Immunoelectron microscopic visualization of pro- and secreted forms of decorin and biglycan in the predentin and during dentin formation in the rat incisor

• Published in: Calcified tissue international Vol. 69; no. 1; pp. 38 - 45
• Main Authors: Septier, D, Hall, R C, Embery, G, Goldberg, M
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01-07-2001
• Subjects: Animals; Biglycan; Calcification, Physiologic - physiology; Decorin; Dentin - chemistry; Dentin - ultrastructure; Extracellular Matrix - chemistry; Extracellular Matrix - ultrastructure; Extracellular Matrix Proteins; Immunohistochemistry; Incisor - ultrastructure; Male; Microscopy, Immunoelectron; Odontoblasts - chemistry; Odontoblasts - ultrastructure; Proteoglycans - analysis; Proteoglycans - ultrastructure; Rats; Rats, Wistar
• ISSN: 0171-967X; 1432-0827
• DOI: 10.1007/s002230020047

Using antibodies raised against the proform and fully processed (secreted) forms of the proteoglycans decorin and biglycan, combined with gold electron immunohistochemistry, we observed in the incisors of five Sprague-Dawley rats that the proforms were mostly located in the cell bodies of odontoblasts, with a presence reduced to one-third or one-fourth in the processes. Proforms, also present in the extracellular matrix, were uniformly distributed throughout predentin, with higher labeling for probiglycan than pro-decorin. Both were present in lesser amounts in metadentin and dentin. With respect to the secreted form, grain density was at a constant level for biglycan in predentin and dentin, whereas a gradient was detected for decorin, the grain density being increased three times in the distal predentin. Although decorin labeling was diminished in metadentin, staining in circumpulpal dentin was similar to that found in distal predentin. We have previously reported a reverse gradient for chondroitin sulfate/dermatan sulfate distribution. To reconcile these diverging data, our hypothesis is that enzymatic proteolytic cleavage may remove the glycosylated N-terminal-containing region, resulting in a non- proteoglycan form of the molecule. Although substantial differences in distribution were apparent between the two proteoglycans, increasing interactions between proteoglycans and collagen, facilitated by the cleavage and loss of the N-terminal glycosaminoglycan chain region in the distal predentin, may be a prerequisite for dentin mineralization.