Abstract-Degradation of the elastic media is a hallmark of abdominal aortic aneurysms (AAAs). We examined the expression of 2 elastolytic matrix metalloproteinases (MMPs), MMP-2 and MMP-9, in AAA aortic tissues compared with those from atherosclerotic occlusive disease (AOD) and nondiseased control tissues. Quantitative competitive reverse transcription-polymerase chain reaction and gelatin zymography showed increased MMP-9 mRNA and protein in both AAA and AOD tissues compared with those in control tissue, but there was no significant difference between AAA and AOD. In contrast, MMP-2 mRNA and protein levels were significantly higher in AAA than in AOD or control tissues. Sequential extraction of the MMPs from the aortic tissue with a physiological salt solution, 2% dimethylsulfoxide (DMSO), and 10 mol/L urea showed that large amounts of MMP-2 and MMP-9 were bound to the matrix. The most conspicuous finding was that the levels of MMP-2 were significantly elevated in the DMSO fraction in AAA tissues compared with AOD and control tissues. In addition, a large portion of MMP-2 found in the DMSO and urea fractions was in the active 62-kDa form, indicating that the precursor of MMP-2 in AAA is largely activated locally and binds to the tissue matrix tightly. By immunolocalization, MMP-9 was found to be primarily produced by macrophages and MMP-2 by mesenchymal cells.

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After extraction of lipid, calcium, and soluble proteins, hydroxyproline (collagen) and desmosine-isodesmosine (elastin) contents were determined by high-performance liquid chromatography in the ascending and descending thoracic, supraceliac, and suprarenal aorta. By repeated measures of analysis of covariance, collagen was found to be increased throughout the aorta in AAA as compared with normal aorta or aorta with atherosclerotic occlusive disease. This difference remained significant when adjustments were made for group differences in age and degree of atherosclerosis. This increase in collagen content results in a dilutional decrease in elastin concentration. These data demonstrate that the same matrix protein alterations found in AAA tissue occur throughout the aorta, differing only in magnitude in the aneurysmal and nonaneurysmal segments. These data suggest that aneurysm formation may related to alterations in the regulation of elastin and collagen.

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