Isolation, Characterization, and Chromosomal Location of the Mouse Enamelysin Gene

Caterina, John J.; Shi, Joanne; Krakora, S.; Bartlett, John D.; Engler, Jeffrey A.; Kozak, Christine A.; Birkedal‐Hansen, Henning

doi:10.1006/geno.1999.5990

Cited by 17 publications

(10 citation statements)

References 11 publications

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“…AY673603) and mouse (Caterina et al, 1999) MMP20 genes, the toad MMP20 orthologs had 10 exons separated by 9 introns (Fig. 3), which completely corresponded to the borders reported for human and mouse MMP20 genes.…”

Section: Genomic Organization Of Caiman and Toad Mmp20 Genessupporting

confidence: 73%

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Identification and characterization of matrix metalloproteinase-20 (MMP20; enamelysin) genes in reptile and amphibian

Shintani

Kobata

Kamakura

et al. 2007

Gene

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Section: Genomic Organization Of Caiman and Toad Mmp20 Genessupporting

confidence: 73%

“…XM235796) specimens. It is located in a cluster of 9 other MMP genes at human chromosome 11q22.3-q23 and at the centromeric end of mouse chromosome 9 (Llano et al, 1997;Caterina et al, 1999). Recently, MMP20-null mouse enamel was demonstrated to be hypoplastic (Caterina et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of matrix metalloproteinase-20 (MMP20; enamelysin) genes in reptile and amphibian

Shintani

Kobata

Kamakura

et al. 2007

Gene

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“…The mouse enamelysin gene includes 10 exons and is located within the MMP cluster at the centromeric end of chromosome 9 (42). To disrupt the functional expression of the enamelysin gene, a 10.6-kb-segment-containing sequence starting at the 3Ј end of intron 2 and extending through most of intron 5 was modified such that the majority of intron 4 and exon 5 was replaced by a phosphoglycerate kinase promoter-controlled hypoxanthine-guanine phosphoribosyltransferase minigene (Fig.…”

Section: Targeted Disruption Of the Enamelysin Locus-mentioning

confidence: 99%

Enamelysin (Matrix Metalloproteinase 20)-deficient Mice Display an Amelogenesis Imperfecta Phenotype

Caterina¹,

Skobe²,

Shi³

et al. 2002

Journal of Biological Chemistry

236

243

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Enamelysin is a tooth-specific matrix metalloproteinase that is expressed during the early through middle stages of enamel development. The enamel matrix proteins amelogenin, ameloblastin, and enamelin are also expressed during this same approximate developmental time period, suggesting that enamelysin may play a role in their hydrolysis. In support of this interpretation, recombinant enamelysin was previously demonstrated to cleave recombinant amelogenin at virtually all of the precise sites known to occur in vivo. Thus, enamelysin is likely an important amelogenin-processing enzyme. To characterize the in vivo biological role of enamelysin during tooth development, we generated an enamelysindeficient mouse by gene targeting. Although mice heterozygous for the mutation have no apparent phenotype, the enamelysin null mouse has a severe and profound tooth phenotype. Specifically, the null mouse does not process amelogenin properly, possesses an altered enamel matrix and rod pattern, has hypoplastic enamel that delaminates from the dentin, and has a deteriorating enamel organ morphology as development progresses. Our findings demonstrate that enamelysin activity is essential for proper enamel development.Dental enamel covers the crown of the tooth and is unique among mineralized tissues because of its high mineral content, large crystals, and organized prism pattern. Other mineralized tissues such as bone, dentin, and cementum are composed of ϳ20% organic material. In contrast, mature enamel has less than 1% organic matter by weight (1, 2). Moreover, enamel crystallites possess a volume that is 100 times greater than the volume of crystallites found in other mineralizing tissues. These enamel crystallites form enamel rods that, in turn, form a unique interlacing (decussating) prism pattern. As a result, dental enamel is the hardest substance in the body. Its hardness is intermediate between that of iron and carbon steel, yet it also has a high elasticity (3).Although mature enamel is a very hard protein-free tissue, it does not start this way. Enamel development (amelogenesis) consists of several stages that include the secretory, transition, and maturation stages. During the secretory stage, enamel crystallites elongate into long thin ribbons that are only a few apatitic unit cells in thickness (about 10 nm) with a width of ϳ30 nm (4, 5). The ribbons are evenly spaced, are oriented parallel to each other, and grow in length but very little in width and thickness. Ultimately, enamel crystal length determines the final thickness of the enamel layer as a whole (for review, see Ref. 6). It is during the secretory stage that the columnar-shaped ameloblast cells, located adjacent to the forming enamel, secrete specialized enamel proteins into the enamel matrix. These proteins include amelogenin (7), ameloblastin (8), and enamelin (9). Amelogenin is the predominant component and comprises ϳ90% of total enamel matrix protein (10). Interestingly, the full-length enamel proteins are found only at the mineralizing front, su...

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“…KLK4 is a proteolytic enzyme that was first detected in porcine enamel (Fukae et al, 1977), and degrades the 20-kDa amelogenin into two fragments, corresponding to the 6-kDa and 13-kDa amelogenins (Shimizu and Fukae, 1983). Enamelysin mRNA has been detected in odontoblasts and ameloblasts of the enamel organ by in situ hybridization (Bègue-Kirn et al, 1998;Caterina et al, 1999). KLK4 mRNA signal was detected in the ameloblasts during the early maturation stage by in situ hybridization (JC Hu et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Relative Levels of mRNA Encoding Enamel Proteins in Enamel Organ Epithelia and Odontoblasts

et al. 2003

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Amelogenin, enamelin, sheathlin (ameloblastin/ amelin), enamelysin (MMP-20), and KLK4 (EMSP-1) are the major structural proteins and proteinases in developing tooth enamel. Recently, odontoblasts were reported to express amelogenin, the most abundant enamel protein. In this study, we hypothesized that odontoblasts express all enamel proteins and proteases, and we measured their relative mRNA levels in enamel organ epithelia and odontoblasts associated with porcine secretory- and maturation-stage enamel by RT-PCR, using a LightCycler instrument. The results showed that amelogenin mRNA in secretory-stage EOE is 320-fold higher than in odontoblasts beneath secretory-stage enamel, and over 20,000-fold higher than in odontoblasts under maturation-stage enamel. Similar results were obtained for enamelin and sheathlin. Enamelysin mRNA levels were equivalent in these two tissues, while KLK4 mRNA was higher in odontoblasts than in secretory-stage EOE. These results support the conclusion that odontoblasts are involved in the formation of the enamel layer adjacent to enamel-dentin junction.

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Isolation, Characterization, and Chromosomal Location of the Mouse Enamelysin Gene

Cited by 17 publications

References 11 publications

Identification and characterization of matrix metalloproteinase-20 (MMP20; enamelysin) genes in reptile and amphibian

Identification and characterization of matrix metalloproteinase-20 (MMP20; enamelysin) genes in reptile and amphibian

Enamelysin (Matrix Metalloproteinase 20)-deficient Mice Display an Amelogenesis Imperfecta Phenotype

Relative Levels of mRNA Encoding Enamel Proteins in Enamel Organ Epithelia and Odontoblasts

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