PROTEOGLYCANS OF PERIODONTIUM

PROTEOGLYCANS
DR.SYED DHASTHAHEER
PG PERIODONTICS

• GENERAL STRUCTURE AND COMPOSITION
GLYCOSAMINOGLYCANS
OLIGOSACCHARIDES
GLYCOPEPTIDE LINKAGE
CORE PROTEINS
• PROTEOGLYCAN SYNTHESIS
• PROTEOGLYCAN TYPES
MATRIX ORGANIZERS AND SPACE FILLERS
CELL SURFACE PROTEOGLYCANS
PROTEOGLYCANS OF HEMATOPOETIC CELLS
• PROTEOGLYCAN FUNCTIONS
• PROTEOGLYCANS OF PERIODONTIUM
• CONCLUSION
CONTENTS

• The term “PROTEOGLYCAN” first introduced in 1967 by Balazs to
describe a family of macromolecules composed of one or more
Glycosaminoglycans covalently bound to a protein core.
• Prior to this, these molecules had been called Protein-Polysaccharide
complexes or Chondro muco proteins
Introduction :
( Balazs et al.,1967 )

Structure of proteoglycans :
PROTEOGLYCANS
GAGS + CORE PROTEIN
( Bartold.,1983 )

Structure of proteoglycans :
(https://biologywise.com/structure-function-of-proteoglycans)

(https://biologywise.com/structure-function-of-proteoglycans)

• Glycosaminoglycans are the Principal carbohydrate component of
Proteoglycans.
Glycosoaminoglycans :
The GAGs extend perpendicularly from
the core in a brush-like structure.
( Franson 1985, Jackson et al.,1991)

.
GAG’S are composed of repeating disaccharide units of
 Uronic acid (either D-Glucuronic acid or L-Iduronic acid) and
 Hexosamine (either D-Glucosamine or D-Galactosamine)
Glycosoaminoglycans have been classified mainly into :
1) Sulfated Glycosoaminoglycans
2) Non- Sulfated Glycosoaminoglycans
 Hyaluronan is the only Non- Sulfated Glycosoaminoglycans.
 Others are sulfated to varying degrees

Chondroitin sulfate:
Composed of repeating disaccharide
units of
 O-Sulfated N-Acetyl -
Galactosamine and
 D-Glucuronic acid
( Meyar k, et al.,1956 )

 Sulfation may occur at either C-4 or C-6 of N-Acetyl Galactosamine moiety.
 Accordingly , the molecule is termed as chondroitin 4 sulfate and chondroitin
6 sulfate
 The 4- and 6- sulfated isomers are widely distributed throughout mammalian
tissues and predominant in cartilage and bone.

Current Term : Chondroitin Sulfate 4
Old Term : Chondroitin Sulfate A
Repeating Period Monosaccharides : D-glucuronic Acid , D-galactosamine
Other Sugars : D-galactose , D-xylose
Acidic Group : Carboxyl , Sulfate
Distribution : Cartilage, Bone, Cornea, Skin, Gingiva,
Blood Vessels, Intervertebral Discs.
Decreases With Age

Current Term : Chondroitin Sulfate 6
Old Term : Chondroitin Sulfate C
Repeating Period Monosaccharides : D-glucuronic Acid , D-galactosamine
Distribution : Cartilage, Bone, Cornea, Skin, Gingiva,
Blood Vessels, Intervertebral Discs.
Increases With Age

Dermatan sulfate:
 It consists of disaccharides units
of N-acetyl galactosamine and
Iduronic acid.
( Malmstorm et al.,1975 )

Very similar to Chondroitin Sulfate except that the glucoronic acid
is replaced by L-Iduronic acid.

 Small portions of D-glucuronic acid have been detected in
hydrosylates of purified dermatan sulfate.
 Widely distributed throughout the mammalian tissues, but occurs
predominantly in fibrous connective tissue such as skin and tendon.

Current Term : Dermatan sulfate
Old Term : Chondroitin Sulfate B
Repeating Period Monosaccharides : L-iduronic acid D-glucuronic Acid ,
D-galactosamine
Distribution : Most connective tissues, especially
fibrous tissue such as skin, ligament,
gingiva, blood vessels .

