

• MAIN EVENTS:

• Degradation of enamel proteins by proteinases (protein degrading enzyme -Kellikerin

4)
• Withdrawal of great amounts of degraded proteins &water from enamel
• Rapid influx of mineralizing salts (calcium and phosphate ions)
• Enamel mineralization increased from 30% to 96%
Ameloblasts alternate cyclically in developing smooth and
ruffled borders in the apical cytoplasm during the maturative
stage . These changes are referred to as modulation

 Modulation is a reversible change in cell activity and

morphology of ruffle ended and smooth ended
ameloblasts.

 It is due to the difference in permeability of junctional They can modulate once

complexes every 8 hours

 Significance of the modulations: maintaining an

environment that allows accretion of mineral content and
loss of organic matrix, in part through alterations in
permeability of the enamel organ.
Ruffle Ended ameloblast
Contain:
 numerous lysosomes,
 calcium-binding proteins
 membrane-associated calcium-adenosine triphosphatases or Calcium ATPase
(promote the pumping of calcium ions into the maturing enamel).

 Therefore, Active secretion of matrix degrading enzymes (proteinases) AND

incorporation of mineral ions into crystals occurs mainly in relation to the ruffle
ended cells
 Some protein fragments from the enamel layer also may be taken up by endocytosis
across the membrane infoldings of the ruffled border.
 Ruffle ended ameloblasts secrete bicarbonate ion to keep the mineralizing front
alkaline, prevent acidification and thereby helps to keep the mineralization process
to continue.
Ruffled ended ameloblasts secrete lysosomes, calcium and phosphate ions into the
maturing enamel through the ruffled border
Ruffle Ended Ameloblasts
• Ruffled ended ameloblasts have tight
distal junction and leaky proximal
junction
• Cells spend 8o% of its lifetime in this
form
• The route by which calcium moves
from blood vessels to enamel is via
ruffle ended ameloblasts. (because
their distal ends are tight).
• show considerable endocytotic
activity and they absorb protein break
down product.
• Ruffled ended ameloblasts secrete
lysosomes, calcium and phosphate
ions into the maturing enamel
through the ruffled border
Smooth Ended Ameloblasts
• Smooth ended ameloblasts have leaky distal junctions and
tight proximal junction
• Cell spends 20% of its lifetime in this form
• Have almost no membrane calcium-ATPase activity (thus
don’t pump Ca ions),
• Show little endocytotic activity, thus Polypeptide fragments
leaving the enamel likely pass between the leaky distal
junctions of smooth-ended cells and diffuse laterally among
the ameloblasts to be taken up along their basolateral
surfaces.
• Smooth ended ameloblasts permit exit of degraded proteins
and water from the maturing enamel through the leaky
distal junctions
Significance of pH maintenance
during modulation
Ruffle ended Ameloblast
The acidification associated with ongoing
mineral accretion during maturation causes
ruffle-ended ameloblasts to produce
bicarbonate ions.
This process continuously alkalizes the
enamel fluid to prevent:
• reverse demineralization of the growing
crystallites and
• maintain pH conditions optimized for
functioning of the matrix degrading
enzymes, which prefer slightly acidic to
near neutral conditions
Smooth ended Ameloblast
• Low pH triggers the modulation of
smooth ended amelobalsts
• Interstitial fluids that may leak into the
maturing enamel during the smooth
ended phase, may also contribute to
neutralizing the pH of the enamel fluid.
• Bulk-Degrading enzymes act
extracellularly to digest various matrix
proteins into fragments small enough to
leave the enamel.
• Polypeptide fragments leave the enamel
through distal (leaky) junctions of
smooth ended ameloblasts and diffuse
laterally among the ameloblasts to be
taken up along their basolateral
surfaces.
Post maturation Phase
1. Protective stage
• When the enamel has completely developed and has fully calcified, the ameloblasts
cease to be arranged in a well-defined layer and can no longer be differentiated from the
cells of the stratum intermedium and outer enamel epithelium.
• These cell layers then form a stratified epithelial covering of the enamel, called
reduced enamel epithelium.
FUNCTION of REE:
1. Protecting the mature enamel by separating it from the connective tissue until the tooth
erupts.
2. If connective tissue comes in contact with the enamel, anomalies may develop. Under such
conditions the enamel may be either resorbed or covered by a layer of cementum.
3. The composition of enamel can still be modified. For instance, fluoride, if available, still can
be incorporated into the enamel of an unerupted tooth,
4. As the tooth passes through the oral epithelium, the part of the reduced enamel
epithelium situated incisally is destroyed, whereas that found more cervically interacts with
the oral epithelium to form the junctional epithelium.
Post maturation Phase

