期刊
JOURNAL OF DENTAL RESEARCH
卷 88, 期 4, 页码 323-327出版社
SAGE PUBLICATIONS INC
DOI: 10.1177/0022034509334240
关键词
enamel; dipeptidyl peptidase I; kallikrein-4; amelogenesis; mineralization
资金
- National Institute of Dental and Craniofacial Research [DE016276]
- National Institute of Allergy and Infectious Diseases [AI049261]
- National Institutes of Health, Bethesda, MD, USA [20892]
Kallikrein-4 (KLK4) is a serine protease expressed during enamel maturation, and proteolytic processing of the enamel matrix by KLK4 is critical for proper enamel formation. KLK4 is secreted as an inactive zymogen (pro-KLK4), and identification of its activator remains elusive. Dipeptidyl peptidase I (DPPI) is a cysteine aminopeptidase that can activate several serine proteases. In this study, we sought to examine DPPI expression in mouse enamel organ and determine if DPPI could activate KLK4. Real-time PCR showed DPPI expression throughout amelogenesis, with highest expression at maturation, and immunohistochemical staining of mouse incisors confirmed DPPI expression by ameloblasts. We demonstrate in vitro that DPPI activates pro-KLK4 to cleave a fluorogenic peptide containing a KLK4 cleavage site. Examination of mature enamel from DPPI null mice by FTIR showed no significant accumulation of protein; however, microhardness testing revealed that loss of DPPI expression significantly reduced enamel hardness.
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