The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

LMNA  -  lamin A/C

Homo sapiens

Synonyms: CDCD1, CDDC, CMD1A, CMT2B1, EMD2, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of LMNA


High impact information on LMNA

  • The protein product of LMNA is lamin A/C, which is a component of the nuclear envelope [7].
  • Through a positional cloning approach we have identified five different missense mutations in LMNA among ten kindreds and three individuals with PLD [7].
  • Heterozygous mutations in LMNA have recently been identified in kindreds with the variant form of muscular dystrophy (MD) known as autosomal dominant Emery-Dreifuss MD (EDMD-AD; ref. 7) and dilated cardiomyopathy and conduction-system disease (CMD1A) [7].
  • This region contains the lamin A/C gene (LMNA), a candidate gene encoding two proteins of the nuclear lamina, lamins A and C, produced by alternative splicing [8].
  • We carried out a genome-wide scan with a set of highly polymorphic short tandem-repeats (STR) in individuals from five well-characterized pedigrees and mapped the FPLD locus to chromosome 1q21-22 [9].

Chemical compound and disease context of LMNA


Biological context of LMNA


Anatomical context of LMNA


Associations of LMNA with chemical compounds

  • RESULTS: We found a homozygous nucleotide substitution, 1718C>T, in exon 11 of the LMNA gene, resulting in substitution of a well-conserved residue serine at position 573 with leucine (S573L) [20].
  • CONCLUSIONS: We conclude that two homozygous missense LMNA mutations involving the arginine 527 and alanine 529 residues cause MAD with subtle variations in phenotype [21].
  • RESULTS: We now report that both these patients have a novel homozygous missense mutation (c.1586C-->T; c refers to cDNA reference sequence) in LMNA that replaces a well-conserved residue alanine at position 529 to valine [21].
  • In 971 participants from the Amish Family Diabetes Study, the H566H polymorphism of LMNA was associated with metabolic syndrome diagnosed according to National Cholesterol Education Program ATP III criteria and also higher mean fasting triglyceride and lower mean high-density lipoprotein-cholesterol concentrations [22].
  • On the other hand, the R377L mutation, also located within the rod domain, is a novel mutation, although a histidine substitution instead of leucine (R377H) has been reported previously in an LGMD1B patient [23].

Regulatory relationships of LMNA


Other interactions of LMNA


Analytical, diagnostic and therapeutic context of LMNA

  • BACKGROUND: A cohort of 49 nuclear families, 40 with familial DCM and 9 with sporadic DCM (269 subjects, 105 affected), was screened for mutations in LMNA using denaturing high-performance liquid chromatography and sequence analysis [27].
  • The LMNA mutation carriers had a significantly poorer cumulative survival compared with non-carrier DCM patients: event-free survival at the age of 45 years was 31% versus 75% in non-carriers [27].
  • Immunofluorescence microscopic analysis of the patient's cultured skin fibroblasts revealed nuclear disorganization and abnormal distribution of A-type lamins, similar to that observed in patients harboring other LMNA mutations [28].
  • In radiation hybrid mapping LMNA was most significantly linked to SW270 on chromosome 4 (39 cR; LOD = 7.86) [29].
  • To identify disease-specific transcripts for EDMD, we applied a leave-one-out (LOO) cross-validation approach using LMNA patient muscle as a test data set, with reverse transcription-polymerase chain reaction (RT-PCR) validations in both LMNA and emerin patient muscle [30].


