As we age the production of tropocollagen chains (when they twist into helices and finally fibrils) begins to decrease about 1.0% - 1.7% per year from about the 25th year of life. The foremost problem is rather "defective" service of collagen. So-called collagen filtration, or cross-weaved formations, advance resulting in increasing stiff and brittle collagen fibers. Collagen fibers decrease in number and in a precise level of organisation and density. This leads to a decreased level of active fibroblasts, which also create elastin, a sister protein of collagen responsible for the elasticity of the connective tissue.

Collagen synthesis is also enabled by vitamin C and is responsible for its production at every step. In-vitro studies have shown that prolonged exposure of cultures of connective tissue cells to ascorbate or ascorbic acid (vitamin C) induced an eight-fold increase in the synthesis of collagen. It assists in the formation of the polypeptide chains of procollagen. So in essence vitamin C is considered a "co-factor" in the production of collagen.

Interestingly, it is the body's own stress hormone Cortisol (hyrdocortisone) that causes the degradation of collagen in tissue into amino acids. Cortisol-induced collagen loss in the skin is ten times greater than in any other tissue.