Neuromuscular DiseasesNeuromuscular DiseasesНервно-мышечные болезни2222-87212413-0443Publishing House ABV Press46210.17650/2222-8721-2021-11-3-51-63CLINICAL CASEКЛИНИЧЕСКИЙ РАЗБОРNew mutation in the TRIP4 gene associated with congenital muscular dystrophy Davignon–Chauveau type (clinical case)Новая мутация в гене TRIP4, ассоциированная с фенотипом врожденной мышечной дистрофии типа Давиньон–Шове (клинический случай)https://orcid.org/0000-0001-9101-5213KozhanovaT. V.КожановаТ. В.
Russian Federation

Tatyana V. Kozhanova

38 Aviatorov St., Moscow 119620,

1 Ostrovityanova St., Moscow 117997

Татьяна Викторовна Кожанова

119620 Москва, ул. Авиаторов, 38,

117997 Москва, ул. Островитянова, 1

vkozhanov@bk.ruhttps://orcid.org/0000-0002-2400-0748ZhilinaS. S.ЖилинаС. С.
Russian Federation

38 Aviatorov St., Moscow 119620,

1 Ostrovityanova St., Moscow 117997

119620 Москва, ул. Авиаторов, 38,

117997 Москва, ул. Островитянова, 1

 

https://orcid.org/0000-0002-5970-565XMescheryakovaT. I.МещеряковаТ. И.
Russian Federation

38 Aviatorov St., Moscow 119620

119620 Москва, ул. Авиаторов, 38

ShorinaM. Yu.ШоринаМ. Ю.
Russian Federation

38 Aviatorov St., Moscow 119620

119620 Москва, ул. Авиаторов, 38

DemenshinI. F.ДеменьшинИ. Ф.
Russian Federation

38 Aviatorov St., Moscow 119620

119620 Москва, ул. Авиаторов, 38

ProkopievG. G.ПрокопьевГ. Г.
Russian Federation

38 Aviatorov St., Moscow 119620

119620 Москва, ул. Авиаторов, 38

https://orcid.org/0000-0003-0499-5167KanivetsI. V.КанивецИ. В.
Russian Federation

Build. 5, 8 Podolskoe Shosse, 115093 Moscow

115093 Москва, Подольское шоссе, 8, корп. 5

https://orcid.org/0000-0002-0552-6939SuchorukovV. S.СухоруковВ. С.
Russian Federation

80 Volokolamskoe Shosse, 125367 Moscow

125367 Москва, Волоколамское шоссе, 80

AnufrievP. L.АнуфриевП. Л.
Russian Federation

80 Volokolamskoe Shosse, 125367 Moscow

125367 Москва, Волоколамское шоссе, 80

https://orcid.org/0000-0002-8999-9986BaranichT. I.БараничТ. И.
Russian Federation

