2ypt

Structural highlights

Disease

[FACE1_HUMAN] Mandibuloacral dysplasia with type B lipodystrophy;Hutchinson-Gilford progeria syndrome;Lethal restrictive dermopathy. Mandibuloacral dysplasia with type B lipodystrophy (MADB) [MIM:608612]: A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, joint contractures, and generalized lipodystrophy with loss of subcutaneous fat from the extremities, face, neck and trunk. Note=The disease is caused by mutations affecting the gene represented in this entry.^{[1] [2] [3] [4]} Lethal tight skin contracture syndrome (LTSCS) [MIM:275210]: Rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance. Note=The disease is caused by mutations affecting the gene represented in this entry.^[5] [LMNA_HUMAN] Defects in LMNA are the cause of Emery-Dreifuss muscular dystrophy type 2, autosomal dominant (EDMD2) [MIM:181350]. A degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.^{[6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18]} Defects in LMNA are the cause of Emery-Dreifuss muscular dystrophy type 3, autosomal recessive (EDMD3) [MIM:181350]. Defects in LMNA are the cause of cardiomyopathy dilated type 1A (CMD1A) [MIM:115200]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.^{[19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31]} Defects in LMNA are the cause of familial partial lipodystrophy type 2 (FPLD2) [MIM:151660]; also known as familial partial lipodystrophy Dunnigan type. A disorder characterized by the loss of subcutaneous adipose tissue in the lower parts of the body (limbs, buttocks, trunk). It is accompanied by an accumulation of adipose tissue in the face and neck causing a double chin, fat neck, or cushingoid appearance. Adipose tissue may also accumulate in the axillae, back, labia majora, and intraabdominal region. Affected patients are insulin-resistant and may develop glucose intolerance and diabetes mellitus after age 20 years, hypertriglyceridemia, and low levels of high density lipoprotein cholesterol.^{[32] [33] [34] [35] [36] [37] [38] [39]} Defects in LMNA are the cause of limb-girdle muscular dystrophy type 1B (LGMD1B) [MIM:159001]. LGMD1B is an autosomal dominant degenerative myopathy with age-related atrioventricular cardiac conduction disturbances, dilated cardiomyopathy, and the absence of early contractures. LGMD1B is characterized by slowly progressive skeletal muscle weakness of the hip and shoulder girdles. Muscle biopsy shows mild dystrophic changes.^{[40] [41] [42] [43] [44] [45]} Defects in LMNA are the cause of Charcot-Marie-Tooth disease type 2B1 (CMT2B1) [MIM:605588]. CMT2B1 is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or CMT2. Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2B1 inheritance is autosomal recessive.^[46] Defects in LMNA are the cause of Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]. HGPS is a rare genetic disorder characterized by features reminiscent of marked premature aging. Note=HGPS is caused by the toxic accumulation of a mutant form of lamin-A/C. This mutant protein, called progerin, acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina.