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 Amelogenesis is under genetic control
 Amelogenesis & Dentinogenesis occurs
almost simultaneously, but as distinctly
different process
 They both begin @ DEJ
 Odontoblasts initiate Dentine matrix
formation prior to the beginning of
amelogenesis.
 They produce collagen, that is formed into
bundles that point towards the cells of the
internal enamel epithelium (Pre-
ameloblasts)
Proximal
end
Distal
end
IEE
cell
Pre-
ameloblasts
This stage has 2 principal features
1. Differentiation of the pre-
ameloblasts
2. Formation & subsequent resorption
of the basal lamina
During bell stage ,
Cells of IEE ceased to divide
committed enamel forming cell  pre-
ameloblasts
resorption
of the
basal
lamina
Dentine
 Ameloblasts differentiate from,
cuboidal  columnar
 The cell become polarized
 These columnar cells  pre-
ameloblasts
Pre-
ameloblasts
 A basal lamina separates the preameloblasts
from the dental papilla
 This lamina marks the position of future DEJ
 Differentiation of the odontoblasts 
controlled by cells of IEE  by release of
growth factors (TGF-β)
 Once the odontoblasts
have differentiated
basal lamina disappears
as the first layer of the
dentine matrix is laid
down
 IEE enzymes 
degradation
resorption
of the
basal
lamina
Dentine
 For a brief period  future ameloblasts &
odontoblasts are in intimate contact 
 first cells to lay down matrix
 provide signal for to begin
secretion
 Odontoblasts non-collagenous protein &
DSPP (also by pre-ameloblasts) this initial
matrix defines DEJ
 Before any mineralization begins, pre-
ameloblasts secrete enamel protein on the top
of the dentinal matrix some of which diffuse &
taken up by odontoblasts
form in the enamel matrix within these irregularities in
contact with the ameloblasts
Cell processes extend into irregularities on the adjacent predentine
surface
of the pre-ameloblasts
Immediately after this, is laid down
 Initial enamel absence of Tomes process

 Pre-ameloblast
› Length= 40 μm
› Diameter = 2-4 μm
 Ameloblasts become long, cells 
length =60 μm & width= 2-4 μm
 Following deposition of aprismatic enamel 
a forms at the distal
secretory end of the ameloblasts
Ameloblasts
Enamel
matrix
Dentine
St.
intermedium
Tomes process
of tomes process  responsible for
of enamel
 Relationship between ameloblasts size &
prism pattern
› Large ameloblasts = type 3 pattern
› Smallest ameloblasts = type 2 pattern
Ameloblasts
Developing
enamel
Tomes
process
Interpit
prongs
“picket fence” arrangement
front changes
Tomes process
Tomes
process
 As the ameloblasts shifts from
Presecretory phase  secretory
phase , there is marked
aggregation of
 The material contained within the
vesicle represents the
Secretory
granules
 The contents of the vesicles are
discharged into the extracellular
space
› at the distal end of the cell
› between the cell membrane of the
adjacent ameloblasts
 As the enamel matrix
is secreted  the
ameloblasts are
pushed away from the
dentinal surface
Ameloblasts
Developing
enamel
Developing
dentine
Odontoblasts
so a distinct like
predentine is seen in enamel
appear almost
Within this organic matrix before matrix
is thick
Secreted
matrix
between
ameloblasts
Secretory
vesicle
Early
enamel
dentine
Ameloblasts
 1st formed crystals  ,
10-15 nm wide & 1-2 nm thick
 During development  enamel crystals form
 aligned to the surface
of the ameloblasts
 Enamel crystals  elongate around the of
tomes process  prism
 Crystallites extending from where ameloblasts
are joined  prism
 As a part of ameloblast is non-secretory  clear
border between core & boundary
 Full thickness of enamel matrix  Secretory
phase
 Tomes process  retracts  distal end
becomes flat  , thin layer of
enamel is formed at surface
 4 ameloblasts  single prism
 Each ameloblasts  development of 4
prims
 Enamel prism elongate incrementally
 Daily increment – cross striations
 Weekly increment– enamel striae
 Period in which ameloblasts change from
secretory  maturation form
 Initially deposited enamel 
› High content of water & protein
› Low content of mineral
 Enamel maturation  by ameloblasts  but
