Effect of “in vitro” induced glycation on thermostability of bone tissue

Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues

“…A better organization of the collagen helices and/ or homogeneity of fibres in ribosylated samples can be presumed also from the narrower denaturation endotherms, though the change of DT 1/2 was insignificant in meniscus and in young adult cornea (Tables 2-4). Stabilizing effects of glycation were also shown in other DSC studies in tendon [20,303], skin [20,55], lens capsules [56] and bone [25].…”

“…The main macromolecule of extracellular matrix in these tissues is type I collagen, even though the other components and the structure of the matrix are different [35][36][37]. Collagen in tissues was frequently characterized in the terms of thermal denaturation parameters [24][25][26][27][28][29][30][31][32], and in particular, differences in temperature of denaturation were used as an Table 2 Parameters of thermal denaturation of cornea from young adult (Y-) and ageing (A-) rabbits incubated in ribose solution (-R) and in buffer (-B) Mean values (standard deviation) are listed; n = 6 in each group p values for significance of differences between -B and -R samples calculated from paired t test Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues 1907 indicator of differences in collagen crosslinking on the basis of numerous reports from previous experiments [17,18,20,21,25,27,38]. The temperature of denaturation in corneal samples was not different between young mature (Y-C) and ageing (A-C) groups (Table 1).…”

“…Parameters of thermal denaturation are also very sensitive to hydration of collagen fibres [22][23][24]. The thermal studies of collagens were conducted using model collagen-like peptides [14], collagens extracted from tissues [17,18,22,23,25] and on tissue collagens in situ [24][25][26][27][28][29][30][31][32]. Tissues from musculoskeletal system were the most frequently examined [24-26, 28, 29, 32], and thermal parameters of collagen denaturation were shown to be related to different types of the tissues disorders.…”

“…Effects of glycation on collagen were studied by means of various in vitro models which try to mimic structural changes of fibrils and to evaluate their effects on tissue properties [20,21,25,33]. An issue still discussed is whether stabilization of collagen fibres by AGEs formation resulting from an excess of sugars follows a similar pattern as that seen in normal ageing [10][11][12]21].…”

Effects of Asn-33 glycosylation on the thermostability ofThermomyces lanuginosuslipase

“…For example, thermodynamics of collagen conformations was affected by glycation which significantly increased the denaturation temperature by 3–4°C (Trebacz et al . ). After 1 h incubation at 50°C, a vacuolar invertase from Solanum lycopersicum (TIV‐1) retained its full activity, while nonglycosylated variants retained about 50% of their activity (Tauzin et al .…”