Cross Linkimg Theory

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Abstract The crosslinking theory of aging has been gaining acceptance at a steady pace, as evidenced by many independent rediscoveries. While several earlier studies were indicative, none seemed conclusive until it was shown, using Differential Scanning Calorimetry (DSC), that protein from young human brains could be made to closely resemble protein from old brains by exposing it to either of two entirely different crosslinking agents (glutaraldehyde and dipotassium diperoxy sulfate). This work has now been repeated with additional brain material, and a statistically more significant number of determinations. It is now shown that a treatment of brain protein with either one or two chemically totally different compounds which have no property in common except that both are crosslinkers, changes young brain protein so that it greatly resembles old, crosslinked protein. This shows that crosslinking reactions are involved in the age related changes in the studied proteins. Developmental aging and cross-linking were first proposed in 1942 by Johan Bjorksten. He applied this theory to aging diseases such as sclerosis, a declining immune system and the most obvious example of cross-linking, loss of elasticity in the skin. Collagen is one of the most common proteins found in the skin, tendons, ligaments, bone and cartilage. Collagen protein can be compared to the legs of a ladder with very few rungs. Each protein is connected to its neighbors by other rungs forming a cross-link. In young people there are few cross-links and the ladders are free to move up and down. The collagen stays soft and pliable. With age however the number of cross-links increases, causing the skin to shrink and become less soft and pliable. It is thought that these cross-links increases, causing the skin to shrink and become less soft and pliable. It is thought that these cross-links begin to

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