期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 495, 期 2, 页码 1896-1900出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2017.12.040
关键词
Dental enamel hardening; Enamel defects; Enamel matrix; Hydroxyapatite binding; KLK4 autolysis
资金
- Melbourne Research Unit for Facial Disorders, Department of Pharmacology Therapeutics
- Department of Paediatrics and Faculty of Medicine, Dentistry and Health Science (MH) at the University of Melbourne
- NHMRC Australia [APP1073603]
- Becas Chile
- University of Talca [RU-6352011]
The protease kallikrein 4 (KLK4) plays a pivotal role during dental enamel formation by degrading the major enamel protein, amelogenin, prior to the final steps of enamel hardening. KLK4 dysfunction is known to cause some types of developmental defect in enamel but the mechanisms responsible for transient retention of KLK4 in semi-hardened enamel matrix remain unclear. To address contradictory reports about the affinity of KLK4 for enamel hydroxyapatite-like mineral, we used pure components in quasi-physiological conditions and found that KLK4 binds hydroxyapatite directly. Hypothesising KLK4 self-destructs once amelogenin is degraded, biochemical analyses revealed that KLK4 progressively lost activity, became aggregated, and autofragmented when incubated without substrate in both the presence and absence of reducer. However, with non-ionic detergent present as proxy substrate, KLK4 remained active and intact throughout. These findings prompt a new mechanistic model and line of enquiry into the role of KLK4 in enamel hardening and malformation. (C) 2017 Elsevier Inc. All rights reserved.
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