^{[47] [48] [49] [50] [51] [52]} Defects in LMNA are the cause of cardiomyopathy dilated with hypergonadotropic hypogonadism (CMDHH) [MIM:212112]. A disorder characterized by the association of genital anomalies, hypergonadotropic hypogonadism and dilated cardiomyopathy. Patients can present other variable clinical manifestations including mental retardation, skeletal anomalies, scleroderma-like skin, graying and thinning of hair, osteoporosis. Dilated cardiomyopathy is characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Defects in LMNA are the cause of mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]. A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroide appearance, partial alopecia, soft tissue calcinosis, joint contractures, and partial lipodystrophy with loss of subcutaneous fat from the extremities. Adipose tissue in the face, neck and trunk is normal or increased.^{[53] [54] [55]} Defects in LMNA are a cause of lethal tight skin contracture syndrome (LTSCS) [MIM:275210]; also known as restrictive dermopathy (RD). Lethal tight skin contracture syndrome is a rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance.^[56] Defects in LMNA are the cause of heart-hand syndrome Slovenian type (HHS-Slovenian) [MIM:610140]. Heart-hand syndrome (HHS) is a clinically and genetically heterogeneous disorder characterized by the co-occurrence of a congenital cardiac disease and limb malformations. Defects in LMNA are the cause of muscular dystrophy congenital LMNA-related (MDCL) [MIM:613205]. It is a form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures.^[57]

Function

[FACE1_HUMAN] Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C. [LMNA_HUMAN] Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics.^{[58] [59]} Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence.^{[60] [61]}

References

1. ↑ Agarwal AK, Fryns JP, Auchus RJ, Garg A. Zinc metalloproteinase, ZMPSTE24, is mutated in mandibuloacral dysplasia. Hum Mol Genet. 2003 Aug 15;12(16):1995-2001. PMID:12913070
2. ↑ Agarwal AK, Zhou XJ, Hall RK, Nicholls K, Bankier A, Van Esch H, Fryns JP, Garg A. Focal segmental glomerulosclerosis in patients with mandibuloacral dysplasia owing to ZMPSTE24 deficiency. J Investig Med. 2006 May;54(4):208-13. PMID:17152860
3. ↑ Miyoshi Y, Akagi M, Agarwal AK, Namba N, Kato-Nishimura K, Mohri I, Yamagata M, Nakajima S, Mushiake S, Shima M, Auchus RJ, Taniike M, Garg A, Ozono K. Severe mandibuloacral dysplasia caused by novel compound heterozygous ZMPSTE24 mutations in two Japanese siblings. Clin Genet. 2008 Jun;73(6):535-44. doi: 10.1111/j.1399-0004.2008.00992.x. Epub, 2008 Apr 22. PMID:18435794 doi:10.1111/j.1399-0004.2008.00992.x
4. ↑ Ahmad Z, Zackai E, Medne L, Garg A. Early onset mandibuloacral dysplasia due to compound heterozygous mutations in ZMPSTE24. Am J Med Genet A. 2010 Nov;152A(11):2703-10. doi: 10.1002/ajmg.a.33664. PMID:20814950 doi:10.1002/ajmg.a.33664
5. ↑ Navarro CL, De Sandre-Giovannoli A, Bernard R, Boccaccio I, Boyer A, Genevieve D, Hadj-Rabia S, Gaudy-Marqueste C, Smitt HS, Vabres P, Faivre L, Verloes A, Van Essen T, Flori E, Hennekam R, Beemer FA, Laurent N, Le Merrer M, Cau P, Levy N. Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy. Hum Mol Genet. 2004 Oct 15;13(20):2493-503. Epub 2004 Aug 18. PMID:15317753 doi:10.1093/hmg/ddh265
