COLLAGEN

GUIDED BY- DR.P.S. RAKHEWAR

DR.LISA CHACKO
DR.MANOJ THORAT
Introduction
Collagen is the most abundant protein in
mammals, comprising approximately one-
third
of the total body protein.
Collagen is the predominant component of
the connective tissue, although its
distribution varies in different tissues.
it is the main fibrous component of the skin
,bone , cartilage ,tendon and periodontium.
 The predominant extracellular matrix
component of the periodontium is collagen, a
genetically distinct superfamily of extracellular
macromolecules that contain one or more triple-
helical domains.
there are as many as 25 different genes that
code for at least 14 different collagen
molecules.
Six different collagen types have been detected
in
the periodontium.
Structure of collagen
Triple helical structure.
The collagen molecule consists of 3 distinct polypeptide
chains, twisted around each other to form rod like
structure. alpha chains, that form homotrimeric or
heterotrimeric domains.
Depending upon type of collagen the molecule may be
made up of either 3identical alpha chains or 2or3 different
alpha chains.
Alpha chain-left handed helices that wrap around each
other into a right handed rope like triple helicle rod.
Each such helix is around 1.4 nm in diameter and 300nm in
length.
 Formation of the triple helix depends on the
amino acid composition of the protein and the
winding of the polypeptide chains.
The amino acid sequence of the triple helix is
glycine-X-Y, where X and Y represent the proline
and hydroxyproline 30% of the time.
1/3rd of the amino acids are glycine. i.e every 3 rd
amino acid is glycine.
The imino acids rigid, cyclic backbone
stabilizes the triple helix by limiting the rotation
 The triple helical structure is stabilized
by extensive network of hydrogen
bonds, covalent cross links, electrostatic
and hydrophobic interactions and van
der waales forces.
The triple helix domain serves two
important functions. It physically
separates the globular domains within
the molecule and offers the potential for
lateral interactions from those amino
acids in the X-Y positions.
Types of collagen with respective genes
and tissues
 The family of collagens can be separated into 7
broad groups:
1) fibrillar,
2) fibril-associated collagens with interrupted
triple helices
3)sheet-forming
4) beaded filaments
5) anchoring fibrils
6) growth plate-specific and
7) miscellaneous.
Fibrillar collagen
Most commonly occuring collagen
proteins and accounts for greatest
percentage of mass in all conn.tissues
Forms extensive linear aggregats.
Fibril formation is is an exact
,parallelconfiguration of collagen
molecules is a letral association of
collagen molecules staggered by 67nm.
It includes collagen type I,Type II, Type
III,Type v, type XI.
Fibril associated collagens with interrupted
triple helices (FACITs)

They do not form fibrills .

Consist of interrupted triple helices and large
amino terminal domains.
3 functional domains
One domain consist 1-2 of triple helices, interacts
and adheres to fibrils
Second domain also consist triple helix, which
projects out of the fibril.
Third domain which consist of a non helical
,globular region is thought to be involved with
matrix or cellular interactions.
 it has been suggested that fibril
associated collagen with interrupted
triple helical structure connects fibrillar
collagen to matrix.
It includes type IX, type XII, type XIV
collagens.
Collagen forming sheets
Non fibrillar collagen, have regions of
helical and non helical structure domain.
Unable to associate into compact
banded fibers.
Type IV Forms a complex ,branching
,net like structure whose globular
regions contact with other type4
molecules.
These collagens found in basement
membranes.
Type VIII-Dumbbell shaped molecule-
Collagen forming beaded
filaments
Only type VI collagen is included in this
class.
Heterotrimrtric molecule consist of short
triple helix domain with large nonhelical
amino and carboxyl regions.
Function of type VI is not known
Pathologic accumaltions have been
noted in sevral fibrotic diseases and
osteoarthritic disorders.
Collagen forming anchoring
fibers
Type VII.
Homotrimrtric molecules that contains very large
globular region.
The cell type secreting type VII collagen is
keratinocytes.
Forms an association with type IV,in basement
membrane and the anchoring plaques in conn.
Tissues.
secure basement membrane to underlying stroma.
Ulterations seen in disease like epidermolysis
bullosa.
Growth plate specific collagens

Homotrimetric collagen .
Type X structural homology to type
VII,but not shown to produce a sheet
structure.
Secreted by hepertrophic chondrocytes
Associated with endocondral bone
formayion.
Function is not known
Suggested that it might influence the
remodelling of cartillage prior to
Miscellaneous collagen
Type XII
No well define function and
stochiometry.
Alpha chains consist of 3 collgenous and
4 noncollagenous domains.
Collagen in periodontium and tooth
structure
gingiva
In healthy gingiva,collagens accounts
approximately three fifth of total protein.
Collagen type I forms the bulk of lamina propia and
provides the tensile strength to the gingival tissue.
Type I and Type III has less proline and
hydroxyproline and more lysine and hydrolysine
than skin type I collagen
Type IV-(Argyrophilic Reticulum Fiber) is locted on
basement membrane.

Periodontal ligament

Main type of collagen in pdl is type I and type III

Type I accounts for more then 70% of pdl collgen

Uniformly distributed in pdl with two identical 1and 2chains.

Reticular fibers are composed of Type III collagen& accounts for about 20% of
pdl collagen.

Consist of three identical 1(III) chains.