2. Desmolytic stage

 The reduced enamel epithelium (REE) proliferates and seems to induce atrophy of the
connective tissue separating it from the oral epithelium, so that fusion of the two
epithelia can occur.
• Epithelial cells elaborate enzymes that are able to destroy the connective tissue
fibers by desmolysis.
• As the tooth passes through the oral epithelium, the part of the reduced enamel
epithelium situated incisally is destroyed, whereas that found more cervically
interacts with the oral epithelium to form the junctional epithelium. (this is the fate
of REE)
• Premature degeneration of the reduced enamel epithelium may prevent the
eruption of a tooth
FUNCTION of R.E.E:
1. Protecting the mature enamel by separating it from the connective
tissue until the tooth erupts.
2. If connective tissue comes in contact with the enamel, anomalies may
develop. Under such conditions the enamel may be either resorbed or
covered by a layer of cementum.
3. The composition of enamel can still be modified. For instance, fluoride, if
available, still can be incorporated into the enamel of an unerupted tooth,
4. As the tooth passes through the oral epithelium, the part of the reduced
enamel epithelium situated incisally is destroyed, whereas that found
more cervically interacts with the oral epithelium to form the junctional
epithelium
Review questions
1. What is meant by amelogenesis?? Give its phases
2. Enumerate different morphological and functional phases/stages which an ameloblasts passes
through during amelogenesis
3. Explain morphogenetic, histodifferentiation and secretory phases of amelogenesis in terms of
histological appearance and dimensions of cells
4. Explain the formation and location of Tome’s process and its role in enamel mineralization during
secretory phase of amelogenesis?
5. How secretory phase ameloblast regulate this prismatic and aprismatic appearance of enamel?
6. Enlist the important events taking place during transition phase of amelogenesis?
7. What is the unique feature of basement membrane present between ameloblast and enamel surface during
amelogenesis?
8. What is meant by modulation cycle seen during maturation phase of amelogenesis? Also explain its significance,
functional and morphological changes in ameloblasts, and permeability of junctional complexes during maturation
phase.
9. During the maturative stage of amelogenesis, explain the
changes that take place in the:
 Structure and function of amelogenesis
 Structure of enamel
10. What is the significance of pH maintenance during
maturation phase of amelogenesis?
11. What is reduced enamel epithelium?
12. Enlist four functions of reduced enamel epithelium?
13. What is the fate of reduced enamel epithelium ???
ENAMEL PROTEINS

• Organic matrix of forming enamel is composed of non-collageneous

proteins (enamel proteins and enzymes) and water only.

• Enamel proteins are unique proteins different from

any other proteins of body
Proteins contributing to appositional growth in thickness of enamel

Enamel matrix Proteins

Amelogenins Non Amelogenins

90% 10%
Ameloblastin
Enamelins
Sulphated proteins

Proteins involved in post secretory processing and degradation of

amelogenins and non amelogenins

Enamelysin Enamel matrix serine protease

(Kallikrein 4)
Proteins related to basal lamina covering maturing and mature pre-eruptive
enamel

Amelotin Odontogenic Ameloblast-associated

Legacy Proteins

Tuftelin Amelin/ Sheathlin

 FORMATION OF THE ENAMEL MATRIX
ENAMEL MATRIX PROTEINS
• The ameloblasts begin their secretory activity when a small amount of dentin
has been laid down.
• As enamel deposition proceeds, a thin, continuous layer of enamel is formed
along the dentin.
Amelogenins is the major component of enamel matrix proteins. (makes up
90% of the enamel proteins)
• It undergoes extracellular degradation by proteolytic enzymes like matrix
metalloproteinases into smaller low molecular weight fragments, like tyrosine
rich amelogenin protein, and leucine rich amelogenin polypeptide
• Low molecular weight proteins (5-45 kDa)
• Hydrophobic in nature
• Rich in amino acids like proline, histidine and glutamine
• Function: regulating crystal growth
Prevent premature crystals union
• The genes coding for amelogenin is present in X and Y
chromosomes.
Hence variation in amino acid sequences also exist between
the gender in humans.
• Most of the secreted amelogenin is removed during
maturation.
• It is suggested that amelogenins form thixotropic gels so
that they can be easily squeezed out by the pressure from
the growing crystals.
Amelogenins have been shown to form minute nanospheres
(20 nm in diameter) between which enamel crystals form.
Function: maintaining spaces between the crystals.
• Regulate growth in thickness and width of crystals (inhibits
volumetric expansion)
• Prevent premature crystals union
• Must be removed during maturation to allow crystals growth
in volume
In the fully formed enamel amelogenin remains in between the
crystals and also surrounding them.
Experimentally, absence of amelogenin, resulted in the
formation of hypoplastic teeth.
NON AMELOGENINS
Ameloblastin and are the other important proteins of the enamel matrix.
They also undergo extracellular processing like amelogenin, but at a rapid rate. It is
secreted during secretory and maturation phases
of amelogenesis
 Present in low concentration (10 %)
 Its molecular weight is around 70kDa
 It is larger (2.5 times) than amelogenin but smaller than enamelin
Function: help in nucleation and growth of crystals.
• Promote and guide formation of crystals
• Allow lengthwise increase in crystals
• Adherence of ameloblasts with enamel surface
In case of loss of function of mutant protein:
Terminal differentiating ameloblasts detach from the dentin, and enamel formation
aborts. Enamel organ regresses and becomes cystic.
Experimentally, in the absence of ameloblastin, no structural layer of enamel
formation is observed.
Enamelin: Largest enamel protein.
• molecular weight is 186 kDa
• Least abundant protein (less than 5% of enamel matrix)
• Has extensive post secretory modification – smaller sized fragments are
formed
Enamelin and its large fragments (to about 89 kDa) are found near ameloblasts
and not in deeper enamel layer