in a very changed form
 Enamel secretion stops
 Much of matrix is removed
 Reduction in height of ameloblasts  signals
onset of transition
 No. of ameloblasts reduced by 50%
(apoptosis)
 In remaining ameloblasts  organelles
associated with protein synthesis (RER)
reduced by autophagocytosis
 Enamel organ invaginated by blood vessels
 Blood vessels  lie close (but not in contact)
with the proximal end (base) of the ameloblasts
 Proteins & peptides  25-30 % by weight
(mature enamel  1 %)
 Developing enamel matrix during the early
secretory phase 
 Enamel protein Unique protein different from
any other protein found in body
1 % of weight
Proteins (mainly non-amelogenenins )
Mature enamel
The majority of enamel protein are degraded
Following the process of maturation
90-95 %5-10 %
 Amelogenins hydrophobic , tends to clump or
aggregate
 They spread throughout the whole developing
enamel thickness
 Resultant matrix  , through which
molecules & ions can spread readily
significant in production of large crystals
 Folding of molecule  self assembly
formation of minute
(20nm)
 1st crystals are formed between these
spheres
 It is broken down by proteolytic cleavage with
increasing depth of enamel
 Absent from inner layer of enamel
 25 kDa  20 kDa  5 kDa (TRAP)tyrosine-rich
amelogenin peptide
 occurs after secretion of enamel
matrix  continues throughout secretory stage
 Location prism cores
 Control growth of crystals by an inhibitory
action
 Largest enamel protein
 Initially located  prism near secretory
ameloblasts
 Smaller breakdown products prism
 Function  generation of
 Also produced by HERS during root formation
 Signaling molecule during epithelial
mesenchymal interaction
 Location DEJ nucleator at the
commencement of initial enamel
mineralization
 Enamel tufts tuft protein
 Produced by ameloblasts @ maturtion stage
 Expressed later than other enamel protein
 Associated with basal lamina role in cell
adhesion
 Proteinases & metalloproteinases
 Enamelysin  whose cleavage product
accumulate as the hydroxyapatite crystals
lengthen
 Kallikrein 4 enamel matrix serine proteinase
 Activity of these enzymes  peak @ maturation
stage  when most of enamel protein is lost
 The process by which enamel changes into
final form
 Once the entire thickness of the enamel has
formed  it is structurally complete
 Newly formed enamel  , 20
% organic & 15 % inorganic
 Enamel crystals  increase in width &
thickness
 Consequent reduction in intercrystallite
space
 Ameloblasts move Ca, phosphate &
carbonate ion into the matrix
 Ameloblasts remove water & degrade
enamel matrix protein from it.
content of the enamel reduced
from 30 % 
 Crystallites expand from 1.5 nm thick  25
nm removal of matrix
 Enamel organ  serine proteinase 
degradation of enamel protein  mineral
gain
 At this initial stage  space created is
occupied by water  enamel become
porous
 Tomes process is lost
 Organelle content reduced
 Remaining organelle congregate at the
distal end of the ameloblasts ruffled border
 ‘Ruffle- ended’ ameloblasts alternates with
‘smooth-ended’ ameloblasts
Ruffled
border
Resorptive
vesicle
Enamel
 Modulation  indicate alternation between
resorptive & secretory phase of activity
 Movement of Ca2+ ions
› Ruffle- ended : actively controlled
› Smooth- ended : diffusion (hence few would
enter the enamel)
 Local pH changes
› Ruffle- ended normal pH favors mineralization
› Smooth – ended  mildly acidic pH  resist
mineralization
 Ameloblasts may induce pH changes
modulating bicarbonate level
 Lowering of molecular weight of enamel
protein  by a group of proteinases in
enamel matrix
 The of the mineralization
process  after virtually all protein has been
removed
The increase in
mineral density
begins over the
cusp tips &
progresses
cervically
Initial
enamel
deposition
Increased
mineralization
follows during
maturation
 Once maturation is complete  ameloblasts
become
 A thin amorphous layer of protein (
) separates the cells
from the enamel
 Ultrastructure level this has appearance of
basal lamina
Enamel space
Dental follicle
Oral epithelium
Reduced enamel
epi.
