The focus of our laboratory is to elucidate the molecular mechanisms by which the aging process leads to impairment of protein function. In particular we are interested in the structure and biological role of protein modifications by reducing sugars (Advanced Glycation Endproducts/Maillard reaction) and reactive oxygen species. These reactions are dramatically accelerated in diabetes, in patients with end stage renal disease and atherosclerosis, and during the formation of cataracts. The structure of the modified proteins is analyzed by mass-spectrometry, whereby particular emphasis is being placed on the structure of glycated lens crystallins as well collagen crosslinks which increase with age and are responsible for the progressive stiffening of aging vessels. Using an approach based on molecular biology, we are seeking to find novel microbial enzymes that can degrade glycated proteins and specifically regenerate the native protein. We are currently developing transgenic animal models of accelerated aging based on overexpression of the human vitamin C transporter into the lens, and the knocking out of glutathione synthesis, i.e. a key defense against aging. We are also developing novel animal models of accelerated collagen crosslinking.
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