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MR detection of quantitative and structural changes in human aortic aneurysms
Author(s) -
Vinée Philippe,
Meurer Bernard,
Constantinesco André,
Kohlberger Bernd,
Hauenstein Karl Heinz,
Stöver Brigitte,
Laubenberger Jörg,
Petkov Simeon,
Oursin Caroline,
Eisenmann Bernard
Publication year - 1993
Publication title -
journal of magnetic resonance imaging
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.563
H-Index - 160
eISSN - 1522-2586
pISSN - 1053-1807
DOI - 10.1002/jmri.1880030215
Subject(s) - extracellular matrix , aorta , nuclear magnetic resonance , materials science , biophysics , chemistry , anatomy , medicine , biology , biochemistry , physics
Collagen is a major component of the extracellular matrix and a determinant of the elastic behavior of the human aorta. To investigate the changes found in aneurysmal degeneration, the authors studied the solid‐state hydrogen‐1 nuclear magnetic resonance line shape of collagen in aneurysms and normal human aortas. A three‐component decomposition of the free induction decay was performed, with collagen characterized by a T2 of about 18 μsec. The second moment of the collagen line shape was found to be increased in aneurysms (5.3 vs 4.8 G 2 ), while, correspondingly, the T2 of collagen was lower in aneurysms (16.3 vs 17.7μsec). This corresponds to a modification of collagen structure and molecular motion. Collagen concentration was lower in nondiseased aortic walls (9.4% vs 7.3%). These results are discussed in reference to the contradictory conclusions in the current literature. The increase in collagen and the modification of its structure and molecular motion are explained by the need to resist an increasing tangential tension due to increased aortic diameter and diminished wall thickness in aneurysms and by intercalation or site binding in the helices or electric dipolar interactions in the less mobile side groups.