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J Dent Res 81(11): 738-742, 2002
© 2002 International and American Associations for Dental Research

RESEARCH REPORT
Clinical

Autosomal-dominant Hypoplastic Form of Amelogenesis Imperfecta Caused by an Enamelin Gene Mutation at the Exon-Intron Boundary

M. Kida1,2, T. Ariga1,*, T. Shirakawa2, H. Oguchi2, and Y. Sakiyama1

1 Research Group of Human Gene Therapy, Hokkaido University Graduate School of Medicine, N-15, W-7, Kita-ku, Sapporo, 060-8638, Hokkaido, Japan; and
2 Pediatric Dentistry, Hokkaido University Graduate School of Dental Medicine N-13, W-7, Kita-ku, Sapporo, 060-8586,Hokkaido, Japan;

* corresponding author, tada-ari{at}med.hokudai.ac.jp


   ABSTRACT
TOP
 ABSTRACT
INTRODUCTION
 MATERIALS & METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
Amelogenesis imperfecta (AI) is currently classified into 14 distinct subtypes based on various phenotypic criteria; however, the gene responsible for each phenotype has not been defined. We performed molecular genetic studies on a Japanese family with a possible autosomal-dominant form of AI. Previous studies have mapped an autosomal-dominant human AI locus to chromosome 4q11-q21, where two candidate genes, ameloblastin and enamelin, are located. We studied AI patients in this family, focusing on these genes, and found a mutation in the enamelin gene. The mutation detected was a heterozygous, single-G deletion within a series of 7 G residues at the exon 9-intron 9 boundary of the enamelin gene. The mutation was detected only in AI patients in the family and was not detected in other unaffected family members or control individuals. The male proband and his brother showed hypoplastic enamel in both their deciduous and permanent teeth, and their father showed local hypoplastic defects in the enamel of his permanent teeth. The clinical phenotype of these patients is similar to that of the first report of AI caused by an enamelin gene mutation. Thus, heterogeneous mutations in the enamelin gene are responsible for an autosomal-dominant hypoplastic form of AI.

KEY WORDS: amelogenesis imperfecta • autosomal-dominant • enamelin • hypoplastic enamel


   INTRODUCTION
TOP
 ABSTRACT
 INTRODUCTION
MATERIALS & METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
Amelogenesis imperfecta (AI) is a heterogeneous group of genetic disorders characterized by defects in tooth enamel formation in the absence of any generalized or systemic diseases. The prevalence of AI is reported at 1/700 in northern Sweden (Bäckman and Holm, 1986) and 1/14,000 in the US (Witkop and Sauk, 1976). There has been no comprehensive study of the prevalence of AI in Asian countries, although clinical phenotypes of hypoplastic and hypocalcified AI have been reported in Japan (Ooya et al., 1988; Sekiguchi et al., 1998). AI is currently classified into 14 distinct subtypes based on the clinical phenotype and mode of inheritance (Witkop, 1988); however, the gene responsible for every subtype has not yet been defined.

Major enamel matrix proteins (amelogenin, enamelin, and ameloblastin) are suggested to contribute to the enamel formation of teeth (Uchida et al., 1991). During the secretory stage of enamel formation, these proteins are secreted by ameloblasts and play key roles in the growth of enamel crystal (Robinson et al., 1998).

Several reports have shown that mutations in the amelogenin gene located at Xp22.1-p22.3 cause X-linked AI (Lagerström et al., 1991; Lagerstrom-Fermer et al., 1995; Hart et al., 2000). However, the X-linked AI presents in less than 5% of all reported cases. The most common type of AI is the autosomal-dominant form (Kärrman et al., 1996). The locus responsible for one autosomal-dominant form of local hypoplastic AI (AIH2) has been mapped to chromosome 4q11-q21 (Kärrman et al., 1997). A gene encoding a tooth-specific protein ameloblastin has been mapped to 4q21 (MacDougall et al., 1997), suggesting that ameloblastin might be the candidate gene responsible for the autosomal-dominant form of AI. However, to date, no case of AI has identified a mutation in the ameloblastin gene (Kärrman-Mårdh et al., 2001).

