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By Rodolfo Paoletti, Dr. David Kritchevsky

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In a later work, Hoff and Gaubatz (1979) characterized the conditions for Lipoproteins and the Arterial Mesenchyme 29 optimal release of the bound LDL fraction from human plaques. Elastase was found to be more efficient for solubilizing immunoelectrophoretically evaluated, apoB-containing particles; collagenase and chondroitinase ABC were found to be less effective. These results, together with those of Smith et al. (1976), confirmed that LDL in arterial intima is bound by noncovalent forces to components of the extracellular matrix and that hydrolysis of elastin, collagen, and arterial proteoglycans is necessary in order to extract the immunologically recognizable LDL.

The problem of plasma lipoprotein influx into human arterial intima has been reinvestigated by Nicoll etal. (1981). Injection of radioiodinated VLDL up to 30 hours before vascular reconstructive surgery enables sampling of normal and atherosclerotic arterial intima. The measured influx of LDLapoB was found to be 16- to 18-fold higher than the influx of VLDL-apoB or IDL-apoB in normal or atherosclerotic aortic intima. 1 ng cm - 2 hours -1 ) was significantly higher in atheromatous aortic intima than in normal segments.

1976) have carried out immunohistochemical studies in cholesterol-fed rabbits. , 1973, 1974). The apoB antigen was concentrated in the lipid-rich extracellular space. These results indicate that the atherosclerotic lesion in humans and other mammals contains particles with apoB-related antigens that are associated with the extracellular matrix and that probably are derived from plasma lipoproteins, are in different stages of processing by the tissue, and are in complexes of dissimilar labilities.

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