 Basal lamina
› Material extruded from the enamel during
maturation
› Last secretory product of ameloblasts
 The remnants of the enamel organ merges
with flattened ameloblasts RER
 Ca  reaches the matrix principally via the
enamel organ
 It travels via extracellular route
 The ameloblasts layer has a limited &
variable but controlled permeability
 This property  proximal cell junctional
complex
Ameloblasts
Enamel
Calcium
 First formed enamel at the DEJ  less well
organized than the bulk of the enamel in terms
of crystallite size & morphology  Aprismatic
 Tuftelin – crystallite growth & nucleation
 Amelogenins capable of self-assembling into
minute spheres between which the 1st
crystallite of enamel are formed
 The form as a from the
matrix that is supersaturated with
hydroxyapatite
 Initially crystals grow by fusion of nucleation
sites
 Once prismatic structure is established
crystallites enlarge in rather than width
The matrix can control the crystallite growth
pattern by two mechanisms
 By breaking down protein in a controlled pattern
to provide the space for new crystallite
deposition same dimension microchannels
 By modulating the effect of inhibitory molecule
 After maturation phase the role of the
matrix proteins is largely ended
 Virtually all proteins has been lost & what
remains is replaced by tissue fluid
 The matrix proteins  actually removed long
before crystallite growth ends
 The degraded matrix proteins accumulate in
the extracellular space around the
ameloblasts and by inhibiting further activity,
could control & limit the thickness of enamel
deposited.
 The increase in mineral during maturation
follows a different pattern from the initial
deposition
 The initial crystallites form as a precipitate
within the matrix that is supersaturated with
hydroxypapatite.
 Crystallites form and grow while close to the cell
membrane of the tomes process.
 They grow by the deposition of ions on the
crystallites faces.
 As the ameloblasts retreat, they form pyramidal
tomes processes at their distal ends  the
enamel formed thereafter is  prismatic
Tomes
process
 Morphogenic
 Organizing
 Formative
 Maturative
 Protective
 Desmolytic
Amelogenesis
Amelogenesis
Amelogenesis

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Amelogenesis

  • 1.
  • 2.  Amelogenesis is under genetic control  Amelogenesis & Dentinogenesis occurs almost simultaneously, but as distinctly different process  They both begin @ DEJ
  • 3.
  • 4.  Odontoblasts initiate Dentine matrix formation prior to the beginning of amelogenesis.  They produce collagen, that is formed into bundles that point towards the cells of the internal enamel epithelium (Pre- ameloblasts)
  • 5. Proximal end Distal end IEE cell Pre- ameloblasts This stage has 2 principal features 1. Differentiation of the pre- ameloblasts 2. Formation & subsequent resorption of the basal lamina During bell stage , Cells of IEE ceased to divide committed enamel forming cell  pre- ameloblasts resorption of the basal lamina Dentine
  • 6.  Ameloblasts differentiate from, cuboidal  columnar  The cell become polarized  These columnar cells  pre- ameloblasts Pre- ameloblasts
  • 7.  A basal lamina separates the preameloblasts from the dental papilla  This lamina marks the position of future DEJ  Differentiation of the odontoblasts  controlled by cells of IEE  by release of growth factors (TGF-β)
  • 8.  Once the odontoblasts have differentiated basal lamina disappears as the first layer of the dentine matrix is laid down  IEE enzymes  degradation resorption of the basal lamina Dentine
  • 9.  For a brief period  future ameloblasts & odontoblasts are in intimate contact   first cells to lay down matrix  provide signal for to begin secretion
  • 10.  Odontoblasts non-collagenous protein & DSPP (also by pre-ameloblasts) this initial matrix defines DEJ  Before any mineralization begins, pre- ameloblasts secrete enamel protein on the top of the dentinal matrix some of which diffuse & taken up by odontoblasts
  • 11. form in the enamel matrix within these irregularities in contact with the ameloblasts Cell processes extend into irregularities on the adjacent predentine surface of the pre-ameloblasts Immediately after this, is laid down
