1999 Volume 187 Issue 4 Pages 291-303
Elastic fiber is one of the major component of the extracellular matrix, which provides the resilience to many tissues. Elasticity is an important property of human aorta, and this elastic property decreases in various pathological conditions such as dissecting aneurysm (DA). Since the cross-linking structures in elastin are responsible for this elasticity, we studied the alteration of various cross-linking amino acids in human aorta associated with DA by a new method using high-performance liquid chromatography (HPLC). Materials were obtained from non-atherosclerotic areas of thoracic aorta of 27 autopsy cases which had no particular aortic disease and 19 cases of DA at replacement operation. 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 crosslinks of elastin were decreased in DA as compared to the age-matched control. The decrease of ISOXO was marked. The increase of PYR and PYR/(DES+ISDES) were not statistically significant. It is suggested oxidative degradation on elastin crosslinks occur in DA, and the ratio of collagen to elastin didn't contribute to the pathogenesis of DA.