The ultrastructural organization of proteoglycans and collagen in human and rabbit scleral matrix.

Abstract

The distribution of proteoglycans and their association with collagen fibrils were studied in human and rabbit sclera following fixation of tissue in glutaraldehyde containing Cuprolinic Blue, a specific stain for proteoglycans when used in the presence of critical concentrations of electrolytes. Proteoglycans were visualized by electron microscopy as fine filaments, approximately 54 nm in length and 5 nm in diameter, associated with the d band in the gap zone of the periodic collagen banding pattern. Filaments were present in three orientations: (1) radiating from the d band to associate with corresponding sites on adjacent collagen fibrils; (2) encircling the collagen fibril at the d band position; and (3) lying along the fibril axis, often linking consecutive d bands. No difference was apparent between the proteoglycan-collagen organization in human and rabbit sclera. A similar arrangement of proteoglycan filaments in association with the d band was also evident throughout all levels of the sclera in spite of considerable variations in fibril diameter from inner to outer stroma. Furthermore, the specific relationship of proteoglycans with the collagen fibrils in sclera closely resembled that previously described in tendon and in articular cartilage, lending support to the view that the association of proteoglycans with collagen may be consistent in a majority of connective tissues, irrespective of their diverse functional specializations.