Effect of aging on human aortic protein composition: II. Two-dimensional polyacrylamide gel electrophoretic analysis

Abstract

Arterial intima proteins were extracted by 9 M urea from matching histologically atheroma-free areas of 27 human thoracic aortas of both sexes from younger (15–34) and older (35–82) age groups and studied after separation by high-resolution two-dimensional polyacrylamide gel electrophoresis. Seventeen specific protein groups on each gel were identified according to their relative charges and molecular weights and their distribution in the two age groups compared. Some plasma-derived proteins occurred rarely in young aortas while they were consistently found in those from older cases, i.e., protein group 4 ( α 1-antichymotrypsin) 1 13 (8%) vs 12 14 (86%), group 7 (haptoglobin β-chain) 1 13 (8%) vs 13 14 (93%) and groups 6 and 9 (IgG chains) 1 13 (23%) vs 9 14 (64%), respectively. Other plasma-derived proteins such as group 3 (albumin) and 5 ( α 1-antitrypsin) were identified in all samples of both age groups but their expression in the aortic intima increased with age. Proteins which are typically found intracellularly such as those from groups 11 (actin), 12 (cytoskeleton proteins), and 13 (tropomyosin-like proteins) appeared in samples of intima of both age groups but were less apparent in older specimens. These studies suggest that the changes in aortic intima protein distribution in the absence of atherosclerosis closely correlate with histological changes such as intimal thickening often found with aging, providing new sensitive markers of vascular senescence.