6. ↑ Haque F, Mazzeo D, Patel JT, Smallwood DT, Ellis JA, Shanahan CM, Shackleton S. Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. J Biol Chem. 2010 Jan 29;285(5):3487-98. doi: 10.1074/jbc.M109.071910. Epub 2009 , Nov 21. PMID:19933576 doi:10.1074/jbc.M109.071910
7. ↑ Bonne G, Di Barletta MR, Varnous S, Becane HM, Hammouda EH, Merlini L, Muntoni F, Greenberg CR, Gary F, Urtizberea JA, Duboc D, Fardeau M, Toniolo D, Schwartz K. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat Genet. 1999 Mar;21(3):285-8. PMID:10080180 doi:10.1038/6799
8. ↑ Raffaele Di Barletta M, Ricci E, Galluzzi G, Tonali P, Mora M, Morandi L, Romorini A, Voit T, Orstavik KH, Merlini L, Trevisan C, Biancalana V, Housmanowa-Petrusewicz I, Bione S, Ricotti R, Schwartz K, Bonne G, Toniolo D. Different mutations in the LMNA gene cause autosomal dominant and autosomal recessive Emery-Dreifuss muscular dystrophy. Am J Hum Genet. 2000 Apr;66(4):1407-12. Epub 2000 Mar 16. PMID:10739764 doi:10.1086/302869
9. ↑ Bonne G, Mercuri E, Muchir A, Urtizberea A, Becane HM, Recan D, Merlini L, Wehnert M, Boor R, Reuner U, Vorgerd M, Wicklein EM, Eymard B, Duboc D, Penisson-Besnier I, Cuisset JM, Ferrer X, Desguerre I, Lacombe D, Bushby K, Pollitt C, Toniolo D, Fardeau M, Schwartz K, Muntoni F. Clinical and molecular genetic spectrum of autosomal dominant Emery-Dreifuss muscular dystrophy due to mutations of the lamin A/C gene. Ann Neurol. 2000 Aug;48(2):170-80. PMID:10939567
10. ↑ Felice KJ, Schwartz RC, Brown CA, Leicher CR, Grunnet ML. Autosomal dominant Emery-Dreifuss dystrophy due to mutations in rod domain of the lamin A/C gene. Neurology. 2000 Jul 25;55(2):275-80. PMID:10908904
11. ↑ Brown CA, Lanning RW, McKinney KQ, Salvino AR, Cherniske E, Crowe CA, Darras BT, Gominak S, Greenberg CR, Grosmann C, Heydemann P, Mendell JR, Pober BR, Sasaki T, Shapiro F, Simpson DA, Suchowersky O, Spence JE. Novel and recurrent mutations in lamin A/C in patients with Emery-Dreifuss muscular dystrophy. Am J Med Genet. 2001 Sep 1;102(4):359-67. PMID:11503164
12. ↑ Ostlund C, Bonne G, Schwartz K, Worman HJ. Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy. J Cell Sci. 2001 Dec;114(Pt 24):4435-45. PMID:11792809
13. ↑ Ki CS, Hong JS, Jeong GY, Ahn KJ, Choi KM, Kim DK, Kim JW. Identification of lamin A/C ( LMNA) gene mutations in Korean patients with autosomal dominant Emery-Dreifuss muscular dystrophy and limb-girdle muscular dystrophy 1B. J Hum Genet. 2002;47(5):225-8. PMID:12032588 doi:10.1007/s100380200029
14. ↑ Vytopil M, Benedetti S, Ricci E, Galluzzi G, Dello Russo A, Merlini L, Boriani G, Gallina M, Morandi L, Politano L, Moggio M, Chiveri L, Hausmanova-Petrusewicz I, Ricotti R, Vohanka S, Toman J, Toniolo D. Mutation analysis of the lamin A/C gene (LMNA) among patients with different cardiomuscular phenotypes. J Med Genet. 2003 Dec;40(12):e132. PMID:14684700
15. ↑ Boriani G, Gallina M, Merlini L, Bonne G, Toniolo D, Amati S, Biffi M, Martignani C, Frabetti L, Bonvicini M, Rapezzi C, Branzi A. Clinical relevance of atrial fibrillation/flutter, stroke, pacemaker implant, and heart failure in Emery-Dreifuss muscular dystrophy: a long-term longitudinal study. Stroke. 2003 Apr;34(4):901-8. Epub 2003 Mar 20. PMID:12649505 doi:10.1161/01.STR.0000064322.47667.49