Function: promotes crystal initiation

promotes crystal elongation
Sulphated Enamel proteins

 acidic
enamel proteins
• molecular weight is 65 kDa
• Present in small amounts
• They have a very short half life and degraded within 1- 2 hours of
formation

Function is unknown
PROTEINS INVOLVED IN POST SECRETORY PROCESSING AND
DEGRADATION OF AMELOGENINS AND NON AMELOGENINS
Enamelysin (MMP20)
 It is a proteinase enzyme
 It is calcium dependent matrix metalloproteinase (MMP).
 Found mainly in newly secreted enamel (secretory phase)
 Involved in short term processing of proteins (amelogenins, ameloblastin and enamelin)
and cleaves larger proteins into smaller fragments
Function:
Involved in post translation modification of newly secreted amelogenin and non
amelogenins into smaller sized functional fragments during secretory phase of
amelogenesis
In case of loss of function:
hypomaturation of enamel occurs Thinner enamel layer
(Hypomineralized enamel, Rod-interrod organization is disturbed, enamel proteins persist
during maturation)
Kallikrein 4
• Bulk digesting (degrading) proteinase
• Secreted during maturation phase of amelogenesis
• Breaks down amelogenin and non amelogenins fragments into smaller
polypeptides which easily leave enamel layer - space is created for crystals growth

In case of loss of function: hypomatured/ hypomineralized soft enamel is formed

(Hypomineralized enamel, Rod-interrod organization is disturbed, enamel proteins

persist during maturation)
PROTEINS RELATED TO BASAL LAMINA COVERING MATURING
AND MATURE PRE-ERUPTIVE ENAMEL
Amelotin
• Recently discovered, Secreted during maturation stage
Location:
• Resides in the surface basal lamina along with laminin-332
throughout maturation,
• Also found at the interface between the junctional epithelium
and the tooth.
Function:
• Plays a role in adhesion of basal lamina with maturing enamel
Surface cell adhesion to the tooth surface plays an important role in
maintaining periodontal integrity and health.
• Disruption of laminin-332 production causes enamel
hypomaturation.
Odontogenic
ameloblast-associated (ODAM)
Secreted by ameloblasts at maturation stage.
Location:
• In the surface basal lamina throughout maturation,
• In membrane infoldings of ruffle-ended ameloblasts.
• Also found in the basal lamina located at the surface of junctional
epithelium
Function:
• Adhesion of basal lamina to the maturing enamel surface.
• cell adhesion to the tooth surface plays an important role in maintaining
periodontal integrity and health.
Loss of function:
• No enamel phenotype
• Junctional epithelium defects
Tuftelin
• 58-60 kDa molecular weight
• It is the earliest protein produced even before differentiation of ameloblasts
• Have a role in epithelial mesenchymal signaling
• It is located at dentinoenamel junction
Calcium ions pass actively through the ruffle ended ameloblasts and passively
through the sides of the smooth ended ameloblast to the mineralizing front.
Ruffle ended ameloblasts secrete bicarbonate ion to keep the mineralizing front
alkaline, prevent acidification and thereby helps to keep the mineralization
process to continue.
Ameloblasts secrete proteases of different types of which metalloproteinases
and serine proteases are important.
Metalloproteinases alter the basic structure of amelogenins by hydrolysis into
many low molecular weight fragments.
Serine proteases function as bulk digestive enzymes to clear matrix proteins
from intercrystal spaces.
• It degrades the enamel proteins into small polypeptides to be absorbed by the
ruffle ended ameloblast and through leaky distal junctions as well as through
the basolateral surfaces of the smooth ended ameloblasts
Membrane bound proteins present in the
ameloblasts like CD63, annexin A2 and
lysosomal associated glycoprotein 1
interact with secreted proteins to initiate
removal of the organic matrix.
The fact that organic components as well
as water are lost in mineralization is a
striking difference between enamel and
other mineralized tissues.
Over 90% of the initially secreted protein is
lost during enamel maturation, and that
which remains forms envelopes around
individual crystals.
MINERALIZATION PATHWAY AND MATURATION OF THE ENAMEL MATRIX

Mineralization of the enamel matrix takes place in two stages:

• In the first stage an immediate partial mineralization occurs in the matrix
segments and the interprismatic substance as they are laid down.

