I |
Triple superhelix composed of two identical α1 and one α2 chain; a form consisting of three α1 chains (homotrimeric) is also found |
Bones, tendons, ligaments, skin, cornea |
Tensile strength of tissues and bone stiffness |
II |
Three identical α1[III]3 chains—homotrimer; similar properties and size to type I, but higher content of hydroxylysine and glucose and galactose residues |
The dominant component of vitreous tissue (approx. 80%), corneal epithelium, and cartilage |
One of the main components of ECM (extracellular matrix), maintains chondrocyte functions, induces cell adhesion and proliferation |
III |
Three identical α1[III]3 chains |
Element of the dermis, liver and lung tissues, spleen and blood vessels |
Gives elasticity to tissues |
V |
Three different chains—heterotrimers |
Bones, skin, placenta, cornea |
Initiation of collagen fibrillogenesis |
XI |
Three different chains—heterotrimers |
Cartilage, intervertebral discs |
Initiation of collagen fibrillogenesis |
XXIV |
The fragment of the Gly-Xaa-Yaa repeated sequence is relatively short, constitutes approximal |
Bones, cornea |
A marker of osteoblast differentiation and bone formation in mice |
XXVII |
Forms non-striated, thread-like structures, unlike other members of the subfamily |
Cartilage |
Deposited mainly in skeletal tissues at the junction of cartilage and bone |