Age-Related Alteration of Cross-Linking Amino Acids of Elastin in Human Aorta.

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Abstract
It is well known that the elastic property of human aorta decreases gradually with age. Since the cross-linking structures are responsible for this elasticity, age-related changes of cross-linking amino acids in human aorta were studied using a high-performance liquid chromatography (HPLC). Non-atherosclerotic areas of thoracic aorta of 27 autopsy cases which had no particular aortic disease were obtained. After acid hydrolysis, SEP-PAK silica-gel column and Fe3+/activated charcoal column pretreatment were carried out for analysis of desmosine (DES), isodesmosine (ISDES), neodesmosine (NEO), oxodesmosine (OXO) and isooxodesomosine (ISOXO), and for analysis of aldosine (ALD), respectively. These prepared samples were applied to the reversed-phase HPLC column. We also analyzed pyridinoline (PYR), a major cross-linking amino acid of collagen as an index of fibrosis. All cross-linking amino acids of elastin rapidly increased in infancy and then gradually decreased with age. In the middle- and old-age, the amount of OXO showed marked variety. PYR was little detected at 0-year-old, and then gradually increased with age. The crosslinks of elastin were rapidly formed in childhood and then decreased with age. These findings suggest that the relative increase of NEO, OXO or ISOXO to DES and ISDES is associated with age-related weakening and/or damage of elastin, and that the gradual shift from elastin- to collagen-dominant state is a possible cause of the loss of elasticity and the gain of stiffness in the aging aorta.