Heparin and Heparan sulfate :
Heparin and Heparan sulfate consist of
alternating
 Uronic acid(l-iduronic acid and
glucoronic acid) and
 D - Glucosamine residues.

Heparin contains less
glucoronic acid , more N-acetyl
groups and more iduronic acid.
Heparan sulfate contains more
Glucuronic acid , more N-acetyl
groups and less Iduronic acid.
( Lindhal et al.,1977 ) ( Cifonelli et al.,1977 )

Heparin found
Intracellularly(mast cells and
basophils) and Extracellularly
within blood and connective
tissue.
Heparin molecule is strongly
acidic and highly charged.
Heparan sulfate is found
extracellularly in most
mammalian connective
tissues.
Primarily located in basement
membrane, the
microenvironment of cells,
and within cell membrane.

Current Term : Heparan sulfate
Old Term : heparitin sulfate
Repeating Period Monosaccharides : L-iduronic acid D-glucuronic Acid ,
D-glucosamine
Distribution : Basement membranes, cell surfaces,
pericellular environment.

KERATAN SULFATE :
Does not contain any Uronic acid.
Disaccharide units of Keratan
sulphate consist of D -Galactose
and N-Acetylglucosamine both of
which may be variably sulfated at
C-6.
( Franson et al.,1985 )

Contains small amount of D-galactosamine, D- Mannose, L-Fucose, Sialic
Acid.
Keratin Sulfate exist in 2 forms:
KS I → Found mainly in cornea
KS II → Found mainly in skeletal tissues
These 2 forms can be distinguish by their mode of linkage to their respective
proteoglycan core protein.
Keratan Sulfate II contains small amount of N- Acetylgalactosamine and
Sialic acid replacing Mannose in Keratan Sulfate I.

Current Term : keratan sulfate
Old Term : kerato sulfate
Repeating Period Monosaccharides : D-galactose,
D-glucosamine
Other Sugars : D-galactosamine , D-mannose,
L-fucose, Sialic acid
Acidic Group : Sulfate
Distribution : Cornea (keratan sulfate I),
Cartilage (keratdn sulfate 11).
These differ in their linkage to the protein core

HYALURONAN :
Only Non Sulfated GAG
composed of repeating
disaccharide units of
 D-Glucuronic acid and
 N- Acetyl - D - Glucosamine.
(Prehm et al.,1989 )

 Its molecular mass is polydisperse, hyaluronan has the largest
molecular size with an average Mr (Relative Molecular Mars) of
several million.
 Only GAG that does not bind covalently to a protein core to form a
proteoglycan molecule.
 Biosynthesis is also unique:
(Prehm et al.,1989 )

OLIGOSACCHARIDES :
 Smaller Oligosaccharides have been identified in most proteoglycans.
 These components may be bound by either O-glycosidic (or) N-glycosidic
linkages to the proteoglycan core protein.
 O-linked Oligosaccharide are found primarily in chondroitin | dermatan sulfate
- rich portion of proteoglycans.
(Thonar and Sweet ,1977 )

 N-linked types are usually found within the portion of those core
proteins capable of binding to hyaluronan.
 O-linked Oligosaccharides act as a primer for the addition of
keratan sulfate chains on proteoglycans in mature tissues.
(Thonar and Sweet ,1977 )

CORE PROTEINS :
Proteoglycans have very heterogeneous protein contents.
For example, Aggrecan contains 2% and 18% protein while protein
content of decorin may be as high as 50%.
This variability is associated with differences in core protein size and
available sites for Glycosaminoglycan attachment.
Proteoglycan core proteins range in size from 10 to 300 KD with one to
several hundred attached glycosaminoglycan chains.
(Hassel et al,1986 )

Within the Amino Acid sequences of proteoglycan core proteins, several
specific regions have been identified that relate to hydrophilic and globular
domains.
Each of these sequences appear to correlate with a particular proteoglycans
locations supposed function.
There is considerably diversity in the proteoglycan core protein, each
belongs to its own gene family, not genetically related.
(Hassel et al,1986 )

