What, in fact, causes wrinkles on the skin?
The aging skin cells, keratinocytes and fibroblasts, after the changes in protein, they begin to behave abnormally and eventually accumulate in the human skin. They produce more metalloproteinase-like enzymes, that damage proteins in the surrounding extracellular mass (matrix in which there are cells, lymph nodes, blood vessels and other associated skin structures). Moreover, aging causes irreversible damage to the body’s proteins. The underlying mechanism behind this damage is glycation. A simple definition of glycation is the crosslinking of proteins and sugars to form non-functioning structures in the body. The process of glycation can be superficially seen as unsightly wrinkled skin.
The aging cells also produce adhesion molecules that cause thickening of the walls of blood vessels and their stiffness (atherosclerosis). The aging cells produce other additional degradative enzymes and anti-inflammatory cytokines, which act in distant parts of the body (they are transported through the blood). In this way, a relatively small amount of aged cells causes large changes in the function and integrity of the skin. The aging cells accumulate in all organs and tissues where they suffer apoptosis (programmed cell death) and summon the degenerative processes of aging. Moreover, the distortion of microscopic environment by accumulated aging cells can be reason for the increased incidence of malignant disease in older people.
Dr. Leonard Hayflick demonstrated in 1961 that cells can reach a limited number of cell divisions and then lose their ability of division. His well-known experiments have demonstrated that human fibroblasts (connective tissue cells) have the option of sharing (division) 60 to 80 times, fibroblasts of young people 30 to 40 times, and fibroblasts of older people , only 10 to 20 times. Carnosine extends the average life of fibroblasts in cultures, destroys their transformed (mutagenic) shapes and protects against aldehydes. At the same time, carnosine suppresses, at least in laboratory conditions, protein glycation and the formation of harmful cross links of DNA/proteins.