Human Molecular Genetics, 2000, Vol. 9, No. 9 1453-1459
© 2000 Oxford University Press
Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
INSERM UR523, Institut de Myologie, GH Pitié-Salpétrière, 75013 Paris, France, and 1Department of Neurology, Academic Medical Centre, University of Amsterdam, The Netherlands
Received 8 March 2000; Accepted 29 March 2000.
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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LGMD1B is an autosomal dominantly inherited, slowly progressive limb girdle muscular dystrophy, with age-related atrioventricular cardiac conduction disturbances and the absence of early contractures. The disease has been linked to chromosome 1q11–q21. Within this locus another muscular dystrophy, the autosomal dominant form of Emery–Dreifuss muscular dystrophy (AD-EDMD) has recently been mapped and the corresponding gene identified. AD-ADMD is characterized by early contractures of elbows and Achilles tendons and a humero-peroneal distribution of weakness combined with a cardiomyopathy with conduction defects. The disease gene of AD-EDMD is LMNA which encodes lamins A/C, two proteins of the nuclear envelope. In order to identify whether or not LGMD1B and AD-EDMD are allelic disorders, we carried out a search for mutations in the LMNA gene in patients with LGMD1B. For this, PCR/SSCP/sequencing screening was carried out for the 12 exons of LMNA on DNA samples of individuals from three LGMD1B families that were linked to chromosome 1q11–q21. Mutations were identified in all three LGMD1B families: a missense mutation, a deletion of a codon and a splice donor site mutation, respectively. The three mutations were identified in all affected members of the corresponding families and were absent in 100 unrelated control subjects. The present identification of mutations in the LMNA gene in LGMD1B demonstrates that LGMD1B and AD-EDMD are allelic disorders. Further analysis of phenotype–genotype relationship will help to clarify the variability of the phenotype observed in these two muscular dystrophies.
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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Limb girdle muscular dystrophies (LGMDs) represent a genetically heterogeneous group of myogenic disorders with a limb girdle distribution of weakness. The inheritance pattern in LGMD is also heterogeneous. Four dominant (LGMD1) and eight recessive (LGMD2) forms have been individualized to date. The disease genes of one dominant and seven recessive forms have been identified (1–8). For the other forms, chromosomal locations have been described or are still unknown.
The LGMD1B form is inherited as an autosomal dominant trait. It is slowly progressive, with age-related atrioventricular cardiac conduction disturbances and dilated cardiomyopathy (DCM), and absence of early contractures (9). The locus of the disease has been mapped to chromosome 1q11–q21, with maximum LOD scores >6 at 
= 0, which is considered to be a definite proof of genetic linkage (10). Within this locus another muscular dystrophy, the autosomal dominant form of Emery–Dreifuss muscular dystrophy (AD-EDMD) has recently been mapped by some of us, and the corresponding gene identified (11). AD-EDMD is characterized by early contractures of the elbow and Achilles tendons, a humero-peroneal distribution of weakness, combined with a cardiomyopathy with atrioventricular conduction defects (12,13). Mutations were identified in the LMNA gene, which encodes lamins A/C, two proteins of the nuclear envelope (11). Lamins A/C are members of the intermediate filament multigene family. They form dimers through their rod domain and interact with chromatin and integral proteins of the inner nuclear membrane through binding sites located in their rod domain and their carboxy-terminal globular tail (14–19). In order to identify whether or not LGMD1B and AD-EDMD are allelic disorders, we carried out a search for mutations in the LMNA gene in patients with LGMD1B.
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RESULTS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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The 12 exons of LMNA were screened by PCR/single strand conformation polymorphism (SSCP)/sequencing as previously described (11) in 79 members of the three LGMD1B families, out of whom 31 individuals were diagnosed as having slowly progressive autosomal dominant LGMD (9) (Fig. 1).
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In family A, among the 34 subjects analysed, 14 were diagnosed as having LGMD1B (Fig. 1a). An abnormal SSCP pattern was observed for the PCR fragment of exon 3 in the 14 affected members of the family (Fig. 2a). The sequencing of this abnormal conformer of exon 3 identified an in-frame deletion of codon 208, delAAG, eliminating the corresponding lysine 208 (delK208). This mutation was not found in healthy pedigree members (Fig. 1a). These results are in complete agreement with the linkage data reported previously (10). Furthermore, the mutation was not found in 200 normal chromosomes.
