Periodontal Ligament Biochemistry Flashcards

1
Q

What cells are in the periodontal ligament

A

Fibroblasts
Cementoblasts
Osteoblasts

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2
Q

What fibres and other things make up the periodontal ligament

A

Nerves and vasculature
Extracellular matrix
Fibres (major is collagen the minor is oxytalan and elastin)
Ground substance

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3
Q

How does elastin for and mature?

A

Oxytalan
Elaunin
Elastin

Elastin protein is deposited in these oxytalan fibres until the mature into elastin

This makes it resemble foetal connective tissue

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4
Q

What is elastin made of

A

10-15 no microfibrils if oxytalan fibre
Microfibrillat component 10%

Amorphous polymeric fore (90%) elastin protein

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5
Q

What is collagen made of (structure)

A

All made of 3 collagen polypeptide (alpha polypeptides)

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6
Q

What is the structure of each polypeptide collagen chain

A

Tripeptide glycine followed by 2 amino acids proline or its hydroxylated form. The third amino acid is alanine

If we looked down the chain we could see the single H side chain faces the middle because there is no steric hinderance here

Every third amino acid proline has its bulky side chain orientated outward this side chain forms H bonds with other things around in the surrounding solution

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7
Q

What collagen types form the PDL

A

Type 1 80%

Type 3 20%

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8
Q

What is the importance of hydroxyproline in the collagen structure

A

Stability in the triple helix through OH group

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9
Q

What happens when hydroxilation of proline is absent

A

Scurvy a connective tissue disease

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10
Q

How is proline converted to hydroxyproline

A

Proline is hydroxilated via a vitamin C dependant enzyme prolyl hydroxalysae. Vitamin C is a reducing agent keeping fe2+ ions mood

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11
Q

How is collagen formed (chains assemble)

A

Alpha chains assemble and are stabilised by S-S bonds at the carboxyl end of the chains then the helix forms spontaneously and the globular end at the N terminus forms

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12
Q

What happens to the procollagen when it leaves the cell to the extracellular matrix

A

The globular ends are cleaved leaving the tropocollagen that can now assemble into fibres

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13
Q

What happens in fibrillogenesis

A

This is the aggregation of tropocollagen to form fibrils intermolecular cross links form

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14
Q

How are the fibrils stabilised

A

Covalent cross links from modified lysine and hydroxylysine residues

Lysyl oxadase converts r groups of LYS and HYL to aldehydes

They are all reducible

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15
Q

What are intramolecular allysine cross links

A

These are formed within the actual tropocollagen molecules

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16
Q

What happens to cross linked as collagen ages.

Is this the same in the PDL

A

More stable non reducible cross links form spontaneously

There are no non reducible cross links in the PDL

17
Q

What is the ration of DHLNL:HLN

A

1:3

18
Q

Giver and overview of collagen synthesis

A
Synthesis of alpha chains 
Hydroxylation of PRO&LYS 
Glycosylation og HYL and ASN
Alignment of pro a chains 
Pro-collagen triple helix 

Outside -
Cleavage if terminal ends
Aggregation stagger array
Formation of intermolecular cross links

19
Q

What is the hierarchical structure of collagen type 1

A
Procollagen 
Tropocollagen 
Microfibrils 
Fibrils 
Fibres 
Fibre bundles
20
Q

How is collagen broken down

A
Collagenase enzyme (matrix metalloprotiase) produced as an inactive precursor it cleaves collagen to 3/4 and 1/4 parts 
In the PDL phagocytosis by fibroblasts is an significant degradation factor
21
Q

What is the collagen synthesis in the PDL and degradation compared to everything else

A

6 times alveolar bone and 4 times skin

Degradation is 15 times what it is in the skin and 6 times what it is in alveolar bone

Approx 40 min cycle in PDL

22
Q

What happens to gelatinise activity in sheep with diseased mouths

A

Greater activity more degradation

23
Q

What does the Western blot of GCF show

A

Collagen only present in GCF in diseased sheep

24
Q

What comprises ground substance

A

Non collagenous proteins
Hyaluronic acid
Proteoglycans
Glycoproteins such as fibronectin and these are protiase resistant

25
Q

Proteoglycans in ground substance

A

Have a protein core and then glycosylaminoglucans (gags)
These are hetropolymers made of repeated disaccharide monomers
GAGs= hexosamine and ironic acid are hydrophilic

26
Q

What is a proteoglycans structure

A

GAG and core protein to for proteoglycans monomer

Proteoglycans + link protein + hyaluronan monomer = proteoglycans aggregate

27
Q

What proteoglycans are in the PDL

A

Decorum and biglycan (small)

Versions (large)

D and V sulphate rich

28
Q

Why are proteoglycans needed in ground substance

A

They control fibrilogenesis via ability to bind collagen
High gag content is associated with unimpdal distribution of small fibrils

Decorin larger fibrils

Proteoglycans also direct orientation of collagen fibrils

Gag in tissue is highest at 2 month

29
Q

What do PGs and GAGs do (2)

A

Control mineralisation they inhibit mineral deposition

Generates the eruption force

30
Q

What happens to sulphate co centration

A
Dermatan - decrease 
Chondroitin - increase 
Decorin increases 
Total gag increases collagen content decreases 
Gelatinise activity increase
31
Q

What are the cells of the periodontium

A

Osteoclasts
Fibroblast
Macrophage
Osteoblasts

32
Q

What’s the secular epethelium

A

Layer of osteoblasts

33
Q

Where are macrophages found

A

In the alveolar bone

34
Q

What do fibroblasts do

A

Degrade and produce collagen in the alveolar bone

35
Q

What’s rankl

A

This is a protein causing osteoblasts to rise and for osteoclasts
Osteoblasts control osteoclasts formation so production and degradation happens at the same rate

36
Q

How does bone change in reaction loading

A

Increased bone when increased loading happens

37
Q

What does LPS do

A

This causes osteoblasts to form Rankl to Christie more osteoclasts and more bone resorption

And on macrophages to for IL 1 which causes osteoblasts to make more osteoclasts

Additionally IL 1 causes fibroblasts to stimulate more IL1 and extracellular collaginases causing net loss off cellular tissue

IL1 causes cathepsin K to increase bone degradation