• Calcium moves from blood vessels through the enamel organ to reach enamel.
The stratum intermedium and ruffled ended ameloblasts participate in the
translocation of calcium since “calcium ATPase”activity has been localized in
their cell membrane

• No matrix vesicles are observed in enamel formation so no unmineralized matrix

like that of predentin or osteoid is seen during enamel formation.
Therefore, apatite crystals are not preformed when they are released by the
secretory granules.
• Nucleation is initiated by the apatite crystallites of dentin on which enamel
is laid.
• First mineral is in the form of crystalline apatite that is octacalcium
phosphate
• which act as a template for hydroxyapatite, however it is unstable and
convert into hydroxyapatite; one unit of it forming two units of
hydroxyapatite

Nucleation: the initial process that occurs in the formation

of a crystal from a solution, a liquid, or a vapour, in which
small number of ions, atoms, or molecules become
arranged in a pattern characteristic of a crystalline solid,
forming a site upon which additional particles are
deposited as the crystal grows.
The second stage, or maturation, is characterized by the gradual
completion of mineralization.

The process of maturation starts from the height of the crown and
progresses cervically.

Each rod matures from the depth to the surface, and the sequence of
maturing rods is from cusps or incisal edge toward the cervical line.
Maturation begins before the matrix has reached its full thickness.
The advancing front is at first parallel to the dentinoenamel junction and later to the outer enamel surface.
Following this basic pattern, the incisal and occlusal regions reach maturity ahead of the cervical regions.

The crystals increase in size from 1.5 to 25 μm during the maturative phase.
Tuftelin an acidic enamel protein localized to the DEJ has been reported to
participate in the nucleation of enamel crystals.
Other enamel proteins regulate enamel mineralization by binding to specific
surfaces of the crystal and inhibiting further deposition.
The rate of formation of enamel is 4 μm/day, therefore to form a layer of enamel
of 1 mm thickness it would take about 240 days.
The rate of enamel formation is more in permanent teeth than in deciduous
teeth.
The crystal sizes increase further after tooth eruption due to ionic exchange
with saliva.
Chemical analysis shows that the loss in volume of the organic matrix is caused
by withdrawal of a substantial amount of protein as well as water.
Regulation of pH during Enamel formation

• pH values of forming enamel are maintained near neutral during secretion.

But they show considerable variation during maturation stage from
 Highly Acidic
 nearly Neutral
 Alkaline
• Carbonic Anhydrases mainly CA2 and CA6, generates local bicarbonate-
chloride exchangers, bicarbonate cotransporters and Na⁺/H⁺ exchangers
• Transport phosphate and nutrients from blood vessels to enamel organ
Uniqueness of the process of Amelogenesis
• The secretory cell is an epithelial cell whereas all other secretory cells of hard tissues are
ectomesenchymal.
• Noncollagenous proteins are involved in mineralization of enamel whereas in all other
hard tissues collagen plays an important role.
• The matrix of enamel does not contain collagen; in other hard tissues collagen is the major
protein.
• The matrix of enamel is partially mineralized; in other hard tissues the matrix is
nonmineralized.
• Enamel therefore lacks a distinct organic phase like osteoid, predentin or cementoid.
• There is no absorption of secreted matrix in other hard tissues but in enamel formation
90% of secreted matrix is absorbed and this activity is done by ameloblasts itself.
• After formation of enamel, ameloblasts undergo apoptosis; hence enamel formation does
not occur later on.
• In other hard tissues formation occurs throughout
REVIEW QUESTIONS

 Classify enamel proteins according to their function during amelogenesis?

 What are amelogenins? Describe its structural features and functions?
 What do u know about mineralization pathway of
enamel? OR
 Describe the four phases of enamel mineralization?
 Describe the four phases of enamel mineralization??
 Describe dimension, shape, function and growth of enamel crystallites (hydroxyapatite)
 What is the significance of pH maintenance during
maturation phase of amelogenesis?
AGE CHANGES
Color
Permeability
Surface structure modification
CLINICAL CONSIDERATIONS