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We analysed the DNA of 36 members of family B, among whom 12 were diagnosed as having LGMD1B (9) (Fig. 1b). Three family members, IV-5, IV-35 and IV-36, who had been identified in the first report as affected individuals on the basis of reported muscle weakness and equivocal weakness on examination (9), were re-examined and turned out not to be affected. As for family members III-38 and IV-9, their clinical follow-up demonstrated that they were affected. An abnormal SSCP conformer was observed for the PCR fragment of exon 9 in 14 individuals of family B, i.e. the 12 affected members and two young unaffected subjects, IV-8 and IV-22, who were 19 and 21 years old, respectively, at the time of examination (Fig. 2b). Both had normal neurological and cardiological investigations at that time (5 years before mutation analysis). As yet, neither of them has been re-examined. The abnormal pattern was absent in the PCR fragment of the remaining healthy family members. The sequencing of this conformer identified a transversion in the consensus splice donor site of intron 9, gtaag>gtaac. This mutation was thus present in the 12 affected members and in IV-8 and IV-22 and was absent in the remaining healthy members (Fig. 1b). These results are in complete agreement with the linkage data reported previously (10). The mutation was not found in 200 normal chromosomes.
The mutation in the consensus splice donor site of intron 9 (gtaag>gtaac) potentially leads to abnormal splicing of the LMNA mRNA (Fig. 3a). RT–PCR on fibroblast transcripts of a family B member (III-8), using specific exonic primers localized in exons 7 and 10 were performed in order to check the consequences of this mutation at the RNA level. The results showed the presence of normally spliced LMNA mRNA in this affected subject as well as in a healthy control subject (377 bp PCR fragment) and an additional PCR fragment (798 bp) present only in the affected individual III-8 (Fig. 3b). The sequencing of these two PCR products revealed that the 798 bp fragment corresponds to the retention of intron 9 within the mRNA of subject III-8 (Fig. 3c). This aberrant transcript encodes 536 normal lamin A/C residues, followed by 35 new amino acids and a premature stop codon, potentially leading to a truncated protein of 571 amino acids, lacking half of the globular tail domain of lamins A/C (Fig. 3a). Given the consequences of this mutation in the splice donor site of intron 9 at the mRNA level and the segregation of this mutation in family B, this is likely to be a disease-causing mutation.
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In family C, a family living in the Caribbean, DNA samples of eight members were analysed. In the previous report we reported the data of three affected members (II-5, 6 and 7) who lived in The Netherlands and were examined by one of us (A.J.v.d.K.). Two other family members (II-2 and 4) were reported to have similar symptoms. For member II-2 information from her cardiologist was available (9) (Fig. 1c). An abnormal SSCP conformer (Fig. 2C) was found in exon 6 for the five affected members and in two healthy subjects, II-8 and II-9, who still live in Curacao, and were, therefore, not examined by us (Fig. 1c). The sequencing of this abnormal conformer of exon 6 identified a guanine-to-adenine transition, CGC>CAC, resulting in a missense mutation that changes the arginine 377 to a histidine (R377H). This mutation was found neither in the healthy member II-1 (Fig. 1c) nor in 200 normal chromosomes.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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We identified three mutations in the lamins A/C gene (LMNA) in affected patients of three families that were described previously with LGMD1B clinical features (9) that were linked to locus 1q11–q21 (10). The three LMNA mutations were not found in 100 unrelated control subjects. In family A, the mutation was not found in unaffected family members. In families B and C four asymptomatic subjects showed the mutation. The family members in family B were 18 and 21 years old, respectively, at the time of examination. From the members of family C, only DNA was available. Clinical examination was not feasible since they live in Curacao. An in-frame deletion in LMNA exon 3 (delK208) and a missense mutation in LMNA exon 6 (R377H) were found in affected members of families A and C, respectively (Fig. 5). These two LMNA mutations affect amino acids that are conserved through different species and different lamins (Fig. 4). These amino acids are localized in the central rod domain that is implicated in the dimerization of lamins (14,15). The family C mutation, R377H, is located within the 32 amino acids highly conserved in all intermediate filaments at the end of the
-helix rod domain (14). By a systematic mutagenesis of this 32 amino acid region, Heald et al. (20) showed that the R377H mutation abolishes the assembly of normal nuclear lamina. On the other hand, mutations affecting the rod domain of keratin intermediate filaments, implicated in epidermolysis bullosa simplex, lead to abnormal dimerization of the mutant keratins (21,22). One might thus hypothesize that the disturbance of the lamina network and disruption of the nuclear architecture would be the first events leading to the disease in LGMD1B patients with mutations in the rod domain of lamins A/C.
