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 accessAbstract
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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Cites
Cellular and Chemical Events During Enamel Maturation
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Full-length Sequence, Localization, and Chromosomal Mapping of Ameloblastin
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Evidence for Amelogenin "Nanospheres" as Functional Components of Secretory-Stage Enamel Matrix
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Self-citationProteinases in Developing Dental Enamel
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Self-citationEnamelysin (Matrix Metalloproteinase 20)-deficient Mice Display an Amelogenesis Imperfecta Phenotype
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Self-citationMutation in kallikrein 4 causes autosomal recessive hypomaturation amelogenesis imperfecta
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Self-Assembly of a Recombinant Amelogenin Protein Generates Supramolecular Structures
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Cited by
Dental Enamel Formation and Implications for Oral Health and Disease
Lacruz, R. S., Habelitz, S., Wright, J. T., & Paine, M. L. (2017) · Physiological Reviews · doi:10.1152/physrev.00030.2016 · Cited by 599
Protein-mediated Enamel Mineralization
Moradian-Oldak, J. (2012) · Frontiers in Bioscience · doi:10.2741/4034 · Cited by 321
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Matrix metalloproteinases in kidney homeostasis and diseases
Tan, R. J., & Liu, Y. (2012) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00037.2012 · Cited by 265
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Metadata
- Authors
- Lu, Y., Papagerakis, P., Yamakoshi, Y., Hu, J. C.-C., Bartlett, J. D., & Simmer, J. P.
- Venue
- bchm
- Publisher
- Walter de Gruyter GmbH
- 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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