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.
The influence of dibasic amino acids arginine and lysine on non-enzymatic glycation of tail tendon fibers from old (900-day-old) and young (61-day-old) rats was investigated in vitro. The biomechanical changes in tendon fibers of young rats after an incubation interval of 7 or 14 days in a glucose solution were abolished by the addition of arginine or lysine (molar ratio amino acid:glucose 1:10). Glucose incorporation into rat tail tendon fibers as well as Amadori product formation was decreased significantly in the presence of the amino acids. The inhibitory effect of arginine was further confirmed by measurement of the amount of ketoamine formed during the glycation reaction using soluble albumin as a protein target. The effective inhibition of non-enzymatic glycation by arginine or lysine suggests their potential use in vivo as a means of controlling protein over-glycation.
Menzel
E J
EJ
Ludwig Boltzmann Institute for Gerontology, Institute of Immunology, University of Vienna, Austria.
Reihsner
R
R
D000375:Aging; D000818:Animals; D001120:Arginine / Q000494:pharmacology*; D019270:Fructosamine; D005947:Glucose / Q000378:metabolism*; D006031:Glycosylation; D006595:Hexosamines / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D008239:Lysine / Q000494:pharmacology*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013314:Stress, Mechanical; D013623:Tail; D013710:Tendons / Q000187:drug effects / Q000254:growth & development / Q000502:physiology*
D006595:Hexosamines; D012710:Serum Albumin, Bovine; D019270:Fructosamine; D001120:Arginine; D005947:Glucose; D008239:Lysine