Comparative Studies of Age Tests on Collagen Fibres

M, Boros-Farkas; Everitt, Arthur V.

doi:10.1159/000211572

Cited by 32 publications

(7 citation statements)

References 4 publications

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“…To a 5 cm long fibre a large w'eight of 5 g was tied w hich completely inhibited any shortening. By isometric thermal denaturation the fibre evolves a large tension without shortening, as was registered in tensimeters in former experiments [2,3,4]. The maximal tension is 4-5 g for the 10-to 15-month-old animals.…”

mentioning

confidence: 56%

Electronmicroscopic Analysis of Thermal Collagen Denaturation in Rat Tail Tendons

Verzár

Iz²

1970

Gerontology

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mentioning

confidence: 56%

Electronmicroscopic Analysis of Thermal Collagen Denaturation in Rat Tail Tendons

Verzár

Iz²

1970

Gerontology

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“…The stability of rat tail tendons was studied by measuring the breaking time in 7 mol/1 urea at 40 ~ using a modified method described by Boros-Farkas and Everitt [15]. Briefly, single tendons were pulled out from the tail, wrapped quickly in parafilm, and the…”

Section: Stability Of Rat Tail Tendon Collagenmentioning

confidence: 99%

Aminoguanidine treatment reduces the increase in collagen stability of rats with experimental diabetes mellitus

Oxlund

Andreassen

1992

Diabetologia

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Alterations in the biophysical properties of connective tissues in diabetes mellitus have been attributed to the nonenzymatic glycation of the collagens and the subsequent formation of browning products, cross-linking the proteins. Aminoguanidine may bind to carbonyl groups of these nonenzymatic glycation products and thereby block the process. Rats with streptozotocin-induced diabetes were treated with aminoguanidine, 25 mg.kg-1.day-1, for 120 days. The aminoguanidine treatment did not counteract the increase in blood glucose concentrations, nor did it prevent the arrest in weight gain of diabetic rats. The increased stability in 7 mol/l urea and increased tensile strength of tail tendons from the diabetic rats, however, were prevented by the aminoguanidine treatment. Aminoguanidine did not reduce the formation of early nonenzymatic glycation products (aldimine and Amadori rearrangement products), whereas the amount of browning products (fluorescent compounds) was reduced in the tail tendon collagen of the diabetic rats. Aminoguanidine treatment of intact rats did not influence these parameters. These findings indicate that the biophysical alterations of collagens induced by experimental diabetes are caused by cross-links derived from the nonenzymatic glycation, and furthermore, that aminoguanidine treatment may prevent the concomitant changes in biophysical properties of connective tissues.

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“…Thermal stability was assessed by measuring the thermal rupture time of collagen fibres in urea (7 mol/l) at 40 ~ using a technique modified from Boros-Farkas and Everitt [14]. After sacrifice, intact tendons were serially removed from the tail with bone crushers, dried in air on filter paper, and subsequently stored at -4 ~ until required.…”

Section: Assessment Of Thermal Stability Of Collagenmentioning

confidence: 99%

The Thermal stability of collagen in diabetic rats: correlation with severity of diabetes and non-enzymatic glycosylation

et al. 1983

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The thermal stability of collagen fibres from rat tail tendon was studied in both normal and diabetic rats. Results were correlated with the age of the animals, glycosylated haemoglobin level and the degree of non-enzymatic glycosylation of the collagen. Age was found to be the most important single determinant of the thermal rupture time of collagen fibres (r = 0,87, p less than 0.005). Thermal rupture time was also increased in diabetes and showed good correlation with glycosylated haemoglobin (r = 0.69, p less than 0.005) and non-enzymatic glycosylation of collagen (r = 0.51, p less than 0.005). The correlation of glycosylated haemoglobin level and thermal rupture time was significant, independent of age and non-enzymatic glycosylation of collagen. Experiments in vitro showed that incubation of collagen fibres with glucose increased the thermal stability of collagen. These results demonstrated an independent effect of severity of diabetes on the physical properties of collagen. The role of non-enzymatic glycosylation in causing the changes in collagen properties in diabetes remains to be fully elucidated.

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Comparative Studies of Age Tests on Collagen Fibres

Cited by 32 publications

References 4 publications

Electronmicroscopic Analysis of Thermal Collagen Denaturation in Rat Tail Tendons

Electronmicroscopic Analysis of Thermal Collagen Denaturation in Rat Tail Tendons

Aminoguanidine treatment reduces the increase in collagen stability of rats with experimental diabetes mellitus

The Thermal stability of collagen in diabetic rats: correlation with severity of diabetes and non-enzymatic glycosylation

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