Ultrastructure abnormalities in proteoglycans, collagen fibrils, and elastic fibers in normal and myxomatous mitral valve chordae tendineae

Normal and myxomatous chordae tendineae were studied using light and electron microscopy. to assess the alterations in the appearance and mutual arrangement of proteoglycans, collagen fibrils, and elastic fibers. Specific staining with ruthenium red and cuprolinic blue in a critical electrolyte concentration mode were used to localize proteoglycans. Fresh tissues were fixed in glutaraldehyde containing the cationic dyes and embedded into Spurr resin. Semithin sections of LR White (London Resin Co., Basingstoke, U.K.)-embedded tissue were used for histochemistry. In normal chordae tendineae, the fibrosa comprised close-packed collagen fibrils intermixed with elastic fibers. These were surrounded by a thin layer of elastic fibers and collagen fibrils, both of which were closely associated with proteoglycans. In myxomatous chordae tendineae, alterations were observed in the connective tissue. Proteoglycans were more abundant and were distributed throughout the tissue. The outermost layer was transformed into an undifferentiated electron-dense mass surrounding the central fibrosa, which contained degraded elastic fibers and collagen fibrils. Collagen fibrils had faint banding or lacked a banding pattern altogether. Spaces between collagen fibrils were occupied by abnormal proteoglycans or proteoglycan aggregates. Elastic fibers showed varying degrees of degeneration and were occasionally replaced by electron-lucent spaces containing microfibrils. Accumulation of abnormal proteoglycan was also observed around degenerated elastic fibres and collagen fibrils. (C) 1999 by Elsevier Science Inc.