  • 12.  Initial enamel absence of Tomes process   Pre-ameloblast › Length= 40 μm › Diameter = 2-4 μm
  • 13.  Ameloblasts become long, cells  length =60 μm & width= 2-4 μm  Following deposition of aprismatic enamel  a forms at the distal secretory end of the ameloblasts
  • 15. of tomes process  responsible for of enamel  Relationship between ameloblasts size & prism pattern › Large ameloblasts = type 3 pattern › Smallest ameloblasts = type 2 pattern
  • 17. “picket fence” arrangement front changes Tomes process Tomes process
  • 18.  As the ameloblasts shifts from Presecretory phase  secretory phase , there is marked aggregation of  The material contained within the vesicle represents the Secretory granules
  • 19.  The contents of the vesicles are discharged into the extracellular space › at the distal end of the cell › between the cell membrane of the adjacent ameloblasts
  • 20.  As the enamel matrix is secreted  the ameloblasts are pushed away from the dentinal surface Ameloblasts Developing enamel Developing dentine Odontoblasts
  • 21. so a distinct like predentine is seen in enamel appear almost Within this organic matrix before matrix is thick Secreted matrix between ameloblasts Secretory vesicle Early enamel dentine Ameloblasts
  • 22.  1st formed crystals  , 10-15 nm wide & 1-2 nm thick  During development  enamel crystals form  aligned to the surface of the ameloblasts
  • 23.  Enamel crystals  elongate around the of tomes process  prism  Crystallites extending from where ameloblasts are joined  prism  As a part of ameloblast is non-secretory  clear border between core & boundary
  • 24.  Full thickness of enamel matrix  Secretory phase  Tomes process  retracts  distal end becomes flat  , thin layer of enamel is formed at surface
  • 25.  4 ameloblasts  single prism  Each ameloblasts  development of 4 prims  Enamel prism elongate incrementally  Daily increment – cross striations  Weekly increment– enamel striae
  • 26.  Period in which ameloblasts change from secretory  maturation form  Initially deposited enamel  › High content of water & protein › Low content of mineral  Enamel maturation  by ameloblasts  but in a very changed form
  • 27.  Enamel secretion stops  Much of matrix is removed  Reduction in height of ameloblasts  signals onset of transition  No. of ameloblasts reduced by 50% (apoptosis)
  • 28.  In remaining ameloblasts  organelles associated with protein synthesis (RER) reduced by autophagocytosis  Enamel organ invaginated by blood vessels  Blood vessels  lie close (but not in contact) with the proximal end (base) of the ameloblasts
  • 29.  Proteins & peptides  25-30 % by weight (mature enamel  1 %)  Developing enamel matrix during the early secretory phase   Enamel protein Unique protein different from any other protein found in body
  • 30. 1 % of weight Proteins (mainly non-amelogenenins ) Mature enamel The majority of enamel protein are degraded Following the process of maturation 90-95 %5-10 %
  • 31.  Amelogenins hydrophobic , tends to clump or aggregate  They spread throughout the whole developing enamel thickness  Resultant matrix  , through which molecules & ions can spread readily significant in production of large crystals
  • 32.  Folding of molecule  self assembly formation of minute (20nm)  1st crystals are formed between these spheres
  • 33.  It is broken down by proteolytic cleavage with increasing depth of enamel  Absent from inner layer of enamel  25 kDa  20 kDa  5 kDa (TRAP)tyrosine-rich amelogenin peptide  occurs after secretion of enamel matrix  continues throughout secretory stage
  • 34.  Location prism cores  Control growth of crystals by an inhibitory action  Largest enamel protein
  • 35.  Initially located  prism near secretory ameloblasts  Smaller breakdown products prism  Function  generation of  Also produced by HERS during root formation
  • 36.  Signaling molecule during epithelial mesenchymal interaction  Location DEJ nucleator at the commencement of initial enamel mineralization  Enamel tufts tuft protein
  • 37.  Produced by ameloblasts @ maturtion stage  Expressed later than other enamel protein  Associated with basal lamina role in cell adhesion
  • 38.
