ROLE OF ADVANCED GLYCATION END-PRODUCTS IN AGING COLLAGEN - A SCANNING FORCE MICROSCOPE STUDY

The collagen structure of young and old rats was examined using a scan ning force microscope (SFM). Rat tail tendons of 8- and 24-month-old W istar rats were frayed by two blades and examined using a Nanoscope II I SFM. In the same tendons, the pentosidine concentrations, a marker o f the Maillard reaction, were determined by HPLC. The SFM inspection o f native fibrils produces images of collagen bundles, with parallel fi brils. The diameters of old rat collagen fibrils were large in compari son to the young ones. Moreover, fibrils obtained from old rats exhibi ted the same band interval, while the depth of the gap between two ove rlap zones showed a higher mean value with respect to young collagen. The pentosidine concentration was also higher in the old than in the y oung tendons. In conclusion, in the presence of an increased concentra tion of advanced glycation end products, significant structural altera tions have been observed in old fibrils.