The gene encoding another tooth-specific protein enamelin has also been mapped to chromosome 4q21 (Dong et al., 2000; Hu et al., 2000). Subsequently, a mutation in the enamelin gene was first identified in a family with the autosomal-dominant hypoplastic form of AI (Rajpar et al., 2001). In this paper, we report a Japanese family with an autosomal-dominant hypoplastic form of AI. We performed mutation analysis focusing on the ameloblastin and enamelin genes, and found a heterozygous single-base deletion at the exon 9-intron 9 border of the enamelin gene. Since the clinical phenotype of this family is similar to that of the first report caused by the enamelin gene mutation (Rajpar et al., 2001), it is possible that heterogeneous mutations within the enamelin gene might also be responsible for the autosomal-dominant hypoplastic forms of AI.


   MATERIALS & METHODS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS & METHODS
RESULTS
 DISCUSSION
 REFERENCES
 
Familial Studies
The pedigree of the AI family in this study and their clinical features are shown in Fig. 1Go. The family individuals were clinically examined and the diagnosis of AI was made by several dentists according to Witkop’s classification (1988). Informed consent was obtained from all the participants prior to their entry into this study. Approval was obtained from the institutional review board for this study, and informed consent from all familial members in this article was provided according to the Declaration of Helsinki.




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  		Figure 1. The clinical features of our AI family. (A) Pedigree of the family. An arrow indicates the proband. Asterisks indicate individuals examined clinically and genetically. (B) Top: Photograph of III-1 at the age of 3 showing the hypoplastic primary teeth with an anterior open bite. Middle: Photograph of III-2 showing the characteristic small, yellow permanent lower right first and second premolar teeth. Bottom: Photograph of II-1 showing local hypoplastic enamel defects characterized by the horizontal lesion located primarily at the middle third of the permanent lower left canine and first premolar teeth.

 
DNA Purification and PCR Analysis
Peripheral-blood mononuclear cells (PBMC) of affected and unaffected individuals in the family were isolated by the Ficoll-Hypaque (Pharmacia Biotech, Piscataway, NJ, USA) gradient method. Genomic DNA was purified from PBMC by Sepa-Gene (Sanko-Junyaku, Tokyo, Japan). We performed the mutation analysis of the ameloblastin and enamelin genes. Primers used for ameloblastin were reported elsewhere (Kärrman-Mårdh et al., 2001). Primers originally designed by Rajpar et al. (2001) were used to amplify the enamelin gene (TableGo). Since Hu et al. (2001) have proposed the presence of an additional exon of the human enamelin gene as exon 2, we have constructed an additional set of primers for it. Accordingly, the numbering of enamelin exons and introns was changed from that in Rajpar’s publication. PCR was performed in a 20-µL volume with the use of an AmpliTaq Gold PCR Master Mix (Applied Biosystems, Foster City, CA, USA), 10 pM of forward and reverse primers, and 100 ng of sample DNA. Amplification was performed in a GeneAmp 9700 thermal cycler (Applied Biosystems). After the initial incubation for 9 min at 94°C, samples were subjected to 40 cycles of 30 sec at 94°C, 30 sec at 60°C, and 30 sec at 72°C. Then the final extension step was performed at 72°C for 7 min.


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  		Table. Primers Used to Evaluate the Human Enamelin Gene

 
SSCP Analysis
For the mutation screening in the AI patients, PCR products were analyzed by the single-strand conformation polymorphism (SSCP) method according to the previous method reported (Orita et al., 1989). The PCR samples, mixed with formamide dye (95% formamide with bromophenol blue and xylenecyanol), were heated to 100°C for 5 min, quenched on ice, and then loaded onto a Gene Gel Exel (12.5%/24-well Kit; Amersham Pharmacia Biotech, Piscataway, NJ, USA). Electrophoresis was performed with the conditions of 600 V, 25 mA, and 15 W at 15°C for 90 min in a GenePhor (Amersham Pharmacia Biotech). After electrophoresis, the gel was silver-stained by means of a DNA Silver Staining Kit (Amersham Pharmacia Biotech).

