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Fibrous long-spacing collagen in human atherosclerosis

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      Abstract

      Extracellular lipid deposition in relation to collagen in arterial plaques and in the mitral valve has been examined by a variety of techniques. Lipid reacting with Oil red O showed an identical distribution to that of apolipoprotein B by light microscopy, using immunofluorescence or the immunoperoxidase technique. Using the latter method, the labelled antiserum reacted with spherical particles of a range of molecular diameters corresponding of those of LDL to VLDL, when material was examined in the electron microscope.
      At the ultrastructural level, lipoproteins were found to be bound in a perifibrous and perifibrillar fashion to “normal” 67 nm-banded collagen in arteries and the heart valve.
      Lipoprotein was also found to be bound to fibrous long-spacing collagen (FLSC) in arteries. In ruthenium-red treated material the periodicity of binding of this dye to FLSC was similar to that of lipoprotein binding, suggesting interaction of the lipoprotein with the fibril through proteoglycan.
      Lipoprotein bound to collagen may represent the “firmly-bound” fraction of plasma lipoprotein, which is difficult to extract from arterial tissue. Lipoproteins, present in high concentration in the environment of fibroblasts in newlyforming connective tissue, may actually induce the formation of FLSC. This “abnormal” form of collagen may account for arterial weakening and dilatation because the tensile strength of FLSC is reduced.

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