Recurrent de novo point mutations in lamin A cause Hutchinson–Gilford progeria syndrome

Nature - Tập 423 Số 6937 - Trang 293-298 - 2003
Maria Eriksson1, W. Ted Brown2, Leslie B. Gordon3,4, Michael W. Glynn5, Joel I. Singer6, Laura J. Scott6, Michael R. Erdos5, Christiane M. Robbins5, Tracy Moses5, Peter Berglund7, Amalia Dutra5, Evgenia Pak5, Sandra G. Durkin5, Antonei B. Csóka8, Michael Boehnke6, Thomas W. Glover5, Francis S. Collins5
1Department of Human Genetics New York State Institute for Basic Research in Developmental Disabilities Staten Island, New York 10314, USA
2Department of Human Genetics, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, USA
3Department of Anatomy and Cellular Biology, Tufts University School of Medicine, Boston
4Department of Pediatrics, Rhode Island Hospital, Providence, USA
5National Human Genome Research Institute, National Institutes of Health, Bethesda, USA
6Department of Human Genetics, and Department of Biostatistics, University of Michigan, Ann Arbor, USA
7National Human Genome Research Institute, and Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, USA
8Department of Molecular Biology, Cell Biology, & Biochemistry, Brown University, Providence, USA

Tóm tắt

Từ khóa


Tài liệu tham khảo

DeBusk, F. L. The Hutchinson-Gilford progeria syndrome. J. Pediat. 80, 697–724 (1972)

Baker, P. B., Baba, N. & Boesel, C. P. Cardiovascular abnormalities in progeria. Case report and review of the literature. Arch. Pathol. Lab. Med. 105, 384–386 (1981)

Burke, B. & Stewart, C. L. Life at the edge: the nuclear envelope and human disease. Nature Rev. 3, 575–585 (2002)

Genschel, J. & Schmidt, H.-J. Mutations in the LMNA gene encoding lamin A/C. Hum. Mutat. 16, 451–459 (2000)

Brown, W. T. Human mutations affecting aging—a review. Mech. Aging Dev. 9, 325–336 (1979)

Brown, W. T., Zebrowser, M. & Kieras, F. J. in Genetic Effects on Aging II (ed. Harrison, D. E.) 521–542 (Telford, Caldwell, New Jersey, 1990)

Trevas-Maciel, A. Evidence for autosomal recessive inheritance of progeria (Hutchinson Gilford). Am. J. Med. Genet. 31, 483–487 (1988)

Khalifa, M. M. Hutchinson-Gilford progeria syndrome: report of a Libyan family and evidence of autosomal recessive inheritance. Clin. Genet. 35, 125–132 (1989)

Lander, E. S. & Botstein, D. Homozygosity mapping: a way to map human recessive traits with the DNA of inbred children. Science 236, 1567–1570 (1987)

Brown, W. T. Progeria: a human disease model of accelerated aging. Am. J. Clin. Nutr. 55, 1222S–1224S (1992)

Fisher, D. Z., Chaudhary, N. & Blobel, G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl Acad. Sci. USA 83, 6450–6454 (1986)

Lin, F. & Worman, H. J. Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C. J. Biol. Chem. 268, 16321–16326 (1993)

Shiang, R. et al. Mutations in the transmembrane domain of FGFR3 cause the most common genetic form of dwarfism, achondroplasia. Cell 78, 335–342 (1994)

Smith, A. S., Wiznitzer, M., Karaman, B. A., Horwitz, S. J. & Lanzieri, C. F. MRA detection of vascular occusion in a child with progeria. Am. J. Neuroradiol. 14, 441–443 (1993)

Pulkkinen, L., Bullrich, F., Czarnecki, P., Weiss, L. & Uitto, J. Maternal uniparental disomy of chromosome 1 with reduction to homozygosity of the LAMB3 locus in a patient with Herlitz junctional epidermolysis bullosa. Am. J. Hum. Genet. 61, 611–619 (1997)

Gelb, B. D. et al. Paternal uniparental disomy for chromosome 1 revealed by molecular analysis of a patient with pycnodysostosis. Am. J. Hum. Genet. 62, 848–854 (1998)

Delgado-Luengo, W. et al. Del(1)(q23) in a patient with Hutchinson-Gilford progeria. Am. J. Med. Genet. 113, 298–301 (2002)

Lutz, R. J., Trujillo, M. A., Denham, K. S., Wenger, L. & Sinensky, M. Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc. Natl Acad. Sci. USA 89, 3000–3004 (1992)

Sinensky, M. et al. The processing pathway of prelamin A. J. Cell Sci. 107, 61–67 (1994)

Hennekes, H. & Nigg, E. A. The role of isoprenylation in membrane attachment of nuclear lamins, a single point mutation prevents the proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J. Cell Sci. 107, 1019–1029 (1994)

Eggert, M. et al. Identification of novel phosphorylation sites in murine A-type lamins. Eur. J. Biochem. 213, 659–671 (1993)

Pendas, A. M. et al. Defective prelamin A processing and muscular and adipocyte alterations in Zmpste24 metalloproteinase-deficient mice. Nature Genet. 31, 94–99 (2002)

Bergo, M. O. et al. Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect. Proc. Natl Acad. Sci. USA 99, 13049–13054 (2002)

Sullivan, T. et al. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J. Cell Biol. 147, 913–920 (1999)

Smith, C. The detection of linkage in human genetics. J. R. Stat. Soc. B 15, 153–184 (1953)

Casper, A. M., Nghiem, P., Arlt, M. F. & Glover, T. W. ATR regulates fragile site stability. Cell 111, 779–789 (2002)

De Sandre-Giovannoli, A. et al. Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. Am. J. Hum. Genet. 70, 726–736 (2002)

Speckman, R. A. et al. Mutational and haplotype analyses of families with familial partial lipodystrophy (Dunnigan variety) reveal recurrent missense mutations in the globular C-terminal domain of lamin A/C. Am. J. Hum. Genet. 66, 1192–1198 (2000); erratum 67, 775 (2000)