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Cited by 255

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

Functions of KLK4 and MMP-20 in dental enamel formation

Open access
Lu, Yuhe, Papagerakis, Petros, Yamakoshi, Yasuo, Hu, Jan C.-C., Bartlett, John D., Simmer, James P.·2008·bchm

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.

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Crossref · 10.1515/bc.2008.080

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Metadata

Authors
Lu, Y., Papagerakis, P., Yamakoshi, Y., Hu, J. C.-C., Bartlett, J. D., & Simmer, J. P.
Venue
bchm
Published
2008-05-15
Volume
389
Issue
6
Pages
695-700
ISSN
  • 1431-6730 (ISSN-L)
  • 1437-4315
OpenAlex
W2072894795
Cited by
255
References
30
FWCI
6.33
Type
journal article
Language
en
Open access
green

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