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Micro-dissection of Enamel Organ from Mandibular Incisor of Rats Exposed to Environmental Toxicants

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Lysosomal protease expression in mature enamel.

Coralee E Tye¹, Rachel L Lorenz, John D Bartlett

¹Department of Cytokine Biology, Forsyth Institute, Boston, Mass. 02115, USA.

Cells, Tissues, Organs

|August 16, 2008

Summary

Lysosomal proteases, including cathepsins and peptidases, are abundant in developing enamel organs. These enzymes likely play a key role in breaking down enamel matrix proteins during tooth development.

Area of Science:

Biochemistry
Developmental Biology
Oral Biology

Background:

Enamel matrix proteins are crucial for tooth development but must be removed for mature enamel.
Matrix metalloproteinase-20 and kallikrein-4 initiate enamel protein degradation.
The exact mechanisms for removing and degrading protein fragments remain unclear.

Purpose of the Study:

To identify lysosomal proteases present in the maturation-stage enamel organ.
To investigate the role of these proteases in enamel protein degradation.

Main Methods:

RNA extraction from mouse molars.
Gene expression analysis using RT-PCR and qPCR.
Immunohistochemical staining of mouse incisors to localize protease expression.

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Main Results:

Most assessed lysosomal proteases, including cathepsins B, D, F, H, K, L, O, S, and Z, were expressed in maturation-stage enamel organs.
Tripeptidyl peptidases I and II and dipeptidyl peptidases I, II, III, and IV were also detected.
Immunohistochemistry confirmed ameloblast expression of cathepsins L and S and tripeptidyl peptidase II.

Conclusions:

Maturation-stage ameloblasts are rich in various lysosomal proteases.
These proteases are likely essential for the degradation of the organic enamel matrix during tooth development.