Sequence Analysis
After electrophoresis, the PCR-amplified fragments were purified from the gel by means of a rapid PCR purification system (Gibco BRLTM, Life Technologies, Rockville, MD, USA), and reacted with the ABI PRISM Big Dye primer cycles Sequencing Ready Reaction Kit (Applied Biosystems). For cycle sequencing, the following conditions was used: 10 sec at 96°C, 5 sec at 50°C, and 4 min at 60°C (25 cycles). The sequencing reactions were analyzed on an ABI PRISM Genetic Analyzer 310 (Applied Biosystems).


   RESULTS
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS & METHODS
 RESULTS
DISCUSSION
 REFERENCES
 
Clinical Features
We asked the family members whether there was any systemic or generalized disease associated with the family. The affected members of the family exhibited enamel hypoplasia without any general complications. The male proband boy and his younger brother showed hypoplastic enamel in both their deciduous and permanent teeth (Fig. 1B III-1, III-2Go) that resulted in hypersensitivity to cold stimuli. Anterior open bite was found in both of them in the primary dentition (Fig. 1B III-1Go). Their father showed local hypoplastic enamel defects demonstrating a horizontal lesion involving primarily the middle third of the permanent teeth (Fig. 1B II-1Go). In the molars, the lesion was further extended occlusally. In contrast to his sons, he showed normal sensitivity to cold stimuli in the affected teeth. We could not confirm the phenotype of their deciduous teeth, but as far as their permanent teeth were concerned, the affected brothers showed a more yellowish enamel than that of their father, and the enamel hypoplasia was more pronounced. Therefore, we concluded that the phenotype of AI in this family was the hypoplastic type, although the severity varied among the individual patients. Judging from this AI family’s pedigree, we considered that the inheritance pattern is autosomal-dominant. It should be noted that the probands’ paternal grandparents had normal enamel surfaces.

Mutation Analysis
    Ameloblastin gene
We screened all 13 exons of the ameloblastin gene by the SSCP followed by sequence analysis. There was no mutation in the ameloblastin gene in this family (data not shown).

    Enamelin gene
Since a recent report demonstrated that a mutation in the enamelin gene caused AI (Rajpar et al., 2001), we next targeted the enamelin gene. The size of the PCR fragments obtained by use of the primers listed in the TableGo was the same among the affected and the control individuals (data not shown). For the screening of mutations in the AI patients, all PCR products were analyzed by the SSCP method. A variant SSCP pattern was found in the fragment including exon 9 of the enamelin gene. This variation was present in all affected members but was not found in unaffected or in more than 100 control individuals (Fig. 2AGo).



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  		Figure 2. Detection of the enamelin gene mutation in the AI family. (A) Screening by SSCP analysis. SSCP analysis of exon 9 of the enamelin gene from AI family individuals and a normal control. An abnormal pattern is detected in the affected individuals (III-1, III-2, and II-1) but not in the unaffected family members (I-1, 2 and II-2, 3) or control (C). The symbols above each lane denote individuals shown in Fig. 1AGo. (B) DNA sequencing analysis. The affected individual III-1 has a single-G deletion at the exon 9-intron 9 boundary of the enamelin gene. The same deletion was confirmed in the other affected members (II-1 and III-2) but not in unaffected members (I-1, 2 and II-2, 3) or control individuals. Normal and mutant sequences at the exon 9-intron 9 boundary of the enamelin gene are indicated at top.

 
Sequencing of the DNA fragment revealed a deletion of a single-G from a series of 7 G residues (AGGGGGGGTAAGT->AGGGGGGTAAGT) at the exon 9-intron 9 boundary of the enamelin gene (Fig. 2BGo, GenBank accession number AF530444). This mutation was confirmed in all affected individuals but was not found in unaffected family members or in the controls. The normal boundary of exon 9-intron 9 consists of AGGGGGG (3' site of exon 9)/GTAAGT (5' site of intron 9), where either a G of exon 9 or a G at a splice donor site of intron 9 has been deleted.