PROTEOGLYCAN SYNTHESIS :
 Initially the protein core is synthesized in the Rough Endoplasmic
Reticulum (RER) with a hydrophobic N - terminal leader sequence that
is removed during ongoing translation of RNA.
 Addition of the Glycosaminoglycan chain only occurs after the specific
glycopeptide linkage has been formed and later modifications to the
GAG chains eventually lead to completion of synthetic process.
 Initiation of Glycosaminoglycan chain elongation occurs through the
sequential addition of sugars that are transported to the Golgi as Uridine
Diphosphate Complexes and are formed in the cytosol of the cell.

 The Xylosyltransferase
preferentially adds xylose onto
Serine residues within the
sequences
Glutamic Acid (Aspartic Acid) -
X - Serine - Glycine
[- Serine - Glycine - Serine -
Glycine - ]n
 After the addition of Xylose, 2
galactose residues are added by 2
different galactosyl transferases to
complete the glycopeptide linkage
sequence.

 The addition of disaccharide repeating
units of uronic acid and hexosamine is
carried out by a battery of Galactosamine
Transferase and glucuronic acid
transferase enzyme.
 In this sequence Glucuronic acid is
added to the second galactose residue in
the linkage sequence.
 During chain elongation, ester sulfate
groups are added by transfer of
Phosphoadenosine Phosphosulfate
(PAPS), utilizing two sulfotransferases
for situation at either the C-4 (or) C-6
position of N - Acetylgalactosamine
residues.

 Dermatan Sulfate undergoes further modification which include
epimerization of glucuronic acid to Iduronic acid and 2-O sulfation of
some of the Iduronic acid residues.
 Heparan Sulfate also undergoes N-deacetylation followed by N-Sulfation
as well as occasional additional sulfation of both the glucosamine and
uronic acid derivatives.

Classification of proteoglycan has been based on their glycosaminoglycan
composition such that proteoglycans proteoglycans were referred to as
 Small dermatan sulfate proteoglycans (or)
 Large aggregating chondroitin sulfate proteoglycans.
It can be still classified into 3 separate groups:
 Matrix Organizers
 Tissue Space Fillers
 Cell Surface Proteoglycans (or) Intracellular Proteoglycans of Hematopoietic
Cells

Large Extracellular Proteoglycans:
1. AGGRECAN is a large proteoglycan
that contains both keratan sulfate and
chondroitin sulfate chains and is able to
form macromolecular aggregates with
hyaluronan.
It is the Archetypal Proteoglycan,
Formerly called large aggregating
chondroitin sulfate proteoglycan,
considered benchmark for all
proteoglycans.
Matrix Organizers :
(Hardingham et al.,1992)

2. VERSICAN
It was originally isolated from
fibroblasts but has since been found to
be present in a wide variety of tissues
including aorta, brain, cartilage,
placenta, tendon as well as skin.
Considered as a large proteoglycan
(Ruoslahti .,1989 )

3. PERLECAN :
Another so called large
proteoglycan composed of 466 KD
protein core to which approximately
3 to 4 heparan sulfate chains are
bound.
This was identified as a
basement - membrane - specific
proteoglycan where it formed
aggregates with type IV collagen and
laminin. Appearance similar to a
chain of pearls. (Noonan.,1991 )

SMALL EXTRACELLULAR PROTEOGLYCANS:
4. LEUCINE RICE - INTERSTITIAL PROTEOGLYCANS - A
group of small proteoglycans with core proteins of around 40 KD, share
homologous leucine - rice core proteins. This includes
 Decorin,
 Biglycan,
 Fibromodulin and
 Lumican
.
(Fisher et al.,1991 )

 Decorin and biglycan have
wide distributions throughout
most tissues.
 Lumican and fibromodulin
have similar core proteins but
substituted with Keratan sulfate
rather than dermatan sulfate,
found in Tendon, Cartilage,
Cornea and Heart-valve tissues

