Collagen synthesis is extremely complicated. Collagen is initially made as a pre procollagen, which is transported and converted to pro collagen, which is then hydroxylated, glycosylated, wound into a helix and transported again, after which it is clipped into collagen molecules, assembled into collagen fibers, and cross-linked into final form. Each of these steps could be impaired by a host of conditions. For example, the hydroxylation of collagen is dependent on vitamin C, which also serves as an antioxidant. Also, the final crosslinking of collagen depends on the enzyme lysyl oxidase , which uses copper as a cofactor.
Copper is also a component of the over-expressed superoxide dismutase.
These two mechanisms may not be easily separable. The competitive effects between overactive and underactive collagen pathways may induce secondary proline or vitamin C deficiencies. In other words, the overactive collagen pathways may squander scarce resources leaving the underactive pathways starved for raw materials. It is this latter observation that led Dixie Tafoya to try feeding the collagen pathways as a nutritional intervention strategy for her daughter. When she added vitamin C, bioflavonoids, alpha-ketoglutarate and proline, her daughter's connective tissue and ligaments improved markedly.