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Submitted on June 10, 2005
Accepted on October 27, 2005
Center for Human Genetics, Department of Orthopedics, University Hospital of Leuven, Leuven, Belgium;Division of Nutrition and Metabolic Diseases, Department of Internal Medicine and Center for Human Nutrition, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390, U.S.A.; Center for Human Genetics, Department of Orthopedics, University Hospital of Leuven, Leuven, Genetics,Department of Nutrition and Metabolic Diseases, Department of Internal Medicine and Center for Human Nutrition, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390, U.S.A.
* To whom correspondence should be addressed. E-mail: Abhimanyu.garg{at}utsouthwestern.edu.
Context. Mutations in lamin A/C (LMNA) gene have been reported in a wide variety of disorders including lipodystrophies, cardiomyopathy, muscular dystrophies, neuropathy, mandibuloacral dysplasia, restrictive dermopathy and progeria.
Objective. To carry out mutational analysis of LMNA in a patient with novel syndrome of arthropathy, tendinous calcinosis and progeroid features.
Design. Descriptive Case Report.
Setting. Referral Center.
Patient. A 44-year-old male of European descent with an autosomal recessive arthropathy syndrome affecting predominantly the distal femora and proximal tibia in the knee with tendinous calcifications. He also had progeroid features such as pinched nose and micrognathia, cataract, alopecia, generalized lipodystrophy and sclerodermatous skin.
Interventions. None
Main Outcome Measures. Mutational analysis of lamin A/C (LMNA) and its processing enzyme, zinc metalloproteinase (ZMPSTE24) as candidate genes.
Results. We found a homozygous nucleotide substitution 1718C > T, in exon 11 of LMNA gene resulting in substitution of a well conserved residue serine at position 573 with leucine (S573L). This missense mutation only affects lamin A and not lamin C as the alternative splicing site is located in exon 10. Immunofluorescence staining of the nuclei from his skin fibroblasts showed occasional misshapen morphology.
Conclusions. The S573L homozygous LMNA mutation is associated with a novel phenotype of arthropathy, tendinous calcifications and progeroid features distinct from acro-osteolysis previously reported in patients with mandibuloacral dysplasia caused by LMNA or ZMPSTE24 mutations. Thus, arthropathy with tendinous calcifications can be added to the growing list of disorders associated with LMNA mutations.
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  A. Decaudain, M.-C. Vantyghem, B. Guerci, A.-C. Hecart, M. Auclair, Y. Reznik, H. Narbonne, P.-H. Ducluzeau, B. Donadille, C. Lebbe, et al. New Metabolic Phenotypes in Laminopathies: LMNA Mutations in Patients with Severe Metabolic Syndrome J. Clin. Endocrinol. Metab., December 1, 2007; 92(12): 4835 - 4844. [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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