CELL SURFACE PROTEOGLYCANS:
Proteoglycans may be associated with cell membranes via 3 separate
mechanisms:
1) As an integral membrane protein spanning the lipid bilayer.
2) Partial insertion into lipid bilayer of a phosphatidylinositol
component of the proteoglycan.
3) Binding of GAG side chain to specific plasma membrane
receptors.
(Gallagher.et al.,1989)

SYNDECANS:
 The Syndecans are a family of related proteoglycan whose protein core
span plasma membrane of mammalian cells.
 Unique protein core composed of both hydrophobic and hydrophilic
domains.
 They may be substituted with Heparan sulfate chondroitin sulfate (or) both.
SYNDECAN - 1:
Considered the Archetypal Syndecan.
Associated with variety of cells including lymphocytes, embryonic dental
mesenchyme and embryonic lung mesenchyme.
( Bernfield et al.,1992 )
( Saunders et al.,1989 )

SYNDECAN - 2:
 Also known as Fibro Glycan.
 First isolated from the cell surface of fibroblast and identified as a
heparan sulfate containing proteoglycan with a core - protein of 20
KD.
SYNDECAN - 3:
 Also know as N - Syndecan.
 Isolated simultaneously from both Neural and cartilage tissues.
 Syndecan - 3 is expressed is high amounts during chondrogenesis.
( Marynen et al.,1989 )
( Carey et al.,1992 )

SYNDECAN - 4:
Also known as Ryudo Can (or) Amphi Glycan.
These proteoglycans have three putative Glycosaminoglycan attachment sites
and a core protein of 20 KD.
( Kojima et al.,1992 )

CD44:
Very broad class of transmembrane glycoproteins expressed in the cell
surfaces of epithelial, mesenchymal and hematopoietic cell and exist in both a
(or) Non proteoglycan form in which there is no GAG substitution.
GLYPICANS:
A group of Glycosylphosphatidylinositol - anchored cell surface
heparan sulfate proteoglycans.
BETAGLYCAN:
Formerly known as Type III TGF 𝛃 - receptor is a membrane anchored
proteoglycan that binds TGF - 𝛃 via its core protein.
Found in most cells and tissues, particularly abundant in Bone and
Osteoblastic cells.
( David et al.,1990 )
( Andres et al.,1989 )

PROTEOGLYCANS OF HEMATOPOIETIC CELLS:
 New breed of proteoglycans identified within hematopoietic cells.
 Found in Secretory granules and was distinct from those proteoglycans
residing in matrix (or) cell surface. This proteoglycan was named as
serglycin.
SERGLYCIN:
 Major secretory granule proteoglycan.
 First identified in Mast cells and so named because of unique, large,
repeat sequence of serine and glycine residues in its protein core.
 Identified in the secretory granules of mast cells, basophils,
neutrophils, platelets, lymphocytes and natural killer cells
( Kolset et al.,1990 )
( Stephens et al.,1987 )

 Proteoglycans are large, highly anionic glycoproteins ubiquitous to all connective
tissues.
 They are located within the matrix as Integral components of the matrix structure,
as well as on cell surface and within cell organelle.
 Variety of functions including tissue hydration, regulation of collagen fiber
formation, growth factor binding, cell adhesion.

 The extracellular matrix proteoglycans and tissue - organizing
proteoglycans are principally associated with conferring
physicochemical properties to the tissues.
 Large proteoglycans such as Aggrecan and Versican serves to maintain
tissue hydration.
 The smaller extracellular matrix proteoglycans such as decorin and
Fibromodulin serve important functions in binding to other matrix
molecules such as collagens, serving either to aid fibrillogenesis or to act
as bridging molecules between various tissue elements.

 The cell surface proteoglycans such as Syndecans, Thrombomodulin, CD44
provide the necessary means for cells to attach to their matrix, in doing so, the
cells are able to communicate with the matrix, providing important feedback
to the cell regarding its immediate milieu.
 The intracellular proteoglycans of hematopoietic cells, important in enzyme
packaging in order to prevent non-specific enzymatic activity (or) autolysis of
cell.
 Cell surface proteoglycans such as syndecan, and matrix proteoglycan such as
decorin and betaglycan have ability to bind and regulate growth factor
activity.

