An overview of carbohydrate–protein interactions with specific reference to myosin and ageing

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Abstract
Non‐enzymatic glycosylation (glycation), a post‐translational modification of proteins, results from the reaction of proteins with reducing sugars. Glycation is implicated in various pathologies like diabetes, Alzheimer’s disease and it has been suggested to play an important role in the ageing process. Research on protein glycation has primarily studied extracellular proteins such as albumin, haemoglobin and collagen. However, there is increasing evidence that intracellular proteins may also be affected by glycation, and glycation of myosin is reported to decrease myosin ATPase activity. Glycated adducts are detected by various techniques such as chromatography, electrophoresis, fluorescence and immunochemistry. Inhibition or removal of these adducts has been achieved by chemical compounds such as aminoguanidine (amG), β‐mercaptoethanol (bME) and N‐phenacylthiazolium bromide (PTB). In the present pilot study, using a novel in vitro motility assay, we have observed an attenuation in the motility speed of actin (≈13%) on myosin extracted from single muscle fibre segments after 15‐min glucose incubation. Addition of bME to the incubation medium maintained actin motility speed.