  • 39.  Proteinases & metalloproteinases  Enamelysin  whose cleavage product accumulate as the hydroxyapatite crystals lengthen  Kallikrein 4 enamel matrix serine proteinase  Activity of these enzymes  peak @ maturation stage  when most of enamel protein is lost
  • 40.  The process by which enamel changes into final form  Once the entire thickness of the enamel has formed  it is structurally complete  Newly formed enamel  , 20 % organic & 15 % inorganic
  • 41.  Enamel crystals  increase in width & thickness  Consequent reduction in intercrystallite space  Ameloblasts move Ca, phosphate & carbonate ion into the matrix
  • 42.  Ameloblasts remove water & degrade enamel matrix protein from it. content of the enamel reduced from 30 %   Crystallites expand from 1.5 nm thick  25 nm removal of matrix
  • 43.  Enamel organ  serine proteinase  degradation of enamel protein  mineral gain  At this initial stage  space created is occupied by water  enamel become porous
  • 44.  Tomes process is lost  Organelle content reduced  Remaining organelle congregate at the distal end of the ameloblasts ruffled border  ‘Ruffle- ended’ ameloblasts alternates with ‘smooth-ended’ ameloblasts
  • 46.  Modulation  indicate alternation between resorptive & secretory phase of activity  Movement of Ca2+ ions › Ruffle- ended : actively controlled › Smooth- ended : diffusion (hence few would enter the enamel)
  • 47.  Local pH changes › Ruffle- ended normal pH favors mineralization › Smooth – ended  mildly acidic pH  resist mineralization  Ameloblasts may induce pH changes modulating bicarbonate level
  • 48.  Lowering of molecular weight of enamel protein  by a group of proteinases in enamel matrix  The of the mineralization process  after virtually all protein has been removed
  • 49. The increase in mineral density begins over the cusp tips & progresses cervically Initial enamel deposition Increased mineralization follows during maturation
  • 50.  Once maturation is complete  ameloblasts become  A thin amorphous layer of protein ( ) separates the cells from the enamel  Ultrastructure level this has appearance of basal lamina
  • 51. Enamel space Dental follicle Oral epithelium Reduced enamel epi.
  • 52.  Basal lamina › Material extruded from the enamel during maturation › Last secretory product of ameloblasts  The remnants of the enamel organ merges with flattened ameloblasts RER
  • 53.  Ca  reaches the matrix principally via the enamel organ  It travels via extracellular route  The ameloblasts layer has a limited & variable but controlled permeability  This property  proximal cell junctional complex
  • 55.  First formed enamel at the DEJ  less well organized than the bulk of the enamel in terms of crystallite size & morphology  Aprismatic  Tuftelin – crystallite growth & nucleation  Amelogenins capable of self-assembling into minute spheres between which the 1st crystallite of enamel are formed
  • 56.  The form as a from the matrix that is supersaturated with hydroxyapatite  Initially crystals grow by fusion of nucleation sites  Once prismatic structure is established crystallites enlarge in rather than width
  • 57. The matrix can control the crystallite growth pattern by two mechanisms  By breaking down protein in a controlled pattern to provide the space for new crystallite deposition same dimension microchannels  By modulating the effect of inhibitory molecule
  • 58.  After maturation phase the role of the matrix proteins is largely ended  Virtually all proteins has been lost & what remains is replaced by tissue fluid  The matrix proteins  actually removed long before crystallite growth ends
  • 59.  The degraded matrix proteins accumulate in the extracellular space around the ameloblasts and by inhibiting further activity, could control & limit the thickness of enamel deposited.
  • 60.  The increase in mineral during maturation follows a different pattern from the initial deposition  The initial crystallites form as a precipitate within the matrix that is supersaturated with hydroxypapatite.
  • 61.  Crystallites form and grow while close to the cell membrane of the tomes process.  They grow by the deposition of ions on the crystallites faces.  As the ameloblasts retreat, they form pyramidal tomes processes at their distal ends  the enamel formed thereafter is  prismatic
  • 63.
  • 64.  Morphogenic  Organizing  Formative  Maturative  Protective  Desmolytic