Extracellular and
pericellular
proteoglycans
Physicochemical
properties
Matrix assembly
Cell mediated
effects
Cell surface
proteoglycans
Osmotic swelling
pressure
Viscoelastic properties
Steric hinderance
Glycoprotein binding
Collagen fibrillogenesis
Regulation of mineralization
Cell substrate adhesion
Cell migration
Cell proliferation
Cell differentiation
( Burcovitz’s PDL health and diseases)

PROTEOGLYCANS OF THE
PERIODONTIUM

1. HEALTHY GINGIVA:
 Gingival tissue contains a variety of noncollagenous glycoproteins and
proteoglycans, some of which have been partially characterized (Narayanan
and Page, 1983; Bartold, 1987)
 Ciano and Mather (1971) were the first to demonstrate the presence of
glycosaminoglycans in human gingival tissue using biochemical methods.

Glycosaminoglycans Distribution Molecular weight
EPI C.T EPI C.T
Hyalunoric Acid 5% 15% 860000 360000
Heparan Sulfate 60% 7% 12300 15000
Dermatan
Sulfate
15% 60% 27000 25000
Chondroitin
Sulfate
20% 15% 25000 21000
 Chondroitin - 4 - Sulfate + Dermatan Sulfate + Hyaluronic
Acid + Heparan Sulfate

GINGIVAL EPITHELIUM :
 In gingival epithelium GAG’s were specifically identified as hyaluronic
acid, heparin sulfate, dermatan sulfate and chondroitin sulfate 4.
 The predominant species was heparan sulfate which accounted for 60%
of the total glycosaminoglycans.
 Heparan sulfate, which is a recognized cell surface macromolecule, also
demonstrates self-aggregation and may be implicated functionally in
cell-cell contact and interactions
( Garrant oral cells and tissues)

 Quantitatively, Dermatan sulfate proteoglycans are characteristic components
in fibrous connective tissues, accounting for 60% of the total
glycosaminogolycans.
 Heparan sulfate is a minor component comprising only 5%, while hyaluronic
acid and chondroitin sulfate account for the remaining 35%.
 . Thus, self-aggregation of the glycosaminoglycan chains could play a
functional role in fiber alignment, assuming the proteoglycans are bound to
the collagen via their protein core
GINGIVAL CONNECTIVE TISSUES :

 Within the gingival tissues, dermatan sulfate appears to be associated with
collagen fibers and it is prevalent at the epithelial connective tissue interface
while heparan sulfate is found primarily in basement membranes of epithelium
and capillary endothelium.
 Decorin, biglycan, versican, syndecan, CD-44 and perlecan have been
identified within gingival tissues.
 Decorin is closely associated with bundles of collagen fibers, especially in the
subepithelial region, while biglycan, which is a relatively minor constituent of
gingiva, is found in filament-like structures in the matrix near the oral
epithelium.

 Decorin , biglycan , and versican are Extracellular proteoglycans have an
organizing role in the formation of collagen fibrils.
 Dermatan sulfate and chondroitin sulfate side chains appear to interconnect
collagen fibrils of the gingiva.
 Dermatan sulfate (decorin) has been localized at the D-band of collagen fibers
in the supra-alveolar fiber apparatus provides stability to the collagen fibers.

2. INFLAMED GINGIVA:
 A decrease in total GAG in inflamed human gingiva was noted.
 Structural studies on the proteoglycans of inflamed gingival tissue
demonstrate evidence of catabolism of the core protein leaving the
glycosaminoglycan chains relatively intact which lead to a loss of
molecular structural integrity
 Heparan sulfate proteoglycan plays an important role in forming adhesive
bonds on plasma fibronectin while hyaluronic acid and chondroitin
sulfate permit cell detachment.
( Bartold et al.,1996 )

 The gingival proteoglycans however manifest fewer changes with
inflammation leading to a decrease in dermatan sulfate and increase in
chondroitin sulfate, and degradation of their proteoglycan core proteins and
hyaluronic acid.
 Degradation of protein core and hyalunoric acid are the characteristics features
of inflamed gingival connective tissues.
 Proteoglycans are lost from inflammatory foci but appears to increase in
concentration around the periphery.
 Inflammatory cells also synthesize proteoglycans containing chondroitin
sulfate later it destroys with collagen.