  1. Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia. Agarwal, A.K., Fryns, J.P., Auchus, R.J., Garg, A. Hum. Mol. Genet. (2003) [Pubmed]
  2. Nuclear envelope defects associated with LMNA mutations cause dilated cardiomyopathy and Emery-Dreifuss muscular dystrophy. Raharjo, W.H., Enarson, P., Sullivan, T., Stewart, C.L., Burke, B. J. Cell. Sci. (2001) [Pubmed]
  3. Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy. Ostlund, C., Bonne, G., Schwartz, K., Worman, H.J. J. Cell. Sci. (2001) [Pubmed]
  4. Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription. Capanni, C., Cenni, V., Mattioli, E., Sabatelli, P., Ognibene, A., Columbaro, M., Parnaik, V.K., Wehnert, M., Maraldi, N.M., Squarzoni, S., Lattanzi, G. Exp. Cell Res. (2003) [Pubmed]
  5. Lack of mutations in LMNA, its promoter region, and the cellular retinoic acid binding protein II (CRABP II) in HIV associated lipodystrophy. Behrens, G.M., Genschel, J., Schmidt, R.E., Schmidt, H.H. Eur. J. Med. Res. (2003) [Pubmed]
  6. Fertility and obstetrical complications in women with LMNA-related familial partial lipodystrophy. Vantyghem, M.C., Vincent-Desplanques, D., Defrance-Faivre, F., Capeau, J., Fermon, C., Valat, A.S., Lascols, O., Hecart, A.C., Pigny, P., Delemer, B., Vigouroux, C., Wemeau, J.L. J. Clin. Endocrinol. Metab. (2008) [Pubmed]
  7. LMNA, encoding lamin A/C, is mutated in partial lipodystrophy. Shackleton, S., Lloyd, D.J., Jackson, S.N., Evans, R., Niermeijer, M.F., Singh, B.M., Schmidt, H., Brabant, G., Kumar, S., Durrington, P.N., Gregory, S., O'Rahilly, S., Trembath, R.C. Nat. Genet. (2000) [Pubmed]
  8. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Bonne, G., Di Barletta, M.R., Varnous, S., Bécane, H.M., Hammouda, E.H., Merlini, L., Muntoni, F., Greenberg, C.R., Gary, F., Urtizberea, J.A., Duboc, D., Fardeau, M., Toniolo, D., Schwartz, K. Nat. Genet. (1999) [Pubmed]
  9. Localization of the gene for familial partial lipodystrophy (Dunnigan variety) to chromosome 1q21-22. Peters, J.M., Barnes, R., Bennett, L., Gitomer, W.M., Bowcock, A.M., Garg, A. Nat. Genet. (1998) [Pubmed]
  10. Type A insulin resistance syndrome revealing a novel lamin A mutation. Young, J., Morbois-Trabut, L., Couzinet, B., Lascols, O., Dion, E., Béréziat, V., Fève, B., Richard, I., Capeau, J., Chanson, P., Vigouroux, C. Diabetes (2005) [Pubmed]
  11. Analysis of the lamin A/C gene as a candidate for type II diabetes susceptibility in Pima Indians. Wolford, J.K., Hanson, R.L., Bogardus, C., Prochazka, M. Diabetologia (2001) [Pubmed]
  12. Association of LMNA 1908C/T polymorphism with cerebral vascular disease and diabetic nephropathy in Japanese men with type 2 diabetes. Liang, H., Murase, Y., Katuta, Y., Asano, A., Kobayashi, J., Mabuchi, H. Clin. Endocrinol. (Oxf) (2005) [Pubmed]
  13. Response to treatment with rosiglitazone in familial partial lipodystrophy due to a mutation in the LMNA gene. Owen, K.R., Donohoe, M., Ellard, S., Hattersley, A.T. Diabet. Med. (2003) [Pubmed]
  14. Various authentic chemoattractants mediating leukocyte adherence inhibition. Thomson, D.M. J. Natl. Cancer Inst. (1984) [Pubmed]
  15. Human laminopathies: nuclei gone genetically awry. Capell, B.C., Collins, F.S. Nat. Rev. Genet. (2006) [Pubmed]
  16. Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss muscular dystrophy. Brown, C.A., Lanning, R.W., McKinney, K.Q., Salvino, A.R., Cherniske, E., Crowe, C.A., Darras, B.T., Gominak, S., Greenberg, C.R., Grosmann, C., Heydemann, P., Mendell, J.R., Pober, B.R., Sasaki, T., Shapiro, F., Simpson, D.A., Suchowersky, O., Spence, J.E. Am. J. Med. Genet. (2001) [Pubmed]
  17. Components of the nuclear envelope and their role in human disease. Worman, H.J. Novartis Found. Symp. (2005) [Pubmed]
