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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Cytochemical localization of dipeptidyl peptidase II activity in rat incisor tooth ameloblasts.

Dipeptidyl peptidase II (DPP II), E.C., a serine class endopeptidase, is widely used as a lysosomal marker in cytochemical studies. To date most ultrastructural studies of ameloblasts use the presence of acid phosphatase activity to identify cellular organelles to be lysosomal. Using decalcified rat mandibles, with kidney tissue as a positive control, DPP II activity, was assessed with specific substrate Lysyl-alanine-4-methoxy-2-naphthylamide in ameloblasts at an ultrastructural level. Reaction product (RP) indicative of DPP II activity was observed only within lysosome-like organelles. These RP-labelled organelles were only localized in the supra- or para-nuclear regions of the ameloblasts, which corresponds with previous studies using acid phosphatase cytochemistry. However, in contrast with these studies, RP was not detected in the distal region of the ameloblasts, viz., in the Tomes' processes of the secretory ameloblasts or near the ruffled border in the maturation ameloblasts. The transitional ameloblasts were notable for the intensity of staining of their RP-labelled organelles. We propose that DPP II may have a role in programmed cell death which is thought to occur in this transition zone. Biochemical analysis of rat incisor enamel organ homogenates, indicated tissue fixation resulted in an 82% reduction in DPP II activity, although the specific activity of DPP II was not affected.[1]


  1. Cytochemical localization of dipeptidyl peptidase II activity in rat incisor tooth ameloblasts. Smid, J.R., Monsour, P.A., Rousseau, E.M., Young, W.G. Anat. Rec. (1992) [Pubmed]
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