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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 389, Issue 6

Issues

Functions of KLK4 and MMP-20 in dental enamel formation

Yuhe Lu
  • 1Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, 1011 North University, Ann Arbor, MI 48109-1078, USA
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/ Petros Papagerakis
  • 2Department of Orthodontics and Pediatric Dentistry, University of Michigan School of Dentistry, 1011 North University, Ann Arbor, MI 48109-1078, USA
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/ Yasuo Yamakoshi
  • 3Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, 1011 North University, Ann Arbor, MI 48109-1078, USA
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/ Jan C.-C. Hu
  • 4Department of Orthodontics and Pediatric Dentistry, University of Michigan School of Dentistry, 1011 North University, Ann Arbor, MI 48109-1078, USA
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/ John D. Bartlett
  • 5Harvard-Forsyth Department of Oral Biology, Department of Cytokine Biology, The Forsyth Institute, 140 The Fenway, Boston, MA 02115, USA
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/ James P. Simmer
  • 6Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, 1011 North University, Ann Arbor, MI 48109-1078, USA
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Published Online: 2008-05-15 | DOI: https://doi.org/10.1515/BC.2008.080

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.

Keywords: amelogenesis imperfecta; EMSP1; enamelysin; kallikrein; matrix metalloproteinase; tooth enamel

About the article

Corresponding author


Published Online: 2008-05-15

Published in Print: 2008-06-01


Citation Information: Biological Chemistry, Volume 389, Issue 6, Pages 695–700, ISSN (Online) 14374315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.080.

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