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The third LMNA mutation identified in family B is a transversion in the splice donor site of intron 9 (Fig. 5). The consequences of this mutation were checked at the mRNA level on the only tissue available in family B, the skin fibroblasts of patient III-8. The results showed that the splice donor site mutation leads to an aberrant LMNA transcript with the retention of intron 9 and a frameshift at position 536 (Fig. 3), which potentially leads to a truncated protein of 571 amino acids, lacking half of the globular tail domain of lamins A/C. Carboxy-terminal deletions of lamin A/C were produced by the introduction of stop codons in the full-length human lamin A/C cDNAs at positions 550 and 554 (23). Transfections in CHO cells of these mutant cDNAs demonstrated structural alterations of both the nuclear envelope and the nucleus (23), thus suggesting that the splice donor site mutation identified in family B may perturb the nuclear structure. Furthermore, a knock-out of mouse LMNA through the deletion of exons 8–11 was reported recently (24). These mice lack detectable lamins A/C and demonstrate a dystrophic condition related to EDMD with the appearance of skeletal and cardiac muscle alterations and perturbations of the nuclear envelope (24).
The present identification of mutations in the lamins A/C gene in LGMD1B patients demonstrates that LGMD1B and AD-EDMD are allelic disorders. AD-EDMD is a disorder characterized by early contractures of the Achilles tendons, elbows and postcervical muscles, slowly progressive wasting and weakness with a predominant humero-peroneal distribution and cardiomyopathy with conduction defects (12,13). Predominantly myopathic changes on electromyography (EMG) and muscle biopsy have been described. In contrast, LGMD1B-affected family members present with slowly progressive pelvic girdle weakness with only late involvement of the humeral muscles and sparing of the peroneal and tibial muscles (9). In six of the LGMD patients (AIII-26, AIII-27, BIII-14, BIV-19, BIV-37) calf enlargement was seen which has been an exclusion criterion for EDMD. Early contractures of neck, spine, elbows and Achilles tendons, while a salient feature in EDMD, were absent in LGMD1B patients. In all but two of the affected LGMD patients (BIII-16, BIV-37) neuromuscular symptoms preceded the cardiological. The AV conduction disturbances were age-related, whereas in EDMD cardiological involvement may occur at any age or may even be present at the very onset (13,25,26). In LGMD, EMG and muscle biopsy were consistent with a mild muscular dystrophy (9).
Even though the same disease-causing mutations underlies AD-EDMD and LGMD1B, the phenotypes nevertheless differ due to additional factors, both genetic and non-genetic. These same factors have been postulated for the chromosome 2p-linked conditions (27), since both LGMD2B and Miyoshi myopathy segregate with the same haplotype (28) and have mutations in the dysferlin gene (29,30). However, LGMD2B patients present with proximal myopathy, whereas Miyoshi myopathy patients manifest predominantly distal wasting and weakness. In two families, both phenotypes have been found (28,31). This variability in the clinical pictures was also reported very recently for a lamin A/C mutation (32). A single nucleotide deletion in LMNA exon 6 was identified in a family in which three phenotypes were described, a DCM with EDMD-like skeletal muscle abnormalities, DCM with LGMD-like skeletal muscle abnormalities and pure DCM with conduction defects (32). In addition, five mutations in LMNA were reported in families with a form of dilated cardiomyopathy associated with conduction defect disease (DCM-CD) (33). These five LMNA mutations affect the amino acids of the central rod domain of both lamins A and C, or the specific tail domain of lamin C. Finally, very recently, missense mutations on codons 482 and 486, localized in exon 8 of LMNA, were reported to be implicated in Dunningan-type familial partial lipodystrophy (FLPD) (34,35). Patients with FPLD are born with normal fat distribution, but then lose subcutaneous fat from their extremities, trunk and gluteal region after the onset of puberty. The regional distribution of degeneration of adipocytes is similar to that of muscle weakness observed in EDMD. Thus, LMNA is implicated in two neuromuscular disorders, AD-EDMD and LGMD1B, in cardiomyopathies with conduction defect (DCM-CD), and in a degenerative disorder of the adipose tissue, FPLD. Further analysis of phenotype–genotype relationships will help to clarify the variability of the phenotypes observed in these different diseases.
