Immunofluorescent localization of type III collagen and the N-terminal propeptide of type III procollagen in dentin matrix in osteogenesis imperfecta.

Demineralized deciduous and permanent teeth from seven patients with six different types of osteogenesis imperfecta (OI) and from four unaffected controls were stained for type III collagen and for the N-terminal propeptide of type III procollagen using indirect immunofluorescence. Sillence types IA, IB and III OI were each represented by one patient. Two patients had type IVB and two had unclassifiable OI. After enzymatic treatment, the dentin matrix of one patient each with type IB OI, type IVB, and unclassifiable OI reacted with the specific antibodies against both type III collagen and the N-terminal propeptide. Positive staining was observed around the pathological canal-like structures and as delicate strands traversing the matrix. The similar patterns of immunofluorescence for both antigens in dentin in OI are suggestive of retention of the N-terminal propeptide in association with type III collagen identical to that in normal nonmineralized connective tissues. The abnormal presence of type III collagen in dentin in OI may be secondary to the aberrant structure of type I collagen. The failure of dentin matrix of all patients with OI to immunostain for type III collagen and the N-terminal propeptide may reflect heterogeneity or additional secondary changes in matrix macromolecule interactions.