TY - JOUR
T1 - Age-related alteration of cross-linking amino acids of elastin in human aorta
AU - Watanabe, Mika
AU - Sawai, Takashi
AU - Nagura, Hiroshi
AU - Suyama, Kyozo
N1 - Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1996/10
Y1 - 1996/10
N2 - 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 isooxodesmosine (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 O 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.
AB - 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 isooxodesmosine (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 O 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.
KW - Aging
KW - Cross-linking amino acids
KW - Elastin
KW - High-performance liquid chromatography (HPLC)
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U2 - 10.1620/tjem.180.115
DO - 10.1620/tjem.180.115
M3 - Article
C2 - 9111761
AN - SCOPUS:0030252872
VL - 180
SP - 115
EP - 130
JO - Tohoku Journal of Experimental Medicine
JF - Tohoku Journal of Experimental Medicine
SN - 0040-8727
IS - 2
ER -