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Collagen
SHASHI KANT CHAUDHARY
JR
DEPT OF PERIODONTOLOGY & ORAL IMPLANTOLOGY
Content
History
Introduction
Structure of collagen
Synthesis
Types
Collagen in periodontium
Clinical significance
Summary
References
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History
Introduction
an
intricate
macromolecules
network
constituting
of
the
Often
referred
to
as
"connective
tissue."
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Collagen
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Structure of collagen
Astbury was the first to suggest a structure for collagen in 1938, which
consisted of a mixture of Trans and Cis peptide units
The same feature was incorporated by Pauling and Corey in the model
proposed by them in 1951 that had three coaxial helices.
Structure
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Glycine, the smallest amino acid, It fits into the restricted spaces where
the three chains of the helix come together.
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Three of these alpha chains are then wound into a righthanded superhelix, forming a rodlike molecule 1.4 nm in
diameter and about 300 nm long.
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Band Spacing
D=670
FIBRIL
13
Hole Zone (0.6D)
MICROFIBRIL
3000 (4.4D)
COLLAGEN
MOLECULE
15 Dia
104
TRIPLE
HELIX
PRIMARY
STRUCTURE
IN -CHAIN
8.7
Glycine
Glycine
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Quarter-Staggered Arrangement
The
tropocollagen
molecules
are
arranged
in
15
'quarter
16
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Synthesis of collagen
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Other Cells
Epithelial cells
Chondroblasts
Endothelial cells
Osteoblasts
Muscle cells
Odontoblasts
Schwann cells
Cementoblasts
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Synthesis of collagen
Hydroxylation
Glycosylation
Cross-link formation
Intracellul
ar
Extracellular
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Gene expression
Type
Genes
Tissue
COL1A1, COL1A2
Most connective
tissues, including bone
II
COL2A1
Cartilage, vitreous
humor
III
COL3A1
Extensible connective
tissues such as skin,
lung, and the vascular
system
IV
COL4A1COL4A6
Basement membranes
COL5A1COL5A3
Minor component in
tissues containing
collagen I
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VI
COL6A1COL6A3
Most connective
tissues
VII
COL7A1
Anchoring fibrils
VIII
COL8A1COL8A2
Endothelium
IX
COL9A1COL9A3
Tissues containing
collagen II
COL10A1
XI
COL11A1,
COL11A2, COL2A1
Hypertrophic
cartilage
Tissues containing
collagen II
XII
COL12A1
Tissues containing
collagen I
XIII
COL13A1
Many tissues
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XIV
COL14A1
Tissues containing
collagen I
XV
COL15A1
Many tissues
XVI
COL16A1
Many tissues
XVII
COL17A1
Skin hemidesmosomes
XVIII
COL18A1
XIX
COL19A1
Rhabdomyosarcoma
cells
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Types
Network-forming
Fibril-associated
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IV
FACIT collagen
VIII and X
VII
VI
Transmembrane collagen
Multiplexin collagen
XV and XVIII
Other collagen
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Fibrillar collagens
Aggregate
in
highly
organized
manner
in
the
extracellular
Collagen fibrils often are composed of more than one type of collagen.
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assemble as fibrils.
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Collagens IX, XII, XIV, XVI, XIX, XX, XXI, and XXII consist of
chains that have different lengths and contain a variety of
noncollagenous domains.
34
Network-forming collagens
35
Anchoring-fibril collagen
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Microfibril-forming collagen
37
Transmembrane collagen
These collagens are transmembrane proteins with extracellular collagenous domains and a
C-terminal noncollagenous domain that functions in cell adhesion.
Type XVII collagen is found in hemidesmosomes of basal epidermal cells and attaches the
cells to the basal lamina.
Type XIII collagen is present in focal adhesion sites of fibroblasts and at cell-matrix interfaces
in some epithelia, muscle, and nerves, also present in the cell-cell adhesive specializations.
These collagens may interact with other cell surface or extracellular matrix molecules to
alter cell behavior.