1 Ostrovityanova St., Moscow 117997,

80 Volokolamskoe Shosse, 125367 Moscow

117997 Москва, ул. Островитянова, 1,

125367 Москва, Волоколамское шоссе, 80

KozinaA. A.КозинаА. А.
Russian Federation

1 Ostrovityanova St., Moscow 117997

117997 Москва, ул. Островитянова, 1

https://orcid.org/0000-0001-8899-4107PritykoA. G.ПритыкоА. Г.
Russian Federation

38 Aviatorov St., Moscow 119620,

1 Ostrovityanova St., Moscow 117997

119620 Москва, ул. Авиаторов, 38,

117997 Москва, ул. Островитянова, 1

Pirogov Russian National Research Medical UniversityГБУЗ «Научно-практический центр специализированной медицинской помощи детям им. В.Ф. Войно-Ясенецкого Департамента здравоохранения г. Москвы»Research Center of NeurologyФГАОУ ВО «Российский национальный исследовательский медицинский университет им. Н.И. Пирогова» Минздрава РоссииGenomedООО «Геномед»Research Center of NeurologyФГБНУ «Научный центр неврологии»Pirogov Russian National Research Medical UniversityФГАОУ ВО «Российский национальный исследовательский медицинский университет им. Н.И. Пирогова» Минздрава РоссииSt. Luka’s Clinical Research Center for ChildrenГБУЗ «Научно-практический центр специализированной медицинской помощи детям им. В.Ф. Войно-Ясенецкого Департамента здравоохранения г. Москвы»1412202111351631312202113122021Copyright ©; 2021, Kozhanova T.V., Zhilina S.S., Mescheryakova T.I., Shorina M.Y., Demenshin I.F., Prokopiev G.G., Kanivets I.V., Suchorukov V.S., Anufriev P.L., Baranich T.I., Kozina A.A., Prityko A.G.Copyright ©; 2021, Кожанова Т.В., Жилина С.С., Мещерякова Т.И., Шорина М.Ю., Деменьшин И.Ф., Прокопьев Г.Г., Канивец И.В., Сухоруков В.С., Ануфриев П.Л., Баранич Т.И., Козина А.А., Притыко А.Г.2021Kozhanova T.V., Zhilina S.S., Mescheryakova T.I., Shorina M.Y., Demenshin I.F., Prokopiev G.G., Kanivets I.V., Suchorukov V.S., Anufriev P.L., Baranich T.I., Kozina A.A., Prityko A.G.Кожанова Т.В., Жилина С.С., Мещерякова Т.И., Шорина М.Ю., Деменьшин И.Ф., Прокопьев Г.Г., Канивец И.В., Сухоруков В.С., Ануфриев П.Л., Баранич Т.И., Козина А.А., Притыко А.Г.https://creativecommons.org/licenses/by/4.0https://nmb.abvpress.ru/jour/article/view/462

Congenital muscular dystrophies are heterogeneous groups of neuromuscular diseases leading to hypotonia, progressive muscle weakness and dystrophic or structural signs in muscle biopsy. At the present time, 34 genes associated with congenital muscular dystrophy have been described. The clinical case of a rare form of congenital muscular dystrophia associated with a homozygous mutation in the TRIP4 gene in a patient with respiratory failure requiring respiratory support, neurological symptoms, muscular hypotonia, and multiple congenital malformations of skeletal system is presented for the first time in Russia. The undescribed pathogenic homozygous variant of the nucleotide sequence in the TRIP4 gene (chr15:64686179, c.136C>T, p.Arg46Ter, 2 exon, NM_016213.4) was detected by whole exome sequencing. The mutation in the TRIP4 gene was validated by Sanger sequencing in a child and its origin was investigated. The mother and father of the girl are carriers of the heterozygous variant in the TRIP4 gene. Identification of the genetic cause of a rare form of neuromuscular disease is important for determining the tactics of patient management and medical and genetic counseling of the family, as well as clarifying the pathogenesis of a rare pathology.

 

Врожденные мышечные дистрофии и врожденные миопатии представляют собой гетерогенную группу нервно-мышечных заболеваний, приводящих к гипотонии, прогрессирующей мышечной слабости и дистрофическим или структурным признакам при мышечной биопсии. В настоящее время описано 34 гена, связанных с врожденной мышечной дистрофией. Впервые в России представляется клинический случай редкой формы врожденной мышечной дистрофии, обусловленной гомозиготной мутацией в гене TRIP4, у пациента с дыхательной недостаточностью, требующей респираторной поддержки, неврологической симптоматикой, мышечной гипотонией, множественными врожденными пороками развития опорно-двигательной системы. В результате проведенного полноэкзомного секвенирования выявлен ранее не описанный патогенный вариант нуклеотидной последовательности в гене TRIP4 в гомозиготном состоянии, приводящий к остановке синтеза полнофункционального белка (chr15:64686179, c.136C>T, p.Arg46Ter, 2 й экзон, NM_016213.4). Мутация в гене TRIP4 была валидирована методом секвенирования по Сэнгеру у ребенка, и исследовано ее происхождение. Мать и отец девочки являются носителями гетерозиготного варианта в гене TRIP4. Выявление генетической причины редкой формы нервно-мышечного заболевания важно для определения тактики ведения пациента и медико-генетического консультирования семьи, а также уточнения патогенеза редкой патологии.

