Distinct Characteristics of Mandibular Bone Collagen Relative to Long Bone Collagen: Relevance to Clinical Dentistry
Figure 2
Diagram of the formation and maturation of the major collagen crosslink in mineralized tissues. The procollagen molecule secreted from the cell is processed by cleavages of both the N- and C-terminal propeptide extensions. The processed collagen molecules then self-assemble through clusters of charge and hydrophobicity of the triple helical domain of the molecule to form a fibril. The molecules in the fibril are then stabilized by extensive intermolecular crosslinking. The crosslink involves the at the residue on the C-telopeptide domain of the two α1 chains and the Hyl at the 87 residue on the triple helical domain of the two α1 chains or the single α1 and α2 chains. The immature crosslink, deH-DHLNL, is formed by pairing of the with the Hyl of the neighboring molecule. The mature crosslink, Pyr, is then formed; it owes its origin to the two of α1 chains and the one Hyl of α1 or α2 chain. If the 87th residue on the helical domain is Lys, the minor immature crosslink, deH-HLNL, is formed, and then the minor immature crosslink, d-Pyr, is made up. The solid and dotted lines represent α1 and α2 chains, respectively. : the aldehyde form of Hyl; HEL: the helical domain; TELO: the telopeptide domain; N: N-terminal telopeptide domain; C16: the residue on the C-telopeptide domain; 87: the 87th residue on the helical domain.