Type III is linked with type I thruoght the ligament.

 Small amount of type V and type VI and traces of type IV and
typeVII are also found in ligament

Type IV is associated with major binded collagen fibers but may play
role in maintaning elasticity and integrity of extracellular
matrix,Found in basal lamina.

Type IV and type VII are associated with epithelial cell rests and
blood vessels.

Type VIII is belived to to occour within pdl ,only when ligament is

fully functional.
cementum
Organic matrix of cementum is
composed of type I (90%) And type
III(about 5%)
Sharpeys fibers which forms the bulk of
the cementum are composed mainly
collagen type I .
Collagen type III appears to coat the
type type I collagen of shrpeys fibers.
Alveolar bone
The organic matrix of bone is known as
osteiod , and it sis made up of collagen and
noncollagenous proteins.
Collagen is major organic component of
mineralised bone tissue
Type I collagen (>95%) is the principal
collagen and together with type V (<5%)
,Forms heterotypic fiber bundles that
provide the basic structural integrity of
conn. Tissue.
The elastisity of collagen provides
resillency to tissue and help to rsist fracture
 Also contains type I, Type III,Type v, And
type XII collagen
Sharpeys fibers contain type III with
type I collagen.
BIOSYNTHESIS OF
COLLAGEN
OSYNTHESIS OF COLLAG
Sites For The Synthesis of
Collagen :
1.Mesenchymal Cells & Their
Derivatives
FIBROBLASTS ( major cells )

2.Other Cells : Epithelial cells. Endothelial cells. Muscle

cells. Schwann cells.
 Collagen is a protein composed of amino acids like proline,hydroxylysine
and hydroxyproline.
The biosynthesis of collgen occurs in fibroblasts to form Tropocollagen
molecule Microfibrils

Fibrils

Fibers

Bundle
Collagen crimping
Diament demonstrated that collagenous tissues
exhibit a quantifiable periodicity of structure of
variable scale and this wave for that describes
this periodicity has been referred to
as a crimp.
Fibroblast processes in the developing
collagenous tissues play a role in fabricating
the crimpedarrangement and consequently that
crimping may be an important feature in tooth
eruption.
 In polarizing microscope,
crimping can be recognized
by a regular banding of dark
lines across a
collagenous bundle
observed when its axis lies
perpendicula to the
polarizer directions.
Crimping may be due not only to a sharp
zig-zag arrangement of collagen fibrils,
but also to the micro anatomical
organization of collagenous sheets and
bundles.
COLLAGEN TURNOVER IN THE PERIODONTAL
LIGAMENT

Measurements of tritiated proline and

glycein uptake in the periodontal
ligament of erupting teeth have indicated
that there is a high turnover of collagen
with a half-life varying between 3 and 23
days.
The turnover rate of collagen in the
periodontal ligament is estimated to be
several times greater than in skin and
oral mucosa (Sodek).
Functional adaptation of collagen fibers of
the periodontal fibers.

Current theories of tooth support envisage a

multiphasic system involving fibers, ground
substances, blood vessels and fluid, all acting
together to resist mechanical forces and it seems
that there is both tension & compression of the
tissues.
Minns et al. showed that the internal orientation of
collagen fibers in the connective tissues influences
the mechanical properties of the tissues and
suggested that, in general the collagenous
bundles could best resist axially directed forces.
 The arrangement of majority of the periodontal
ligament collagen fibers are in horizontal &
oblique direction and hence may be adapted to
resist, axial forces.
But the overlapping arrangement of the
bundles seen in scanning electron microscopy
& by polarizing microscopy demonstrated their
ability to resist rotational forces.
The overlapping arrangement of the bundles is
also advantageous in resisting intrusive forces.
Degradation of collagen
Breakdown of collagen is the normal
component of tissue remodelling
There are two pathways of collagen
degradation
i.e intracellular phagocytosis
extracellular mmps
Intracellular ( phagocytosis)
Collagen is phagocytosized by fibroblasts.
Electron-lucent zone

Electron dence zone

Phagosome fuses with pri.lysosme

phagolysosome
Electron dense zone suggesting that enzyme

degradation has occur and fibril loses its

chractristic structure.
Extracellular events
Rapid degradation of collagen by activity of enzyme called as
collagenase.

Extracellular involves collagenase(MMP-1)

Triple helical portion of molecules within the fibril .

together with MMP-IV denaturation of collagen under

physiologic condition.

Rest molecules undergo proteolysis by MMP-II(gelatinase),MMP-IV.

Age changes in periodontal collagen
fibers

The main changes that occur with age is

increased collagen fibrosis and decreased
cellularity (Grant and Bernick).
The fiber bundles were thicker and that the fiber
groups were broader and more highly organized
with areas of hyalinization and decreased
argyrophlia increased
fuschinophilia and a reduction in alcian blue-
positive areas.
Decrease in the number of periodontal fibers
with increase in size of interstitial spaces.
 Severson et al found that the periodontal alveolar bone
surface was smooth and regular in young adults but in
older adults the corresponding surfaces were jagged and
uneven and an irregular insertion of the fibers was seen.

Cementum was thicker in aged tissues and the

cementum surface also became irregular with time.

This irregularity of the fiber insertion together with

replacement of some of the periodontal ligament space by
interstitial areas and fat cells suggests that the structural
organization of the periodontal ligament degenerates with
age
THANK