   DISCUSSION
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS & METHODS
 RESULTS
 DISCUSSION
REFERENCES
 
In this study, we found a mutation in the enamelin gene from a Japanese family with an autosomal-dominant AI. Mutational analysis revealed a single-G deletion at the exon 9-intron 9 boundary of the enamelin gene. The sequence of the mutation site in the enamelin gene is a series of 7 G residues at the 3' end of exon 9 and the 5' (donor) site of intron 9. Therefore, we cannot determine which "G" (in the exon or the intron) is involved in this deletion mutation. Although studies of the mutant enamelin mRNA of patients would provide useful information, this was not available because the patients’ tooth germ cells were the only samples obtained for the studies.

Two different consequences are proposed for this mutation. The new splice donor site created by a single G deletion (GT->TA) no longer functions properly as a splice donor, resulting in a splice mutation with the probable skipping of exon 9 from the mRNA. This would result in a deletion of 18 amino acids from enamelin protein (Fig. 3AGo) and lead to protein instability. On the other hand, if the splice donor site function is preserved, the deletion could cause the alteration of the reading frame to result in a premature termination codon within exon 10 of the enamelin gene (Fig. 3BGo). Thus, both possibilities could result in abnormal protein synthesis and lead to disease. To investigate which scenario would be most likely, we used a Splice Site Prediction program by Neural Network presented by The Berkeley Drosophila Genome Project shown on the following Web site (http://www.fruitfly.org/index.html). To perform structural analysis of the consequences of disruption of the exon-intron border in the case of this single-G deletion of the enamelin gene, we examined the sequence of the mutant enamelin gene using this program. This analysis revealed that this mutation would neither affect the exon-intron structure nor alter the splice donor site of the intron 9. The effect of this deletion, therefore, is suggested to result in an alteration of the reading frame from exon 9, and the introduction of a premature stop codon at 277 in the 5' region of exon 10 (Fig. 3BGo).



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  		Figure 3. Possible consequences of a single-G deletion at the exon 9-intron 9 boundary of the enamelin gene. (A) Splice mutation. The mutation may introduce a non-functional splice donor site of intron 9, resulting in a probable skipping of exon 9 from the enamelin mRNA. In this case, 18 amino acids (179-196) coded by exon 9 would be absent from the protein. (B) Frame shift mutation. The mutation may preserve the functional splice donor site, resulting in a downstream frame shift at amino acid 196; this would create a premature stop codon at 277.

 
Although there is an obvious difference in the phenotype between the affected brothers and their father, they all have the same mutation in the enamelin gene. What are the differences among them? Since neither of the probands’ paternal grandparents have the mutation in the enamelin gene, we speculated that a de novo mutation has occurred in the enamelin gene of the father, although their parent-child relationship was not fully verified. In that case, the mutation had originated in either gamete of the paternal grandparents or during subsequent cell division after fertilization. The latter case might result in a mosaicism of tooth germ cells in the father. Thus, this scenario might account for the reason why the father exhibited a less severe AI phenotype compared with his sons. However, an alternative scenario might be that the severity in this form of AI is affected by the other factors relating to the enamel formation in conjunction with this enamelin mutation. The phenotype of patients with X-linked AI who harbor mutations in the amelogenin gene is also likely to be varied. Further studies are needed to clarify the relation between the phenotype of AI and mutations in the genes concerned with the enamel formation.


   ACKNOWLEDGMENTS
 
We thank Prof. Michael Dixon, University of Manchester, UK, for kindly providing us with the PCR primer information to amplify the enamelin gene. This work is supported by the H12-genome-003 grant from the Ministry of Health, Labor and Welfare, Japan, and by grants 13670776 and 12470455 from the Ministry of Education, Culture, Sports, Science and Technology, Japan.

Received November 20, 2001; Last revision July 29, 2002; Accepted August 7, 2002


   REFERENCES
TOP
 ABSTRACT
 INTRODUCTION
 MATERIALS & METHODS
 RESULTS
 DISCUSSION
 REFERENCES
 
Bäckman B, Holm AK (1986). Amelogenesis imperfecta: prevalence and incidence in a northern Swedish county. Community Dent Oral Epidemiol 14:43–47.[Medline]

Dong J, Gu TT, Simmons D, MacDougall M (2000). Enamelin maps to human chromosome 4q21 within the autosomal dominant amelogenesis imperfecta locus. Eur J Oral Sci 108:353–358.[Medline]