3. HYPERPLASTIC GINGIVA:
 An extreme form of fibrotic overgrowth is noted in a proportions of
patient being treated for epilepsy with phenytoin.
 When the collagens of phenytoin hyperplastic gingiva were
demonstrated to be present in normal quantities and ratios.
 When the noncollagenous component of hyperplastic gingiva is
demonstrated and it is 2 fold increase over normal gingiva.
 Principle component found to be proteoglycans. This apparent increase
in proteoglycan represents increased synthesis of proteoglycan or
increased degradation of other components remains to be established.

4. PERIODONTAL LIGAMENT:
 The proteoglycans of periodontal ligament have received less attention
than gingiva
 These components should play 2 important rules:
 Due to their highly hydrophilic nature it is expected to be
instrumental in rehydration of ligament following water
displacement as a result of compressive forces of mastication.
 The highly collagenous nature of the ligament would lend
itself to Intricate Interrelationships with proteoglycans
( Gillard et al.,1979 )

 The presence of hyaluronic acid, heparan sulfate, dermatan sulfate and
chondroitin sulfates 4 and 6 was confirmed.
Two major proteoglycan species in periodontal ligament
 Dermatan Sulfate proteoglycan
 Hybrid chondroitin sulfate - dermatan sulfate proteoglycan
Dermatan sulfate was determined to be the Principal glycosaminoglycan
of this tissue, a finding consistent with its highly fibrous nature
( Pearson et al.,1975 )

.
The chondroitin sulfate fraction is believed to occupy spaces between collagen
fibers and to be in part responsible for generating the tissue osmotic pressure
of the PDL.
 The chondroitin Sulfate-rich proteoglycans of the PDL may play an essential
role in absorbing compressive Shocks and thereby protect the cells of the
ligament from damage during occlusal contact.
 Ultrastructural studies of the distribution of glycosaminoglycans in the PDL
suggest that they are associated with the surface of collagen flbrils.

 Hyaluronic acid Because of its large size and polyanionic nature, It occupies a
large hydrated domain in the extracellular Space.
 As a result of its high negative charge and large volume, hyaluronic acid
regulates the permeability of the extracellular environment to other
molecules..
 Tissues rich in hyaluronic acid provide Pathways of cell migration during
embryogenesis.
 As Development progresses, the concentration of hyaluronic Acid in the PDL
decreases and the levels of Dermatan sulfate- and chondroitin sulfate-rich
proteoglycans increases. ( Garrant oral cells and tissues)

 The proteoglycans exert a swelling pressure entrapped within the collagen
matrix.
 External pressure is applied to a tissue will result in loss of fluid , increasing
the effective swelling pressure as proteoglycans concentration increases
fluid loss is restored once the external load is removed ,and the fluid flow
and the maintainance of a hydrated state is controlled by proteoglycans.
 Proteoglycans are heavily involved in maintaining the structural integrity of
connective tissues.
( Burcovitz’s PDL health and diseases)

5. CEMENTUM :
 In cementum, GAG’s components present are hyaluronan, dermantan
sulfate, chondroitin sulfate and keratin sulfate.
 These are found to be present almost exclusively in precementum and
precementocyte lacunae.
 These findings suggest that proteoglycans plays an important role
formation of the mineralized matrix of the cementum.