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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Subjects
Seventy-nine members of three LGMD1B families were analysed (34 samples from family A, 36 from family B, and 8 from family C) who originated from The Netherlands, Surinam, and the Caribbean, respectively (9). Symmetrical weakness started in the proximal lower limb muscles, and gradually upper limb muscles also became affected. Early contractures of the spine were absent. Contractures of elbows or Achilles tendons were either minimal or late. Serum creatine kinase was normal to moderately elevated. EMG and muscle biopsy were consistent with a mild muscular dystrophy. Cardiological abnormalities, found in more than half of the patients, included dysrhythmias and atrioventricular conduction disturbances presenting as bradycardial, syncopal attacks, necessitating pacemaker implantation, and sudden cardiac death. There was a significant relationship between the severity of AV conduction disturbances and age. In nearly all patients neuromuscular symptoms preceded cardiological involvement. The clinical data and linkage analysis studies have been described in detail by van der Kooi et al. (9,10).
Genetic analysis
Genomic DNA was extracted from blood samples taken from families members as described (10). Mutation analysis in LMNA was performed by SSCP on PCR fragments of each exon amplified from genomic DNA using a set of primers flanking the intron/exon boundaries (36). PCR fragments that gave abnormal conformers by SSCP were sequenced as described previously (11). By SSCP analysis, control DNA samples of 100 unrelated individuals were checked for the presence of all LMNA mutations identified.
RNA isolation, cDNA synthesis and LMNA cDNA amplifications
Total cellular RNA was isolated from skin fibroblasts of patient III-8 of family B using RNA plus (Quantum Biotechnology, Montreuil-sous-Bois, France), and the cDNA synthesis was performed as previously described (37). The cDNA products were amplified in a 50 µl PCR using two exonic primers (forward primer in exon 7: 5'-CC GTG GAG GAG GTG GAT GAG-3' and reverse primer in exon 10: 5'-GAC CTG CTC CAT CAC CAC CAC-3') and a touchdown PCR protocol between 70°C and 60°C. The sizes of normal and mutated cDNA-PCR fragments were assessed on agarose gels. After extraction and purification of the normal and putative mutated cDNA, they were sequenced as described previously (11).
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ACKNOWLEDGEMENTS |
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We are indebted to the family members for their invaluable participation. We thank C. Wisnewsky for her excellent technical assistance and A. Rouche for the supervision of Adobe Photoshop image analysis. This work was supported by INSERM and the Association Française contre les Myopathies (grant no. 6710).