Hart S, Hart T, Gibson C, Wright JT (2000). Mutational analysis of X-linked amelogenesis imperfecta in multiple families. Arch Oral Biol 45:79–86.[Medline]

Hu CC, Hart TC, Dupont BR, Chen JJ, Sun X, Qian Q, et al. (2000). Cloning human enamelin cDNA, chromosomal localization, and analysis of expression during tooth development. J Dent Res 79:912–919.[Abstract/Free Full Text]

Hu JC, Zhang CH, Yang Y, Kärrman-Mardh C, Forsman-Semb K, Simmer JP (2001). Cloning and characterization of the mouse and human enamelin genes. J Dent Res 80:898–902.[Abstract/Free Full Text]

Kärrman C, Bäckman B, Holmgren G, Forsman K (1996). Genetic heterogeneity of autosomal dominant amelogenesis imperfecta demonstrated by its exclusion from the AIH2 region on human chromosome 4Q. Arch Oral Biol 41:893–900.[Medline]

Kärrman C, Bäckman B, Dixon M, Holmgren G, Forsman K (1997). Mapping of the locus for autosomal dominant amelogenesis imperfecta (AIH2) to a 4-Mb YAC contig on chromosome 4q11-q21. Genomics 39:164–170.[Medline]

Kärrman-Mårdh C, Bäckman B, Simmons D, Golovleva I, Gu TT, Holmgren G, et al. (2001). Human ameloblastin gene: genomic organization and mutation analysis in amelogenesis imperfecta patients. Eur J Oral Sci 109:8–13.[Medline]

Lagerström M, Dahl N, Nakahori Y, Nakagome Y, Backman B, Landegren U, et al. (1991). A deletion in the amelogenin gene (AMG) causes X-linked amelogenesis imperfecta (AIH1). Genomics 10:971–975.[Medline]

Lagerström-Fermer M, Nilsson M, Bäckman B, Salido E, Shapiro L, Pettersson U, et al. (1995). Amelogenin signal peptide mutation: correlation between mutations in the amelogenin gene (AMGX) and manifestations of X-linked amelogenesis imperfecta. Genomics 26:159–162.[Medline]

MacDougall M, DuPont BR, Simmons D, Reus B, Krebsbach P, Kärrman C, et al. (1997). Ameloblastin gene (AMBN) maps within the critical region for autosomal dominant amelogenesis imperfecta at chromosome 4q21. Genomics 41:115–118.[Medline]

Ooya K, Nalbandian J, Noikura T (1988). Autosomal recessive rough hypoplastic amelogenesis imperfecta. A case report with clinical, light microscopic, radiographic, and electron microscopic observations. Oral Surg Oral Med Oral Pathol 65:449–458.[Medline]

Orita M, Suzuki Y, Sekiya T, Hayashi K (1989). Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction. Genomics 5:874–879.[Medline]

Rajpar MH, Harley K, Laing C, Davies RM, Dixon MJ (2001). Mutation of the gene encoding the enamel-specific protein, enamelin, causes autosomal-dominant amelogenesis imperfecta. Hum Mol Genet 10:1673–1677.[Abstract/Free Full Text]

Robinson C, Brookes SJ, Shore RC, Kirkham J (1998). The developing enamel matrix: nature and function. Eur J Oral Sci 106:282–291.

Sekiguchi H, Minaguchi K, Machida Y, Yakushiji M (1998). PCR detection of the human amelogenin gene and its application to the diagnosis of amelogenesis imperfecta. Bull Tokyo Dent Coll 39:275–285.[Medline]

Uchida T, Tanabe Y, Fukae M, Shimizu M (1991). Immunocytochemical and immunochemical detection of a 32 kDa nonamelogenin and related proteins in porcine tooth germs. Arch Histol Cytol 54:527–538.[Medline]

Witkop CJ Jr (1988). Amelogenesis imperfecta, dentinogenesis imperfecta and dentin dysplasia revisited: problems in classification. J Oral Pathol 17:547–553.[Medline]

Witkop CJ Jr, Sauk JJ Jr (1976). Heritable defects of enamel. In: Oral facial genetics. Stewart RE, Prescott GH, editors. St. Louis: C.V. Mosby, pp. 151-226.




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