16. ↑ Goizet C, Yaou RB, Demay L, Richard P, Bouillot S, Rouanet M, Hermosilla E, Le Masson G, Lagueny A, Bonne G, Ferrer X. A new mutation of the lamin A/C gene leading to autosomal dominant axonal neuropathy, muscular dystrophy, cardiac disease, and leuconychia. J Med Genet. 2004 Mar;41(3):e29. PMID:14985400
17. ↑ Cenni V, Sabatelli P, Mattioli E, Marmiroli S, Capanni C, Ognibene A, Squarzoni S, Maraldi NM, Bonne G, Columbaro M, Merlini L, Lattanzi G. Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy. J Med Genet. 2005 Mar;42(3):214-20. PMID:15744034 doi:42/3/214
18. ↑ Scharner J, Brown CA, Bower M, Iannaccone ST, Khatri IA, Escolar D, Gordon E, Felice K, Crowe CA, Grosmann C, Meriggioli MN, Asamoah A, Gordon O, Gnocchi VF, Ellis JA, Mendell JR, Zammit PS. Novel LMNA mutations in patients with Emery-Dreifuss muscular dystrophy and functional characterization of four LMNA mutations. Hum Mutat. 2011 Feb;32(2):152-67. doi: 10.1002/humu.21361. Epub 2011 Jan 25. PMID:20848652 doi:10.1002/humu.21361
19. ↑ Zhang YQ, Sarge KD. Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies. J Cell Biol. 2008 Jul 14;182(1):35-9. doi: 10.1083/jcb.200712124. Epub 2008 Jul, 7. PMID:18606848 doi:10.1083/jcb.200712124
20. ↑ Ostlund C, Bonne G, Schwartz K, Worman HJ. Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy. J Cell Sci. 2001 Dec;114(Pt 24):4435-45. PMID:11792809
21. ↑ Vytopil M, Benedetti S, Ricci E, Galluzzi G, Dello Russo A, Merlini L, Boriani G, Gallina M, Morandi L, Politano L, Moggio M, Chiveri L, Hausmanova-Petrusewicz I, Ricotti R, Vohanka S, Toman J, Toniolo D. Mutation analysis of the lamin A/C gene (LMNA) among patients with different cardiomuscular phenotypes. J Med Genet. 2003 Dec;40(12):e132. PMID:14684700
22. ↑ Fatkin D, MacRae C, Sasaki T, Wolff MR, Porcu M, Frenneaux M, Atherton J, Vidaillet HJ Jr, Spudich S, De Girolami U, Seidman JG, Seidman C, Muntoni F, Muehle G, Johnson W, McDonough B. Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N Engl J Med. 1999 Dec 2;341(23):1715-24. PMID:10580070 doi:10.1056/NEJM199912023412302
23. ↑ Jakobs PM, Hanson EL, Crispell KA, Toy W, Keegan H, Schilling K, Icenogle TB, Litt M, Hershberger RE. Novel lamin A/C mutations in two families with dilated cardiomyopathy and conduction system disease. J Card Fail. 2001 Sep;7(3):249-56. PMID:11561226 doi:S1071-9164(01)97412-3
24. ↑ Hershberger RE, Hanson EL, Jakobs PM, Keegan H, Coates K, Bousman S, Litt M. A novel lamin A/C mutation in a family with dilated cardiomyopathy, prominent conduction system disease, and need for permanent pacemaker implantation. Am Heart J. 2002 Dec;144(6):1081-6. PMID:12486434 doi:10.1067/mhj.2002.126737
25. ↑ Arbustini E, Pilotto A, Repetto A, Grasso M, Negri A, Diegoli M, Campana C, Scelsi L, Baldini E, Gavazzi A, Tavazzi L. Autosomal dominant dilated cardiomyopathy with atrioventricular block: a lamin A/C defect-related disease. J Am Coll Cardiol. 2002 Mar 20;39(6):981-90. PMID:11897440
26. ↑ Taylor MR, Fain PR, Sinagra G, Robinson ML, Robertson AD, Carniel E, Di Lenarda A, Bohlmeyer TJ, Ferguson DA, Brodsky GL, Boucek MM, Lascor J, Moss AC, Li WL, Stetler GL, Muntoni F, Bristow MR, Mestroni L. Natural history of dilated cardiomyopathy due to lamin A/C gene mutations. J Am Coll Cardiol. 2003 Mar 5;41(5):771-80. PMID:12628721