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Multiplexin (endostatin-forming)
collagens
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Type XVIII collagen is a component of basal lamina of epithelial and endothelial cells
and stabilize structures of the basal lamina.
Type XVIII collagen has multiple interruptions in the central helical domain and a
large, unique C-terminal nonhelical domain.
Type XV collagen has a similar structure and a wider distribution, including the
papillary dermis. However has less potent antiangiogenic activity than type XVIII.
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Other collagens
Type XXVI is found in the extracellular matrix of the testis and ovary
The structure of type XXVIII has some similarities with type IV but the
triple helical domain is longer
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DENTIN COLLAGEN
Type I collagen is the major protein of dentin matrix. Lesser amounts of types III, V, and
VI collagen are also found in dentine and predentine
Demineralized dentine and predentine show closely packed collagen fibers of 20-50nm
Dentinal collagen contains 2-3 fold increase of hydroxylysine compared to that of soft
tissues
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PULPAL COLLAGEN
Initially rich in type III, as matures type I collagen bundles are formed
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Gingival collagen
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Collagen
I
Location
Lamina propria
III
IV
V
Lamina propria
Basement membrane
Subepithelial basement
membrane
VI
VII
Microfibrils
Subepithelial basement
membrane
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PERIODONTAL COLLAGEN
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CEMENTAL COLLAGEN
The major proportion is type I (90%) and type III (about 5%)
collagens
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SHARPEYS FIBERS
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BONE COLLAGEN
Functional adaptation of
collagen
52
This is proved by the atrophy of the alveolar bone that often follows
the removal of the teeth and associated PDL
53
The mineral interface also appears concave and this maximum strength to
the mineral-collagen interface
In case of
periodontal diseases
there is destruction of
PDL , sharpeys
fibers
Due to this teeth is not able to withstand the varying types of mechanical
forces that ultimately leads to tooth mobility
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Areas of hyalinization
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These changes are due to higher cross linking and stabilized forms of
collagen
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COLLAGEN DEGRADATION
EXTRACELLULAR
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Break down of the collagen matrix element is a key component of any normal tissue
that is undergoing morphogenesis and growth
These are specialized enzymes that have evolved specifically to hydrolyze collagens,
because their triple helical collagen structure is resistant to most common proteinases
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MECHANISM OF DEGRADATION
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collagenase
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Stromelysins
Matrilysin(MMP-7)
Metalloelastase(MMP-11)
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Regulation of MMP
Two key regulators are IL-1 and TGF-
COLLAGEN DEGRADATION
INTRACELLULAR
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A.
B.
Formation of phagosome
C.
D.
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Clinical significance
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Collagen disorders
some
of
the
enzymes
or in genes
involved in these
osteogenesis
chondrodysplasias)
imperfecta)
and
cartilage
(eg,
the
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Gene
Diseases
COL1A1, COL1A2
COL2A1
Severe chondrodysplasias
Osteoarthritis
COL3A1
COL4A3COL4A6
COL7A1
COL10A1
Schmid metaphysial
chondrodysplasia
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Enzyme
Disease
Lysyl hydroxylase
Procollagen N -proteinase
Lysyl hydroxylase
Menkes disease
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Due
disease.
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Collagen as membrane
Providing hemostasis,
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Hemostatic Collagen
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Another material commonly used for local drug delivery is Periodontal Plus AB
(EnColl). This product comprises tetracycline fibers impregnated in collagen
fibers, which are available in vials. These brownish-colored fibers are resorbable
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Summary
The various collagens are distinguished by the ability of their helical and nonhelical
regions to associate into fibrils, to form sheets, or to cross-link differentcollagen
types.
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References
Oral Cells And Tissues , Garant P.R , Quintessence Publishing Co,inc ,2003.
Orban`s Oral Histology And Embryology ,Kumar Gs , 12th Edition , 2008, Elsevier Pvt.
Ltd
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Lippincotts Illustrated Reviews: Biochemistry Richard A. Harvey, Denise R. Ferrier, Fifth Edition
2011 Lippincott Williams & Wilkins, A Wolters Kluwer Business
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Thank you
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