The generation of collagen bers occurs through a complex set of pre-and post­translational steps [9]. Following the synthesis of the preprocollagen alpha chains in the rough endoplasmic reticulum and upon transit through the Golgi complex, the signal peptides are lost, generating procollagen alpha chains. These proteins contain a number of additional non-helical N- and C-terminal propeptides that increase the solubility of the protein in the endoplasmic reticulum and will aid in the formation of the helical structure. Upon Golgi transit, numerous modications will take place, including hydroxylation (e.g. by lysine hydroxylases) and glyco­sylation. These modications allow the procollagen alpha chain proteins to twist upon themselves forming the typical triple helical structure. Next, the resulting procollagen brils are packed in secretory vesicles that trafc along the microtu­bules to the membrane. Upon secretion of the procollagens in the extracellular milieu, procollagen proteases will remove the propeptides, reducing their solubility and generating the so- called tropocollagen. Next, multiple tropocollagens will gather and polymerize into collagen bers under the guidance of oxidation of cer­tain lysine residues by extracellular lysine oxidases, which will eventually place covalent bonds within (intramolecular cross-links) and between the molecules (intermolecular cross-links). This is the critical step that gives the collagen bers tremendous strength. Finally, the bers are stabilized via interactions with non­brillary collagens also referred to as bril-associated collagens with interrupted triple helices (FACIT). The higher order conguration of all collagens is a long rod-like structure, that can be identied by the striated effect under the electron microscope, since the assembly of tropocollagens is such that adjacent molecules are displaced approximately 1/4 of their length. Importantly, scar collagen in adults is not so highly organized and only regains a fraction of its initial strength and elasticity.