Distribution patterns of neoglycoprotein-binding sites (endogenous lectins) and lectin-reactive glycoconjugates during cartilage and bone formation in human finger.

The distribution of endogenous lectins, visualized by labelled neoglycoproteins, and of defined oligosaccharide structures, reactive with plant lectins, during fetal development of the fingers was analyzed in sections of human 3- to 8-month-old fetal specimens. Chondrogenesis as well as ossification were correlated with characteristic modulations in the expression of both glycoligand-binding molecules and characteristic carbohydrate structures. Occurrence of xylose-specific receptors was judged to be an early sign of cartilage development. Similarly, alpha-mannosyl residues that had been attached to labelled carrier proteins were strongly bound by the extracellular matrix already during early stages of finger maturation. Staining intensity for heparin gradually increased during chondrogenesis, whereas affinity for mannose showed a stage-related decline. Binding of mannose-6-phosphate was confined to hypertrophied cartilage of primary ossification centers. Accessible binding sites for terminal N-acetylneuraminic acid and N-acetylgalactosamine moieties were detected only in osteoid. In addition to monitoring the sugar-binding capacity, presence and developmental regulation of distinct carbohydrate structures were also assessed. PSA and SBA enabled the demonstration of an abrupt loss of staining affinity in the zone of maturing hypertrophic cartilage. Succinylated WGA proved to be an apparently useful marker of evolving bone tissue. GSL-II binding was restricted to chondroclasts and osteoclasts. The findings of this investigation are consistent with the supposed role of glycoconjugate-lectin interactions in cartilage and bone development.