fibrillar collagen location
abundant in bone, tendon and skin
fibrillar collagen properties
fibrous, inelastic, high tensile strength
how do fibrillar collagens exhibit high tensile strength
staggered array; successive layers formed ar right angles so resist force in all directions
structure of fibrillar collagen
3 a chains in a left-handed stiff triple helix: glycine (small)-x (proline)-y (hydroxyproline)
type I a chain structure
2 same chain, 1 different chain
type II and III a chain structure
all same a chain
a chain to collagen fibre
IC: a chain → triple helix → EC: collagen fibril → collagen fibre
fibrillar collagen biosynthesis: precursor, location, process
synthesised from procollagen in endoplasmic reticulum by hydroxylation
process of fibrillar collagen biosynthesis
procollagen (N and C-terminal propeptides not present in triple helices) → collagen (N and C-terminals removed EC) → fibrils (cross-linking)
what does hydroxylation contribute to
interchain hydrogen bonding, modifying covalent cross-links
what enzymes catalyse hydroxylation
polyl and lysyl hydroxylases
what prosthetic groups do these enzymes require
vitamin C and Fe2+
consequences of absence of these prosthetic groups
tissue instability leading to scurvy
fibril-associated collagen: type IX and XIII function
regulate fibril organisation and size
fibril-associated collagen: type IV function
forms sheet-like network in basal lamina