Alterations of biochemical and biomechanical properties of rat tail tendons caused by non-enzymatic glycation and their inhibition by dibasic amino acids arginine and lysine

Menzel, E. J.; Reihsner, R.

doi:10.1007/bf00404018

Cited by 54 publications

(29 citation statements)

References 30 publications

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“…However, this study did not evaluate changes in short-term diabetic patients. If we consider several reports that have shown that soft tissues exposed to a hyperglycaemic environment are stiffer [10], both our study and that of Salsich et al had unexpected findings. The latter [3], in an effort to find a solution to the contradiction between their study and reports of increased connective tissue stiffness in previous studies, proposed that structures containing collagen within the muscle tendon unit (perimysium, endomysium) contribute to passive stiffness, mostly at the end range of movement, and that within the physiological range of muscle length change, passive stiffness can be attributed to structures within the myofibril (e.g.…”

Section: Discussionsupporting

confidence: 58%

Abnormal viscoelastic behaviour of passive ankle joint movement in diabetic patients: an early or a late complication?

et al. 2005

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Aims/hypothesis: The goal of the present study was to compare the range of motion and both the viscous and elastic components of passive ankle joint movement in short-and long-term diabetic patients with that of a control population. Methods: Thirty-four diabetic patients and 16 control subjects entered into the study. Patients with a history of over 15 years of diabetes were considered as a longterm diabetic group. In order to quantify the passive ankle joint movement, a device was designed to measure the dorsi-and plantar-flexion angle and the net moment at the ankle. Elastic behaviour was examined as the separate slope of regression lines (stiffness) of plantar and dorsal components in the loading moment-angle curve. It was also examined as the slope of the regression line in the final 10% of each component. Hysteresis, a characteristic of viscoelastic materials that indicates loss of energy during unloading, was corrected for range of motion and used to examine viscous behaviour of the ankle joint. Results: Total and plantar ranges of motion were significantly lower in longterm diabetic patients than in short-term diabetic and control groups (p<0.05). Plantar-flexion stiffness was significantly lower in short-term diabetic patients than in control subjects and long-term diabetic groups (p<0.05). Corrected hysteresis was significantly higher in long-term diabetic than in short-term diabetic and control (p<0.05) groups in the dorsal range of motion. Conclusions/interpretation: This study shows that both decreased plantar and total ankle joint ranges of motion, and increased viscous component of passive ankle joint movement are among the late complications of diabetes.

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Section: Discussionsupporting

confidence: 58%

Abnormal viscoelastic behaviour of passive ankle joint movement in diabetic patients: an early or a late complication?

et al. 2005

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“…Further studies by the same investigators demonstrated that exogenous administration of D -lysine to streptozotocin-diabetic rats inhibited nonenzymatic glycation of Hb, serum albumin, and lens proteins [23]. Similar to D -lysine, L -lysine has also been reported to inhibit nonenzymatic glycation of plasma proteins [14]and nonenzymatic glycation-induced biomechanical properties of rat tail tendon fibers [20]. The observed prevention of a rise in glycosylated HbA 1 and glycation of GBM collagen by early institution of L -lysine is consistent with the above data.…”

Section: Discussionmentioning

confidence: 99%

“…These include acetylsalicylic acid [12, 13, 14, 15, 16, 17, 18, 19], L -lysine [14, 20], D -lysine [21, 22, 23], L -arginine [24], vitamin C [20, 25, 26, 27, 28, 29], vitamin E [30], bendazac [31], and aminoguanidine [4, 5, 6, 7, 8, 9, 10, 32, 33]. Other novel therapeutic agents have been shown to improve albuminuria and mesangial expansion in diabetic mice [34, 35]and rats [36], with type 2 diabetes melllitus.…”

Section: Introductionmentioning

confidence: 99%

<i>L</i>-Lysine Reduces Nonenzymatic Glycation of Glomerular Basement Membrane Collagen and Albuminuria in Diabetic Rats

