Oral Tissues Flashcards
what is the most abundant protein in the body?
collagens
how many types of collagen is there?
28
what is the most common type of collagen?
Type I (makes up 80-90%)
what is the starting material for mature collagen?
pro-a collagen chains
what is the base unit structure for all collagen?
chains of tightly wound RIGHT turned triple helices
what can be mix and matched to make the different types of collagens?
different combinations of 3 pro-a collagen chains
what is a defining feature of collagen?
33? glycine
13% proline
9% hydroproline
in its repeating tripeptide form
what is special about glycine in the triple helix?
its a small R group and flexible so can form tightly packed, allows helix turns
what is special about proline/hydroproline in the triple helix?
ridged, provides strength
what bonds strengthen and stabilize collagen?
hydrogen and covalent bonds
(hydroxylation)
what is the difference between tropocollagen and procollagen?
pro still has carboxyl terminal extension peptides
tropo has these removed, it is just the triple pro-a helix
what occurs within the post translational modification of prolines and lysine’s
redox reactions that require Vit C as reducing agent
what are proline and lysine reduced to?
4-hydroxyproline residue or 5-hydroxylysine residue
succinate
CO2
what is the only irreversible aspect of scurvy?
bone growth in children
Collagen is a _______
glycoprotein
Most glycoproteins are ______ or _____ linked in collagen, this also includes hydroxylysine
N-linked (Asparagine) or O-linked (Serine or Threonine)
(he said not a test Q)
Covalent attachment of disacharides to hydroxylysine on collagen occurs in these two steps:
first galactose and then glucose
what does glycosylation not effect?
biochemical properties or
immunogenicity
crosslinks in collagen form both within _____ and _______
1 triple helix and between adjacent triple helices
The _____ route predominates in skin, cornea and sclera
allysine
- The ______ route predominates in bone, cartilage,
ligaments and tendons
hydroxyallysine
what is the first step of Biosynthesis of collagens
Pre-pro-α chains are synthesized in rough ER, where signal peptide is cleaved
what is the second step of Biosynthesis of collagens
Prolines and lysines in pro-α chains are hydroxylated
THIS IS VIT C DEPTENDANT STEP
what is the third step of Biosynthesis of collagens
Glycosylation of pro-α chains occurs in the smooth ER
what is the fourth step of Biosynthesis of collagens
- Triple helix-containing procollagen forms inside the Golgi
what is the fifth step of Biosynthesis of collagens
- Cleavage of extension peptides occurs outside the cell, as does assembly of tropocollagen units into collagen fibers
how are fibrillar collagens assembled?
10% extension area, 90% overlap,
this makes strong and lengthens
what is the arrangement of fibrillar collagens in tendons?
Parallel Bundles
what is the arrangement of fibrillar collagens in cartilage?
No regular arrangement; associated with glycosaminoglycans
what is the arrangement of fibrillar collagens in skin?
Planar sheets of microfibrils layered wat many angles
what is the arrangement of fibrillar collagens in cornea?
Planar sheets stacked crossways for strength
what does collagen IX do?
Connects collagens to cells and other matrix components
where is collagen X made
Produced by chondrocytes, required for normal bone growth
where is collagen IV found?
Unique to basement membranes
what collagen pays a roe in muscular dystrophy?
Collagen VI
what does collagen VII do?
epiderma BM to dermal CT
where is transmembrane collagens found?
connective tissue expressing cells
what do multipexins do?
proteoglycans expressed in endothelial and epithelial cell
what are some symptoms of Ehlers Danlos syndrome?
skin hyperelasticisty
fragile tissue
joint hypermobility
what causes osteogenesis imperfecta?
altered collagen type I
(type 1 causes had normal collagen, type II causes fully disrupted collagen)
what is a similarity shared by elastin and collagen?
high in glycine and proline
Covalent bonds provide
strength
what are some differences in Elastin than collagen
- Unlike collagen, no
repeating patterns - Alternating coiled-coil
domains and hydrophobic
domains create elasticity
in elastin fibrils _______ is identical to covalent links found in collagen
Lysinorleucine
_______ results from
identical chemical reactions,
but is unique to elastin
Desmosine
what is Fibrillin
–provides a scaffold for elastin deposition
–forms more rigid microfibrils in tissues where
elastin is not present
what do fibrillin/Elastin microfibrils do?
facilitate flexibility of skin,
ligaments, and blood
vessels.