27. ↑ Sebillon P, Bouchier C, Bidot LD, Bonne G, Ahamed K, Charron P, Drouin-Garraud V, Millaire A, Desrumeaux G, Benaiche A, Charniot JC, Schwartz K, Villard E, Komajda M. Expanding the phenotype of LMNA mutations in dilated cardiomyopathy and functional consequences of these mutations. J Med Genet. 2003 Aug;40(8):560-7. PMID:12920062
28. ↑ Hermida-Prieto M, Monserrat L, Castro-Beiras A, Laredo R, Soler R, Peteiro J, Rodriguez E, Bouzas B, Alvarez N, Muniz J, Crespo-Leiro M. Familial dilated cardiomyopathy and isolated left ventricular noncompaction associated with lamin A/C gene mutations. Am J Cardiol. 2004 Jul 1;94(1):50-4. PMID:15219508 doi:10.1016/j.amjcard.2004.03.029
29. ↑ Karkkainen S, Helio T, Miettinen R, Tuomainen P, Peltola P, Rummukainen J, Ylitalo K, Kaartinen M, Kuusisto J, Toivonen L, Nieminen MS, Laakso M, Peuhkurinen K. A novel mutation, Ser143Pro, in the lamin A/C gene is common in finnish patients with familial dilated cardiomyopathy. Eur Heart J. 2004 May;25(10):885-93. PMID:15140538 doi:10.1016/j.ehj.2004.01.020
30. ↑ Sylvius N, Bilinska ZT, Veinot JP, Fidzianska A, Bolongo PM, Poon S, McKeown P, Davies RA, Chan KL, Tang AS, Dyack S, Grzybowski J, Ruzyllo W, McBride H, Tesson F. In vivo and in vitro examination of the functional significances of novel lamin gene mutations in heart failure patients. J Med Genet. 2005 Aug;42(8):639-47. PMID:16061563 doi:10.1136/jmg.2004.023283
31. ↑ Millat G, Bouvagnet P, Chevalier P, Sebbag L, Dulac A, Dauphin C, Jouk PS, Delrue MA, Thambo JB, Le Metayer P, Seronde MF, Faivre L, Eicher JC, Rousson R. Clinical and mutational spectrum in a cohort of 105 unrelated patients with dilated cardiomyopathy. Eur J Med Genet. 2011 Nov-Dec;54(6):e570-5. doi: 10.1016/j.ejmg.2011.07.005. Epub, 2011 Aug 4. PMID:21846512 doi:10.1016/j.ejmg.2011.07.005
32. ↑ Ostlund C, Bonne G, Schwartz K, Worman HJ. Properties of lamin A mutants found in Emery-Dreifuss muscular dystrophy, cardiomyopathy and Dunnigan-type partial lipodystrophy. J Cell Sci. 2001 Dec;114(Pt 24):4435-45. PMID:11792809
33. ↑ Speckman RA, Garg A, Du F, Bennett L, Veile R, Arioglu E, Taylor SI, Lovett M, Bowcock AM. 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. 2000 Apr;66(4):1192-8. PMID:10739751 doi:10.1086/302836
34. ↑ Cao H, Hegele RA. Nuclear lamin A/C R482Q mutation in canadian kindreds with Dunnigan-type familial partial lipodystrophy. Hum Mol Genet. 2000 Jan 1;9(1):109-12. PMID:10587585
35. ↑ Shackleton S, Lloyd DJ, Jackson SN, Evans R, Niermeijer MF, Singh BM, Schmidt H, Brabant G, Kumar S, Durrington PN, Gregory S, O'Rahilly S, Trembath RC. LMNA, encoding lamin A/C, is mutated in partial lipodystrophy. Nat Genet. 2000 Feb;24(2):153-6. PMID:10655060 doi:10.1038/72807
36. ↑ Garg A, Speckman RA, Bowcock AM. Multisystem dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamin A/C gene. Am J Med. 2002 May;112(7):549-55. PMID:12015247
37. ↑ van der Kooi AJ, Bonne G, Eymard B, Duboc D, Talim B, Van der Valk M, Reiss P, Richard P, Demay L, Merlini L, Schwartz K, Busch HF, de Visser M. Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and muscular dystrophy. Neurology. 2002 Aug 27;59(4):620-3. PMID:12196663
