Cleavage site specificity of MMP-20 for secretory-stage ameloblastin.

@article{Chun2010CleavageSS,
  title={Cleavage site specificity of MMP-20 for secretory-stage ameloblastin.},
  author={Y-H P Chun and Yasuo Yamakoshi and Fumiko Yamakoshi and Makoto Fukae and Jan C. C. Hu and John D. Bartlett and James P. Simmer},
  journal={Journal of dental research},
  year={2010},
  volume={89 8},
  pages={785-90}
}
Ameloblastin is processed by protease(s) during enamel formation. We tested the hypothesis that MMP-20 (enamelysin) catalyzes the cleavages that generate secretory-stage ameloblastin cleavage products. We isolated a 23-kDa ameloblastin cleavage product from developing enamel and determined its N-terminus sequence. Ameloblastin was stably expressed and secreted from HEK293-H cells, purified, and digested with MMP-20 or Klk4 (kallikrein 4). The digests were analyzed by SDS-PAGE and Western… CONTINUE READING

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