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

Eriksson, Maria, Brown, W. Ted, Gordon, Leslie B., Glynn, Michael W., Singer, Joel, Scott, Laura, Erdos, Michael R., Robbins, Christiane M., Moses, Tracy Y., Berglund, Peter, Dutra, Amalia, Pak, Evgenia, Durkin, Sandra, Csoka, Antonei B., Boehnke, Michael, Glover, Thomas W., Collins, Francis S.·2003·Nature
DOI 10.1038/nature01629
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  • Mutations in genes encoding protein components of the nuclear lamina, or factors affecting their maturation and dynamics, cause accelerated aging syndromes such as Hutchinson-Gilford and Néstor-Guillermo progeria syndromes.

    “The nuclear lamina attracted the attention of aging researchers after the discovery that mutations in genes encoding protein components of this structure, or factors affecting their maturation and dynamics, cause accelerated aging syndromes such as the Hutchinson-Gilford and the Néstor-Guillermo progeria syndromes (HGPS and NGPS, respectively) (Cabanillas et al., 2011; De Sandre-Giovannoli et al.,”

    From The Hallmarks of Aging (2013) · cites this paper as Eriksson et al., 2003

    The Abstract (page not available in our copy) identifies LMNA mutations in lamin A, a nuclear-lamina component, as a cause of Hutchinson-Gilford progeria syndrome. It also describes a lamin-processing factor whose loss produces HGPS-like features in mice, but it does not establish that mutations in maturation factors cause a human progeria syndrome or address Néstor-Guillermo progeria syndrome. (LLM, conf=0.90)

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Research works printed but not linked: 28

  1. DeBusk, F. L. The Hutchinson-Gilford progeria syndrome. J. Pediat. 80, 697–724 (1972) · DOI
  2. 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)
  3. Burke, B. & Stewart, C. L. Life at the edge: the nuclear envelope and human disease. Nature Rev. 3, 575–585 (2002) · DOI
  4. Genschel, J. & Schmidt, H.-J. Mutations in the LMNA gene encoding lamin A/C. Hum. Mutat. 16, 451–459 (2000) · DOI
  5. Brown, W. T. Human mutations affecting aging—a review. Mech. Aging Dev. 9, 325–336 (1979) · DOI
  6. 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)
  7. Trevas-Maciel, A. Evidence for autosomal recessive inheritance of progeria (Hutchinson Gilford). Am. J. Med. Genet. 31, 483–487 (1988) · DOI
  8. Khalifa, M. M. Hutchinson-Gilford progeria syndrome: report of a Libyan family and evidence of autosomal recessive inheritance. Clin. Genet. 35, 125–132 (1989) · DOI
  9. 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) · DOI
  10. Brown, W. T. Progeria: a human disease model of accelerated aging. Am. J. Clin. Nutr. 55, 1222S–1224S (1992) · DOI
  11. 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) · DOI
  12. 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) · DOI
  13. 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) · DOI
  14. 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)
  15. 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) · DOI
  16. 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) · DOI
  17. Delgado-Luengo, W. et al. Del(1)(q23) in a patient with Hutchinson-Gilford progeria. Am. J. Med. Genet. 113, 298–301 (2002) · DOI
  18. 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) · DOI
  19. Sinensky, M. et al. The processing pathway of prelamin A. J. Cell Sci. 107, 61–67 (1994) · DOI
  20. 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) · DOI
  21. Eggert, M. et al. Identification of novel phosphorylation sites in murine A-type lamins. Eur. J. Biochem. 213, 659–671 (1993) · DOI
  22. 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) · DOI · Paper page
  23. 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) · DOI
  24. 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) · DOI
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  27. 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) · DOI
  28. 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) · DOI

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Metadata

Authors
Eriksson, M., Brown, W. T., Gordon, L. B., Glynn, M. W., Singer, J., Scott, L., Erdos, M. R., Robbins, C. M., Moses, T. Y., Berglund, P., Dutra, A., Pak, E., Durkin, S., Csoka, A. B., Boehnke, M., Glover, T. W., & Collins, F. S.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2003-04-25
Volume
423
Issue
6937
Pages
293-298
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature01629
Cited by
1,990
References
0
Language
en
Licence
www.springer.com/tdm (tdm)

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