38. ↑ Caux F, Dubosclard E, Lascols O, Buendia B, Chazouilleres O, Cohen A, Courvalin JC, Laroche L, Capeau J, Vigouroux C, Christin-Maitre S. 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. J Clin Endocrinol Metab. 2003 Mar;88(3):1006-13. PMID:12629077
39. ↑ Lanktree M, Cao H, Rabkin SW, Hanna A, Hegele RA. Novel LMNA mutations seen in patients with familial partial lipodystrophy subtype 2 (FPLD2; MIM 151660). Clin Genet. 2007 Feb;71(2):183-6. PMID:17250669 doi:10.1111/j.1399-0004.2007.00740.x
40. ↑ Ki CS, Hong JS, Jeong GY, Ahn KJ, Choi KM, Kim DK, Kim JW. Identification of lamin A/C ( LMNA) gene mutations in Korean patients with autosomal dominant Emery-Dreifuss muscular dystrophy and limb-girdle muscular dystrophy 1B. J Hum Genet. 2002;47(5):225-8. PMID:12032588 doi:10.1007/s100380200029
41. ↑ Cenni V, Sabatelli P, Mattioli E, Marmiroli S, Capanni C, Ognibene A, Squarzoni S, Maraldi NM, Bonne G, Columbaro M, Merlini L, Lattanzi G. Lamin A N-terminal phosphorylation is associated with myoblast activation: impairment in Emery-Dreifuss muscular dystrophy. J Med Genet. 2005 Mar;42(3):214-20. PMID:15744034 doi:42/3/214
42. ↑ Muchir A, Bonne G, van der Kooi AJ, van Meegen M, Baas F, Bolhuis PA, de Visser M, Schwartz K. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum Mol Genet. 2000 May 22;9(9):1453-9. PMID:10814726
43. ↑ Kitaguchi T, Matsubara S, Sato M, Miyamoto K, Hirai S, Schwartz K, Bonne G. A missense mutation in the exon 8 of lamin A/C gene in a Japanese case of autosomal dominant limb-girdle muscular dystrophy and cardiac conduction block. Neuromuscul Disord. 2001 Sep;11(6-7):542-6. PMID:11525883
44. ↑ Charniot JC, Pascal C, Bouchier C, Sebillon P, Salama J, Duboscq-Bidot L, Peuchmaurd M, Desnos M, Artigou JY, Komajda M. Functional consequences of an LMNA mutation associated with a new cardiac and non-cardiac phenotype. Hum Mutat. 2003 May;21(5):473-81. PMID:12673789 doi:10.1002/humu.10170
45. ↑ Rudnik-Schoneborn S, Botzenhart E, Eggermann T, Senderek J, Schoser BG, Schroder R, Wehnert M, Wirth B, Zerres K. Mutations of the LMNA gene can mimic autosomal dominant proximal spinal muscular atrophy. Neurogenetics. 2007 Apr;8(2):137-42. Epub 2006 Nov 29. PMID:17136397 doi:10.1007/s10048-006-0070-0
46. ↑ De Sandre-Giovannoli A, Chaouch M, Kozlov S, Vallat JM, Tazir M, Kassouri N, Szepetowski P, Hammadouche T, Vandenberghe A, Stewart CL, Grid D, Levy N. 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. 2002 Mar;70(3):726-36. Epub 2002 Jan 17. PMID:11799477 doi:10.1086/339274
47. ↑ Haque F, Mazzeo D, Patel JT, Smallwood DT, Ellis JA, Shanahan CM, Shackleton S. Mammalian SUN protein interaction networks at the inner nuclear membrane and their role in laminopathy disease processes. J Biol Chem. 2010 Jan 29;285(5):3487-98. doi: 10.1074/jbc.M109.071910. Epub 2009 , Nov 21. PMID:19933576 doi:10.1074/jbc.M109.071910
48. ↑ Cao H, Hegele RA. LMNA is mutated in Hutchinson-Gilford progeria (MIM 176670) but not in Wiedemann-Rautenstrauch progeroid syndrome (MIM 264090). J Hum Genet. 2003;48(5):271-4. Epub 2003 Apr 3. PMID:12768443 doi:10.1007/s10038-003-0025-3