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FOOTNOTES |
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+ To whom correspondence should be addressed at INSERM UR523–Institut de Myologie, Bâtiment Babinski, G.H. Pitié-Salpétrière, 47 boulevard de l’Hôpital, 75651 Paris cedex 13, France. Tel: +33 1 42 16 57 23; Fax: +33 1 42 16 57 00; Email: g.bonne@myologie.chups.jussieu.fr
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J. Y. Ji, R. T. Lee, L. Vergnes, L. G. Fong, C. L. Stewart, K. Reue, S. G. Young, Q. Zhang, C. M. Shanahan, and J. Lammerding Cell Nuclei Spin in the Absence of Lamin B1 J. Biol. Chem., July 6, 2007; 282(27): 20015 - 20026. [Abstract] [Full Text] [PDF]
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S. Spuler, T. Kalbhenn, J. Zabojszcza, F.K.H. van Landeghem, A. Ludtke, K. Wenzel, M. Koehnlein, M. Schuelke, L. Ludemann, and H. H. Schmidt Muscle and nerve pathology in Dunnigan familial partial lipodystrophy Neurology, February 27, 2007; 68(9): 677 - 683. [Abstract] [Full Text] [PDF]
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Y. Wang, A. J. Herron, and H. J. Worman Pathology and nuclear abnormalities in hearts of transgenic mice expressing M371K lamin A encoded by an LMNA mutation causing Emery-Dreifuss muscular dystrophy Hum. Mol. Genet., August 15, 2006; 15(16): 2479 - 2489. [Abstract] [Full Text] [PDF]
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R. T. Nitta, S. A. Jameson, B. A. Kudlow, L. A. Conlan, and B. K. Kennedy Stabilization of the Retinoblastoma Protein by A-Type Nuclear Lamins Is Required for INK4A-Mediated Cell Cycle Arrest. Mol. Cell. Biol., July 1, 2006; 26(14): 5360 - 5372. [Abstract] [Full Text] [PDF]
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C. F. Morel, M. A. Thomas, H. Cao, C. H. O'Neil, J. G. Pickering, W. D. Foulkes, and R. A. Hegele A LMNA Splicing Mutation in Two Sisters with Severe Dunnigan-Type Familial Partial Lipodystrophy Type 2 J. Clin. Endocrinol. Metab., July 1, 2006; 91(7): 2689 - 2695. [Abstract] [Full Text] [PDF]
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K. N. Jacob, F. Baptista, H. G. dos Santos, J. Oshima, A. K. Agarwal, and A. Garg Phenotypic Heterogeneity in Body Fat Distribution in Patients with Atypical Werner's Syndrome Due to Heterozygous Arg133Leu Lamin A/C Mutation J. Clin. Endocrinol. Metab., December 1, 2005; 90(12): 6699 - 6706. [Abstract] [Full Text] [PDF]
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F. Lin, J. M. Morrison, W. Wu, and H. J. Worman MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-{beta} signaling Hum. Mol. Genet., February 1, 2005; 14(3): 437 - 445. [Abstract] [Full Text] [PDF]
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E. Markiewicz, M. Ledran, and C. J. Hutchison Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro J. Cell Sci., January 15, 2005; 118(2): 409 - 420. [Abstract] [Full Text] [PDF]
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T. Arimura, A. Helbling-Leclerc, C. Massart, S. Varnous, F. Niel, E. Lacene, Y. Fromes, M. Toussaint, A.-M. Mura, D. I. Keller, et al. Mouse model carrying H222P-Lmna mutation develops muscular dystrophy and dilated cardiomyopathy similar to human striated muscle laminopathies Hum. Mol. Genet., January 1, 2005; 14(1): 155 - 169. [Abstract] [Full Text] [PDF]
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M. C. Vantyghem, P. Pigny, C. A. Maurage, N. Rouaix-Emery, T. Stojkovic, J. M. Cuisset, A. Millaire, O. Lascols, P. Vermersch, J. L. Wemeau, et al. Patients with Familial Partial Lipodystrophy of the Dunnigan Type Due to a LMNA R482W Mutation Show Muscular and Cardiac Abnormalities J. Clin. Endocrinol. Metab., November 1, 2004; 89(11): 5337 - 5346. [Abstract] [Full Text] [PDF]
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E. Mercuri, M. Poppe, R. Quinlivan, S. Messina, M. Kinali, L. Demay, J. Bourke, P. Richard, C. Sewry, M. Pike, et al. Extreme Variability of Phenotype in Patients With an Identical Missense Mutation in the Lamin A/C Gene: From Congenital Onset With Severe Phenotype to Milder Classic Emery-Dreifuss Variant Arch Neurol, May 1, 2004; 61(5): 690 - 694. [Abstract] [Full Text] [PDF]
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J. Kirschner and C. G. Bonnemann The Congenital and Limb-Girdle Muscular Dystrophies: Sharpening the Focus, Blurring the Boundaries Arch Neurol, February 1, 2004; 61(2): 189 - 199. [Abstract] [Full Text] [PDF]
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M. Tazir, H. Azzedine, S. Assami, P. Sindou, S. Nouioua, R. Zemmouri, T. Hamadouche, M. Chaouch, J. Feingold, J. M. Vallat, et al. Phenotypic variability in autosomal recessive axonal Charcot-Marie-Tooth disease due to the R298C mutation in lamin A/C Brain, January 1, 2004; 127(1): 154 - 163. [Abstract] [Full Text] [PDF]
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