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Chymotrypsin C (caldecrin) is associated with enamel development
R S Lacruz1, C E Smith, S M Smith
1Center for Craniofacial Molecular Biology, Herman Ostrow School of Dentistry, University of Southern California, Los Angeles, USA. rodrigo@usc.edu
Journal of Dental Research
|August 11, 2011
Summary
Researchers discovered the serine protease chymotrypsin C (CTRC) is highly expressed in rat incisor enamel during maturation. This finding suggests CTRC may play a role in enamel development and biomineralization.
Area of Science:
- Biochemistry
- Developmental Biology
- Enamel Biology
Background:
- Amelogenesis involves extracellular matrix protein cleavage by proteases.
- Matrix metalloprotease-20 (MMP20) and kallikrein-related peptidase-4 (KLK4) are key proteases in enamel formation.
- Mutations in MMP20 and KLK4 lead to abnormal enamel phenotypes.
Purpose of the Study:
- To investigate the expression and potential role of chymotrypsin C (CTRC) in the developing enamel organ.
- To determine if CTRC is involved in enamel biomineralization.
Main Methods:
- Whole-genome microarray analysis of rat incisor enamel organ cells.
- Quantitative PCR (qPCR) to confirm CTRC mRNA expression.
- Western blot analysis to confirm CTRC protein expression.
Main Results:
- CTRC was significantly up-regulated (> 11-fold) during the enamel maturation stage.
- CTRC expression profile in the enamel organ mirrors that of KLK4, increasing during maturation.
- CTRC mRNA levels were lower than KLK4 mRNA levels during maturation.
Conclusions:
- CTRC, previously thought to be pancreas-specific, is expressed in the developing enamel organ.
- CTRC expression increases during enamel maturation, suggesting a potential role in this stage.
- The discovery of CTRC in enamel development opens new avenues for understanding enamel biomineralization regulation.
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