49. ↑ Chen L, Lee L, Kudlow BA, Dos Santos HG, Sletvold O, Shafeghati Y, Botha EG, Garg A, Hanson NB, Martin GM, Mian IS, Kennedy BK, Oshima J. LMNA mutations in atypical Werner's syndrome. Lancet. 2003 Aug 9;362(9382):440-5. PMID:12927431 doi:http://dx.doi.org/10.1016/S0140-6736(03)14069-X
50. ↑ Eriksson M, Brown WT, Gordon LB, Glynn MW, Singer J, Scott L, Erdos MR, Robbins CM, Moses TY, Berglund P, Dutra A, Pak E, Durkin S, Csoka AB, Boehnke M, Glover TW, Collins FS. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature. 2003 May 15;423(6937):293-8. Epub 2003 Apr 25. PMID:12714972 doi:10.1038/nature01629
51. ↑ Plasilova M, Chattopadhyay C, Pal P, Schaub NA, Buechner SA, Mueller H, Miny P, Ghosh A, Heinimann K. Homozygous missense mutation in the lamin A/C gene causes autosomal recessive Hutchinson-Gilford progeria syndrome. J Med Genet. 2004 Aug;41(8):609-14. PMID:15286156 doi:10.1136/jmg.2004.019661
52. ↑ Kirschner J, Brune T, Wehnert M, Denecke J, Wasner C, Feuer A, Marquardt T, Ketelsen UP, Wieacker P, Bonnemann CG, Korinthenberg R. p.S143F mutation in lamin A/C: a new phenotype combining myopathy and progeria. Ann Neurol. 2005 Jan;57(1):148-51. PMID:15622532 doi:10.1002/ana.20359
53. ↑ Novelli G, Muchir A, Sangiuolo F, Helbling-Leclerc A, D'Apice MR, Massart C, Capon F, Sbraccia P, Federici M, Lauro R, Tudisco C, Pallotta R, Scarano G, Dallapiccola B, Merlini L, Bonne G. Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C. Am J Hum Genet. 2002 Aug;71(2):426-31. Epub 2002 Jun 19. PMID:12075506 doi:S0002-9297(07)60489-3
54. ↑ Garg A, Cogulu O, Ozkinay F, Onay H, Agarwal AK. A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia. J Clin Endocrinol Metab. 2005 Sep;90(9):5259-64. Epub 2005 Jul 5. PMID:15998779 doi:10.1210/jc.2004-2560
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58. ↑ De Vos WH, Houben F, Hoebe RA, Hennekam R, van Engelen B, Manders EM, Ramaekers FC, Broers JL, Van Oostveldt P. Increased plasticity of the nuclear envelope and hypermobility of telomeres due to the loss of A-type lamins. Biochim Biophys Acta. 2010 Apr;1800(4):448-58. doi: 10.1016/j.bbagen.2010.01.002., Epub 2010 Jan 14. PMID:20079404 doi:10.1016/j.bbagen.2010.01.002
59. ↑ Ragnauth CD, Warren DT, Liu Y, McNair R, Tajsic T, Figg N, Shroff R, Skepper J, Shanahan CM. Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging. Circulation. 2010 May 25;121(20):2200-10. doi: 10.1161/CIRCULATIONAHA.109.902056., Epub 2010 May 10. PMID:20458013 doi:10.1161/CIRCULATIONAHA.109.902056
60. ↑ De Vos WH, Houben F, Hoebe RA, Hennekam R, van Engelen B, Manders EM, Ramaekers FC, Broers JL, Van Oostveldt P. Increased plasticity of the nuclear envelope and hypermobility of telomeres due to the loss of A-type lamins. Biochim Biophys Acta. 2010 Apr;1800(4):448-58. doi: 10.1016/j.bbagen.2010.01.002., Epub 2010 Jan 14. PMID:20079404 doi:10.1016/j.bbagen.2010.01.002
61. ↑ Ragnauth CD, Warren DT, Liu Y, McNair R, Tajsic T, Figg N, Shroff R, Skepper J, Shanahan CM. Prelamin A acts to accelerate smooth muscle cell senescence and is a novel biomarker of human vascular aging. Circulation. 2010 May 25;121(20):2200-10. doi: 10.1161/CIRCULATIONAHA.109.902056., Epub 2010 May 10. PMID:20458013 doi:10.1161/CIRCULATIONAHA.109.902056
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