Letter to the Editor |
University of Maryland, School of Medicine, Department of Pathology, Baltimore, Md
An extract of the first 250 words of the full text is provided, because this article has no abstract. |
To the Editor:
We read with great interest the article by Oksjoki et al1 regarding association between complement Factor H and proteoglycans in early human coronary atherosclerotic lesions. We would like to add several comments to this recently published article.
Several studies have demonstrated the presence of terminal complement complex C5b-9 in human atherosclerotic arteries.24 Quantitative determination in the human aorta by ELISA showed that C5b-9 levels were highest in intimal thickening and with detectable levels in both normal and fatty streaks intima.5 Our data indicate that activation of complement starts early during the prelesional stages of the atherosclerotic process. The activation is more intense in initial stages than in advanced fibrous plaques. Similar prelesional C5b-9 deposition was found in experimental atherosclerosis.6 In contrast to these findings, Oksjoki et al1 show that C5b-9 was immunohistochemically absent in grossly normal human coronary artery. This difference in the results might be explained by the higher sensitivity of the ELISA for C5b-9.
We have previously examined the relationship between C5b-9 and the complement inhibitor S-protein/vitronectin.7 S-protein/vitronectin prevents C5b-9 insertion in the cell membrane by binding to C5b-7. The formed SC5b-9 complex is cytolytically inactive. Using immuno-electron microscopy, S-protein/vitronectin was localized in association with elastin fibers, collagen bundles, and cell debris in the vicinity of elastin.7 Cell debris embedded in collagen matrix were S-protein/vitronectin negative. In contrast, all cell debris were positive for C5b-9 deposits. These data suggested that connective tissue matrix by associating S-protein/vitronectin play an important role in regulation of terminal complement
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