Work

Functions of KLK4 and MMP-20 in dental enamel formation

Year: 2008

Type: review

Abstract: Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin (MMP-20). The late protease is kallikrein 4 (KLK4). Mutations in MMP20 and KLK4 both cause autosomal recessive amelogenesis imperfecta, a condition featuring soft, porous enamel containing residual protein. MMP-20 is secreted along with enamel proteins by secretory-stage ameloblasts. Enamel protein-cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. KLK4 is secreted by transition- and maturation-stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. The principle functions of MMP-20 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins.

Source: Biological Chemistry

DOI: 10.1515/bc.2008.080

Authors: Yuhe Lu, Petros Papagerakis, Yasuo Yamakoshi, Jan C.-C. Hu, John D. Bartlett, James P. Simmer

Institutions: University of Michigan, Harvard University, The Forsyth Institute

Language: English

Topic: dental development and anomalies

Subfield: General Dentistry

Field: Dentistry

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Institutes of Health, U.S. Public Health Service, National Institute of Dental and Craniofacial Research