congenital muscular dystrophyTRIP4 genemuscle hypotoniarespiratory failurecontracturesврожденная мышечная дистрофияген TRIP4мышечная гипотониядыхательная недостаточностьконтрактурыDavignon L., Chauveau C., Julien C. et al. The transcription coactivator ASC-1 is a regulator of skeletal myogenesis, and its deficiency causes a novel form of congenital muscle disease. Hum Molec Genet 2016;25:1559–73. DOI: 10.1093/hmg/ddw033.Bonnemann C.G., Wang C.H., QuijanoRoy S. et al. Diagnostic approach to the congenital muscular dystrophies. Neuromuscul Disord 2014;24:289–311. DOI: 10.1016/j.nmd.2013.12.011.Gilbreath H.R., Castro D., Iannaccone S.T. Congenital myopathies and muscular dystrophies. Neurol Clin 2014;32:689–703. DOI: 10.1016/j.ncl.2014.04.006.North K.N., Wang C.H., Clarke N. et al. Approach to the diagnosis of congenital myopathies. Neuromuscul Disord 2014;24:97–116. DOI: 10.1016/j.nmd.2013.11.003.Engel A.G., Gomez M.R., Groover R.V. Multicore disease. A recently recognized congenital myopathy associated with multifocal degeneration of muscle fibres. Mayo Clin Proc 1971;46:666–81.Ferreiro A., Estournet B., Chateau D. et al. Multi-minicore disease – searching for boundaries: phenotype analysis of 38 cases. Ann Neurol 2000;48:745–57.Lehtokari V.L., Ceuterick-de Groote C., de Jonghe P. et al. Cap disease caused by heterozygous deletion of the betatropomyosingene TPM2. Neuromuscul Disord 2007;17:433–42. DOI: 10.1016/j.nmd.2007.02.015.Endo T. Glycobiology of alpha-dystroglycan and muscular dystrophy. J Biochem 2014;157:1–12. DOI: 10.1093/jb/mvu066.Quijano-Roy S., Mbieleu B., Bonnemann C.G. et al. De novo LMNA mutations cause a new form of congenital muscular dystrophy. Ann Neurol 2008;64: 177–186. DOI: 10.1002/ana.21417.Wallgren-Pettersson C., Sewry C.A., Nowak K.J., Laing N.G. Nemaline myopathies. Semin Pediatr Neurol 2011;18:230–8. DOI: 10.1016/j.spen.2011.10.004.Ravenscroft G., Laing N.G., Bonnemann C.G. Pathophysiological concepts in the congenital myopathies: blurring the boundaries, sharpening the focus. Brain 2015;138:246–68. DOI: 10.1093/brain/awu368.Snoeck M., van Engelen B.G., Kusters B. et al. RYR1-related myopathies: a wide spectrum of phenotypes throughout life. Eur J Neurol 2015;22:1094–112. DOI: 10.1111/ene.12713.Horstick E.J., Linsley J.W., Dowling J.J. et al. Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy. Nat Commun 2013;4:1952. DOI: 10.1038/ncomms2952.Nelson B.R., Wu F., Liu Y. et al. Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractility. Proc Natl Acad Sci USA 2013;110:11881–6. DOI: 10.1073/pnas.1310571110.Dowling J.J., Lawlor M.W., Dirksen R.T. Triadopathies: an emerging class of skeletal muscle diseases. Neurotherapeutics 2015;1:773–85. DOI: 10.1007/s13311-014-0300-3.Jungbluth H., Gautel M. Pathogenic mechanisms in centronuclear myopathies. Front Aging Neurosci 2015;6:339. DOI: 10.3389/fnagi.2014.00339.Jungbluth H., Sewry C., Brown S.C. et al. Minicore myopathy in children: a clinical andhistopathological study of 19 cases. Neuromuscul Disord 2000;10:264–73. DOI: 10.1016/s0960-8966(99)00125-x.Chauveau C., Bonnemann C.G., Julien, C. et al. Recessive TTN truncating mutations define novel forms of core myopathy with heart disease. Hum Mol Genet 2014;23:980–91. DOI: 10.1093/hmg/ddt494.Ferreiro A., Quijano-Roy S., Pichereau C. et al. Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: reassessing the nosology of early-onset myopathies. Am J Hum Genet 2002;71:739–49. DOI: 10.1086/342719.Ferreiro A., Monnier N., Romero N.B. et al. A recessive form of central core disease, transiently presenting as multi-minicore disease, is associated with a homozygous mutation in the ryanodine receptor type 1 gene. Ann Neurol 2002;51:750–9. DOI: 10.1002/ana.10231.Clarke N.F., Amburgey K., Teener J. et al. A novel mutation expands the genetic and clinical spectrum of MYH7-related myopathies. Neuromuscul Disord 2013;23:432–6. DOI: 10.1016/j.nmd.2013.02.009.Lorenzoni P.J., Scola R.H., Kay C.S. et al. Congenital myasthenic syndrome and minicore-like myopathy with DOK7 mutation. Muscle Nerve 2013;48:151–2. DOI: 10.1002/mus.23724.Boyden S.E., Mahoney L.J., Kawahara G. et al. Mutations in the satellite cell gene MEGF10 cause a recessive congenital myopathy with minicores. Neurogenetics 2012;13:115–24. DOI: 10.1007/s10048-012-0315-z.Majczenko K., Davidson A.E., Camelo-Piragua S. et al. Dominant mutation of CCDC78 in a unique congenital myopathy with prominent internal nuclei and atypical cores. Am J Hum Genet 2012;91:365–71. DOI: 10.1016/j.ajhg.2012.06.012.Dowling J.J., Arbogast S., Hur J. et al. Oxidative stress and successful antioxidant treatment in models of RYR1-related myopathy. Brain 2012;135:1115–27. DOI: 10.1093/brain/aws036.Lampe A.K., Dunn D.M., von Niederhausern A.C. et al. Automated genomic sequence analysis of the three collagen VI genes: applications to Ulrich congenital muscular dystrophy and Bethlem myopathy. J Med Genet 2005;42:108–20. DOI: 10.1136/jmg.2004.023754.Petrini S., D’Amico A., Sale P. et al. Ullrich myopathy phenotype with secondary ColVI defect identified by confocal imaging and electron microscopy analysis. Neuromuscul Disord 2007;17:587–96. DOI: 10.1016/j.nmd.2007.04.010.Okada M., Kawahara G., Noguchi S. et al. Primary collagen VI deficiency is the second most common congenital muscular dystrophy in Japan. Neurology 2007;69:1035–42. DOI: 10.1212/01.wnl.0000271387.10404.4e.Bertini E., D’Amico A., Gualandi F., Petrini S. Congenital muscular dystrophies: a brief review. Semin Pediatr Neurol 2011;18:277–88. DOI: 10.1016/j.spen.2011.10.010.Clarke N.F., Domazetovska A., Waddell L. et al. Cap disease due to mutation of the beta-tropomyosin gene (TPM2). Neuromuscul Disord 2009;19:348–51. DOI: 10.1016/j.nmd.2009.03.003.Butterfield R.J. Congenital muscular dystrophy and congenital myopathy. Continuum (MinneapMinn) 2019;25(6):1640–61. DOI: 10.1212/CON.0000000000000792.Ravenscroft G., Bryson-Richardson R.J., Nowak K.J., Laing N.G. Recent advances in understanding congenital myopathies. F1000Res 2017. PII: F1000 Faculty Rev-1921. DOI: 10.12688/f1000research.16422.1.Bonne G., Rivier F., Hamroun D. The 2019 version of the gene table of neuromuscular disorders (nuclear genome). Neuromuscul Disord 2018;28(12):1031–63. DOI: 10.1016/j.nmd.2018.09.006.Ferreiro A., Ceuterick-de Groote C., Marks J.J. et al. Desmin-related myopathy with Mallory body-like inclusions is caused by mutations of the selenoprotein N gene. Ann Neurol 2004;55:676–86. DOI: 10.1002/ana.20077.Agrawal P.B., Greenleaf R.S., Tomczak K.K. et al. Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Am J Hum Genet 2007;80:162–7. DOI: 10.1086/510402.Malfatti E., Schaeffer U., Chapon F. et al. Combined cap diseaseand nemaline myopathy in the same patient caused by anautosomal dominant mutation in the TPM3 gene. Neuromuscul Disord 2013;23:992–7. DOI: 10.1016/j.nmd.2013.07.003.Auboeuf D., Honig A., Berget S.M., O’Malley B.W. Coordinate regulation of transcription and splicing by steroid receptor coregulators. Science 2002;298:416–9. DOI: 10.1126/science.1073734.Lee J.W., Choi H.S., Gyuris J. et al. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol 1995;9:243–54. DOI: 10.1210/mend.9.2.7776974.Kim H.J., Yi J.Y., Sung H.S. et al. Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation. Mol Cell Biol 1999;19:6323–32. DOI: 10.1128/mcb.19.9.6323.Jung D.J., Sung H.S., Goo Y.W. et al. Novel transcription coactivator complex containing activating signal cointegrator 1. Mol Cell Biol 2002;22:5203–11. DOI: 10.1128/mcb.22.14.5203-5211.2002.Iyer L.M., Burroughs A.M., Aravind L. The ASCH superfamily: novel domains with a fold related to the PUA domain and a potential role in RNA metabolism. Bioinformatics 2006;22:257–63. DOI: 10.1093/bioinformatics/bti767.Almeida-Vega S., Catlow K., Kenny S. et al. Gastrin activates paracrine networks leading to induction of PAI-2 via MAZ and ASC-1. Am J Physiol Gastrointest Liver Physiol 2009;296:1414–23. DOI: 10.1152/ajpgi.90340.2008.Cherkasova V., Ayyadevara S., Egilmez N., Shmookler Reis R. Diverse Caenorhabditis elegans genes that are upregulated in dauer larvae also show elevated transcript levels in long-lived, aged, or starved adults. J Mol Biol 2000;300:433–48. DOI: 10.1006/jmbi.2000.3880.Ruiz A., Heilmann S., Becker T. et al. Follow-up of loci from the International Genomics of Alzheimer’s Disease Project identifies TRIP4 as a novel susceptibility gene. Transl Psychiatry 2014;4:e358. DOI: 10.1038/tp.2014.2.Yokoyama S., Ito Y., Ueno-Kudoh H. et al. A systems approach reveals that the myogenesis genome network is regulated by the transcriptional repressor RP58. Dev Cell 2009;17,:836–48. DOI: 10.1016/j.devcel.2009.10.011.Zhang Y., Cong X., Wang A., Jiang H. Identification of the STAC3 gene as a skeletal muscle-specifically expressed gene and a novel regulator of satellite cell differentiation in cattle. J Anim Sci 2014;92:3284–90. DOI: 10.2527/jas.2014-7656.Muhammad E., Reish O., Ohno Y. et al. Congenital myopathy is caused by mutation of HACD1. Hum Mol Genet 2013;22:5229–36. DOI: 10.1093/hmg/ddt380.Blondelle J., Ohno Y., Gache V. et al. HACD1, a regulator of membrane composition and fluidity, promotes myoblast fusion and skeletal muscle growth. J Mol Cell Biol 2015;5:429–40. DOI: 10.1093/jmcb/mjv049.Castets P., Bertrand A.T., Beuvin M. et al. Satellite cell loss and impaired muscle regeneration in selenoprotein N deficiency. Hum Mol Genet 2011;20:694–704. DOI: 10.1093/hmg/ddq515.Logan C.V., Lucke B., Pottinger C. et al. Mutations in MEGF10, a regulator of satellite cell myogenesis, cause early onset myopathy, areflexia, respiratory distress and dysphagia (EMARDD). Nat Genet 2011;43:1189–92. DOI: 10.1038/ng.995.Fukada S., Uezumi A., Ikemoto M. et al. Molecular signature of quiescent satellite cells in adult skeletal muscle. Stem Cells 2007;5:2448–59. DOI: 10.1634/stemcells.2007-0019.Li Z., Gilbert J.A., Zhang Y. et al. An HMGA2-IGF2BP2 axis regulates myoblast proliferation and myogenesis. Dev Cell 2012;3:1176–88. DOI: 10.1016/j.devcel.2012.10.019.Belenikin M.S., Zhilina S.S., Barinov A.A. et al. Allelic variant of Salih congenital myopathy. Rossiyskiy vestnik perinatologii i pediatrii = Russian Bulletin of Perinatology and Pediatrics 2015;60(3):89–93. (In Russ.)Беленикин М.С., Жилина С.С., Баринов А.А. и др. Аллельный вариант врожденной миопатии Салиха. Российский вестник перинатологии и педиатрии 2015;60(3):89–93.