  18. Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C. Novelli, G., Muchir, A., Sangiuolo, F., Helbling-Leclerc, A., D'Apice, M.R., Massart, C., Capon, F., Sbraccia, P., Federici, M., Lauro, R., Tudisco, C., Pallotta, R., Scarano, G., Dallapiccola, B., Merlini, L., Bonne, G. Am. J. Hum. Genet. (2002) [Pubmed]
  19. 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. De Sandre-Giovannoli, A., Chaouch, M., Kozlov, S., Vallat, J.M., Tazir, M., Kassouri, N., Szepetowski, P., Hammadouche, T., Vandenberghe, A., Stewart, C.L., Grid, D., Lévy, N. Am. J. Hum. Genet. (2002) [Pubmed]
  20. A homozygous mutation in the lamin A/C gene associated with a novel syndrome of arthropathy, tendinous calcinosis, and progeroid features. Van Esch, H., Agarwal, A.K., Debeer, P., Fryns, J.P., Garg, A. J. Clin. Endocrinol. Metab. (2006) [Pubmed]
  21. A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia. Garg, A., Cogulu, O., Ozkinay, F., Onay, H., Agarwal, A.K. J. Clin. Endocrinol. Metab. (2005) [Pubmed]
  22. Variation in the lamin A/C gene: associations with metabolic syndrome. Steinle, N.I., Kazlauskaite, R., Imumorin, I.G., Hsueh, W.C., Pollin, T.I., O'Connell, J.R., Mitchell, B.D., Shuldiner, A.R. Arterioscler. Thromb. Vasc. Biol. (2004) [Pubmed]
  23. Identification of lamin A/C ( LMNA) gene mutations in Korean patients with autosomal dominant Emery-Dreifuss muscular dystrophy and limb-girdle muscular dystrophy 1B. Ki, C.S., Hong, J.S., Jeong, G.Y., Ahn, K.J., Choi, K.M., Kim, D.K., Kim, J.W. J. Hum. Genet. (2002) [Pubmed]
  24. Loss of lamin A/C expression revealed by immuno-electron microscopy in dilated cardiomyopathy with atrioventricular block caused by LMNA gene defects. Verga, L., Concardi, M., Pilotto, A., Bellini, O., Pasotti, M., Repetto, A., Tavazzi, L., Arbustini, E. Virchows Arch. (2003) [Pubmed]
  25. Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization. Wydner, K.L., McNeil, J.A., Lin, F., Worman, H.J., Lawrence, J.B. Genomics (1996) [Pubmed]
  26. Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation. Varela, I., Cadiñanos, J., Pendás, A.M., Gutiérrez-Fernández, A., Folgueras, A.R., Sánchez, L.M., Zhou, Z., Rodríguez, F.J., Stewart, C.L., Vega, J.A., Tryggvason, K., Freije, J.M., López-Otín, C. Nature (2005) [Pubmed]
  27. Natural history of dilated cardiomyopathy due to lamin A/C gene mutations. Taylor, M.R., Fain, P.R., Sinagra, G., Robinson, M.L., Robertson, A.D., Carniel, E., Di Lenarda, A., Bohlmeyer, T.J., Ferguson, D.A., Brodsky, G.L., Boucek, M.M., Lascor, J., Moss, A.C., Li, W.L., Stetler, G.L., Muntoni, F., Bristow, M.R., Mestroni, L. J. Am. Coll. Cardiol. (2003) [Pubmed]
  28. A new clinical condition linked to a novel mutation in lamins A and C with generalized lipoatrophy, insulin-resistant diabetes, disseminated leukomelanodermic papules, liver steatosis, and cardiomyopathy. Caux, F., Dubosclard, E., Lascols, O., Buendia, B., Chazouillères, O., Cohen, A., Courvalin, J.C., Laroche, L., Capeau, J., Vigouroux, C., Christin-Maitre, S. J. Clin. Endocrinol. Metab. (2003) [Pubmed]
  29. SNP identification, linkage and radiation hybrid mapping of the porcine lamin A/C (LMNA) gene to chromosome 4q. Wagenknecht, D., Stratil, A., Bartenschlager, H., Van Poucke, M., Peelman, L.J., Majzlík, I., Geldermann, H. J. Anim. Breed. Genet. (2006) [Pubmed]
  30. Nuclear envelope dystrophies show a transcriptional fingerprint suggesting disruption of Rb-MyoD pathways in muscle regeneration. Bakay, M., Wang, Z., Melcon, G., Schiltz, L., Xuan, J., Zhao, P., Sartorelli, V., Seo, J., Pegoraro, E., Angelini, C., Shneiderman, B., Escolar, D., Chen, Y.W., Winokur, S.T., Pachman, L.M., Fan, C., Mandler, R., Nevo, Y., Gordon, E., Zhu, Y., Dong, Y., Wang, Y., Hoffman, E.P. Brain (2006) [Pubmed]
WikiGenes - Universities