5. BONE :
 The Glycosaminoglycans of cortical bone reveals that Chondroitin
Sulfate - 4 is the principal species present.
 Hyaluronic Acid, Chondroitin Sulfate - 6, Dermatan Sulfate and Keratan
Sulfate being minor component.
 The arrangement is different to that seen in soft connective tissues or
cartilage in that the interfibrillar proteoglycan filaments are orientated
parallel to the fibril axis.
( Herring et al.,1963 )

 Therefore, it has been postulated that these proteoglycans and their unique
spatial interaction with the collagens may be involved in the mineralization
of bone matrix
 The noncollagenous proteins function in bone matrix mineralization, cellular
adhesion, and regulation of bone cell activity during coupling of bone
formation and resorption.
 Two proteoglycans found in most connective tissues, biglycan and decorin,
are also contained in bone rnatrix
( Scott et al.,1985 )

6. EPITHELIALATTACHMENT:
 Thonard & Scherp first established the presence of glycosaminoglycans in
gingival epithelium.
 Glycosaminoglycans was found in gingival epithelium and later demonstrated
in Junctional Epithelium.Associated with reattachment of epithelium to the
tooth surface following surgery.(cimasoni et al, 1963)
 Proteoglycans in this region plays an intricate role in the defense of tissues
against onset of periodontal disease. (pearson et al,1975)
 Heparan sulphate is the predominant gingival epithelial glycosaminoglycan
further imply the possibility of complex molecular interactions and
arrangements occurring within the extracellular matrix of gingival epithelium

.
 Such putative molecular inter-relationships of the
epithelial extracellular matrix are presumed to act as a
“first-line” defence mechanism against the initiation
of periodontal disease by specifically regulating
extraneous molecular penetration of potential irritants
through the junctional and sulcular epithelium.
 The role of proteases in the degradation of
proteoglycans is well established it appears that
gingival proteoglycans are initially degraded by
proteases
( Pollanen et al, 2003 )

7. SULCULAR FLUID:
 Fluid collected from non-inflamed sites contains only hyaluronic acid .
 From Inflammatory sites contains, in addition to hyaluronic acid, dermatan
sulfate, chondroitin sulfate and an unidentified GAG component
.
 The potential exists for correlating these findings with gingival/periodontal
inflammation.
( Embery et al.,1982 )

 Perhaps of even more significance is the preliminary
observation by this group that keratan sulfate is a component of
alveolar bone proteoglycans.
 If this is confirmed then the possibility of using the presence of
this glycosaminoglycan in sulcular fluid as a marker of active
bone destruction is evocative, since keratin sulfate is not a
component of gingival soft tissues.

Proteoglycan play an important role in the regulation of cellular behaviour
and maintenance of tissue integrity and thus an understanding of their
properties is vital to our perception of biology of periodontium.
Conclusion :

 Biology of Periodontal Connective Tissues P. Mark Bartold, A. Sampath
Narayanan
 Garant, Philias R. Oral Cells and Tissues. Quintessence Pub. Co, 2003.
 Berkovitz, Barry K., et al. The Periodontal Ligament in Health and Disease.
Mosby-Wolofe, 1995.
 Proteoglycans of the Periodontium: Structure, Role and Function Bartold PM
Periodontal Res 1987 : 22 : 431-444
 Bartold PM, Wiebkin OW, Thonard JC.1983. Proteoglycans of human gingival
epithelium and connective tissue. Biochem J 211: 119.
REFERENCES

• Narayanan, A. Sampath, and P. Mark Bartold. "Biochemistry of periodontal
connective tissues and their regeneration: a current perspective." Connective
tissue research 34.3 (1996): 191-201.
• Bartold PM, Wiebkin OW, Thonard JC. 1981. Glycosaminoglycans of human
gingival epithelium and connective tissue. Connect Tiss Res 9: 99.
• Bartold PM, Page RC. 1986. The effect of inflammation on proteoglycans
synthesized by human gingival fibroblasts. In Virro 22: 407
• Rahemtulla, Firoz. "Proteoglycans of oral tissues." Critical Reviews in Oral
Biology & Medicine 3.1 (1992): 135-162.

• Bartold, P. M., O. W. Wiebkin, and J. C. Thonard. "The active role of
gingival proteoglycans in periodontal disease." Medical hypotheses 12.4
(1983): 377-387.
• Suchetha A,1 Koduru Sravani Glance into proteins present in periodontal
tissues-a review annals of dental specialty vol. 2; issue 4. Oct – dec 2014

PROTEOGLYCANS OF PERIODONTIUM

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