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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
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)
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
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