Jyothirmayi¹,

Modak²,

Reddi³

2001

Nephron

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In this study, we examined the hypothesis whether exogenous administration of L-lysine in drinking water would reduce nonenzymatic glycation of glomerular basement membrane (GBM) collagen and thus albuminuria in streptozotocin-diabetic rats. The rationale is that the administered lysine would combine with the circulating glucose and make it unavailable to react with Ε-amino groups of lysine of various proteins in these diabetic rats. Lysine (0.1%) was given to diabetic rats 7 days (early treatment) or 90 days (late treatment) after induction of hyperglycemia. The treatment was continued for 60 days. Diabetic rats had significantly higher glucose, glycosylated HbA₁, kidney weight, nonenzymatic glycation of GBM collagen, albuminuria, and systolic blood pressure than normal rats. Early treatment with lysine prevented the rise in glycosylated HbA₁ (normal 6.98 ± 0.71% vs. diabetic – early treatment – 7.78 ± 1.50%; p = NS), reduced glycosylation of GBM collagen by 86%, and significantly improved albuminuria. There was no significant effect on plasma glucose and systolic blood pressure. However, late treatment reduced the glycosylation of GBM collagen by 46% with a significant improvement in albuminuria. Plasma creatinine levels were not different between normal and untreated diabetic or lysine-treated diabetic rats; however, the creatinine clearance was significantly higher in all groups of diabetic rats (normal 0.45 ± 0.09 vs. diabetic 2.02 ± 0.39 ml/min; p < 0.001). The data suggest that early rather than late treatment is more beneficial in reducing nonenzymatic glycation of collagen, although both treatments significantly reduced albuminuria. There was no nephrotoxicity as assessed by plasma creatinine levels or creatinine clearances. These beneficial effects occurred independent of changes either in blood pressure or plasma insulin concentration.

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“…Glycation can affect collagen in a number of ways: its ability to form precise supramolecular aggregates, the alterations in its charge profile, defects in the 143 144 G. K. REDDY formation of its fibrils, and hence its interaction with cells. In addition to the occurrence of biochemical and morphological manifestations, glycation has been shown to alter the biomechanical functioning of the connective tissues [15][16][17][18][19][20][21]. Both in vivo and in vitro studies have shown that reducing sugars, such as glucose and ribose, react with the amino groups of collagen and other proteins and form cross-linked AGEs in the tissue.…”

mentioning

confidence: 99%

Cross‐Linking in Collagen by Nonenzymatic Glycation Increases the Matrix Stiffness in Rabbit Achilles Tendon

Reddy

2003

Journal of Diabetes Research

213

148

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Nonenzymatic glycation of connective tissue matrix proteins is a major contributor to the pathology of diabetes and aging. Previously the author and colleagues have shown that nonenzymatic glycation significantly enhances the matrix stability in the Achilles tendon (Reddy et al., 2002, Arch. Biochem. Biophys., 399, 174-180). The present study was designed to gain further insight into glycation-induced collagen cross-linking and its relationship to matrix stiffness in the rabbit Achilles tendon. The glycation process was initiated by incubating the Achilles tendons (n = 6) in phosphate-buffered saline containing ribose, whereas control tendons (n = 6) were incubated in phosphate-buffered saline without ribose. Eight weeks following glycation, the biomechanical attributes as well as the degree of collagen cross-linking were determined to examine the potential associations between matrix stiffness and molecular properties of collagen. Compared to nonglycated tendons, the glycated tendons showed increased maximum load, stress, strain, Young's modulus of elasticity, and toughness indicating that glycation increases the matrix stiffness in the tendons. Glycation of tendons resulted in a considerable decrease in soluble collagen content and a significant increase in insoluble collagen and pentosidine. Analysis of potential associations between the matrix stiffness and degree of collagen cross-linking showed that both insoluble collagen and pentosidine exhibited a significant positive correlation with the maximum load, stress, and strain, Young's modulus of elasticity, and toughness (r values ranging from .61 to .94)

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Alterations of biochemical and biomechanical properties of rat tail tendons caused by non-enzymatic glycation and their inhibition by dibasic amino acids arginine and lysine

Cited by 54 publications

References 30 publications

Abnormal viscoelastic behaviour of passive ankle joint movement in diabetic patients: an early or a late complication?

Abnormal viscoelastic behaviour of passive ankle joint movement in diabetic patients: an early or a late complication?

<i>L</i>-Lysine Reduces Nonenzymatic Glycation of Glomerular Basement Membrane Collagen and Albuminuria in Diabetic Rats

Cross‐Linking in Collagen by Nonenzymatic Glycation Increases the Matrix Stiffness in Rabbit Achilles Tendon

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