Lectin binding to elastic fibres and associated components during development of the human aorta.

A panel of peroxidase-conjugated lectins was used to stain frozen sections of human foetal, neonatal, infant and adult aortae. Two main distinctive staining patterns were observed at the light microscope level, depending on the lectin employed. Lectins from Concanavalin A, Triticum vulgaris, Arachis hypogaea and Glycine max resulted in staining of the surfaces of aortic elastic lamellae and the interlamellar areas. With lectins from Dolichos biflorus and Bandeiraea simplicifolia staining was seen predominantly in the interlamellar areas. The findings indicate the presence of several different glycoconjugates at various sites within the aorta. In addition, there were alterations in the lectin binding affinities of the aortae that were dependent upon age. The findings are interpreted as indicating sequential changes in the composition of glycoprotein or proteoglycan moieties in the development of the human aorta.