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Kariminejad, A., Szenker-Ravi, E., Lekszas, C., Tajsharghi, H., Moslemi, A.-R., Naert, T., . . . Reversade, B. (2019). Homozygous Null TBX4 Mutations Lead to Posterior Amelia with Pelvic and Pulmonary Hypoplasia. American Journal of Human Genetics, 105(6), 1294-1301
Open this publication in new window or tab >>Homozygous Null TBX4 Mutations Lead to Posterior Amelia with Pelvic and Pulmonary Hypoplasia
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2019 (English)In: American Journal of Human Genetics, ISSN 0002-9297, E-ISSN 1537-6605, Vol. 105, no 6, p. 1294-1301Article in journal (Refereed) Published
Abstract [en]

The development of hindlimbs in tetrapod species relies specifically on the transcription factor TBX4. In humans, heterozygous loss-of-function TBX4 mutations cause dominant small patella syndrome (SPS) due to haploinsufficiency. Here, we characterize a striking clinical entity in four fetuses with complete posterior amelia with pelvis and pulmonary hypoplasia (PAPPA). Through exome sequencing, we find that PAPPA syndrome is caused by homozygous TBX4 inactivating mutations during embryogenesis in humans. In two consanguineous couples, we uncover distinct germline TBX4 coding mutations, p.Tyr113 and p.Tyr127Asn, that segregated with SPS in heterozygous parents and with posterior amelia with pelvis and pulmonary hypoplasia syndrome (PAPPAS) in one available homozygous fetus. A complete absence of TBX4 transcripts in this proband with biallelic p.Tyr113 stop-gain mutations revealed nonsense-mediated decay of the endogenous mRNA. CRISPR/Cas9-mediated TBX4 deletion in Xenopus embryos confirmed its restricted role during leg development. We conclude that SPS and PAPPAS are allelic diseases of TBX4 deficiency and that TBX4 is an essential transcription factor for organogenesis of the lungs, pelvis, and hindlimbs in humans.

Place, publisher, year, edition, pages
Elsevier, 2019
Keywords
PAPPAS, SPS, TBX4, Xenopus, allelic diseases, animal models, hindlimb amelia, lung and pelvis hypoplasia, semi-dominant, small patella syndrome
National Category
Medical and Health Sciences Medical Genetics
Research subject
Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-17981 (URN)10.1016/j.ajhg.2019.10.013 (DOI)000500935400018 ()31761294 (PubMedID)2-s2.0-85075600162 (Scopus ID)
Available from: 2019-12-05 Created: 2019-12-05 Last updated: 2019-12-27Bibliographically approved
Sedghi, M., Moslemi, A.-R., Olive, M., Etemadifar, M., Ansari, B., Nasiri, J., . . . Tajsharghi, H. (2019). Motor neuron diseases caused by a novel VRK1 variant - A genotype/phenotype study. Annals of clinical and translational neurology, 6(11), 2197-2204
Open this publication in new window or tab >>Motor neuron diseases caused by a novel VRK1 variant - A genotype/phenotype study
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2019 (English)In: Annals of clinical and translational neurology, E-ISSN 2328-9503, Vol. 6, no 11, p. 2197-2204Article in journal (Refereed) Published
Abstract [en]

Background Motor neuron disorders involving upper and lower neurons are a genetically and clinically heterogenous group of rare neuromuscular disorders with overlap among spinal muscular atrophies (SMAs) and amyotrophic lateral sclerosis (ALS). Classical SMA caused by recessive mutations in SMN1 is one of the most common genetic causes of mortality in infants. It is characterized by degeneration of anterior horn cells in the spinal cord, leading to progressive muscle weakness and atrophy. Non-SMN1-related spinal muscular atrophies are caused by variants in a number of genes, including VRK1, encoding the vaccinia-related kinase 1 (VRK1). VRK1 variants have been segregated with motor neuron diseases including SMA phenotypes or hereditary complex motor and sensory axonal neuropathy (HMSN), with or without pontocerebellar hypoplasia or microcephaly. Results Here, we report an association of a novel homozygous splice variant in VRK1 (c.1159 + 1G>A) with childhood-onset SMA or juvenile lower motor disease with brisk tendon reflexes without pontocerebellar hypoplasia and normal intellectual ability in a family with five affected individuals. We show that the VRK1 splice variant in patients causes decreased splicing efficiency and a mRNA frameshift that escapes the nonsense-mediated decay machinery and results in a premature termination codon. Conclusions Our findings unveil the impact of the variant on the VRK1 transcript and further support the implication of VRK1 in the pathogenesis of lower motor neuron diseases.

Place, publisher, year, edition, pages
John Wiley & Sons, 2019
National Category
Neurosciences
Research subject
Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-17787 (URN)10.1002/acn3.50912 (DOI)000487841300001 ()31560180 (PubMedID)2-s2.0-85073966860 (Scopus ID)
Available from: 2019-10-11 Created: 2019-10-11 Last updated: 2019-12-09Bibliographically approved
Sedghi, M., Moslemi, A.-R., Cabrera-Serrano, M., Ansari, B., Ghasemi, M., Baktashian, M., . . . Tajsharghi, H. (2019). Recessive Charcot-Marie-Tooth and multiple sclerosis associated with a variant in MCM3AP. Brain Communications, 1(1)
Open this publication in new window or tab >>Recessive Charcot-Marie-Tooth and multiple sclerosis associated with a variant in MCM3AP
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2019 (English)In: Brain Communications, E-ISSN 2632-1297, Vol. 1, no 1Article in journal (Refereed) Epub ahead of print
Abstract [en]

Variants in MCM3AP, encoding the germinal-centre associated nuclear protein, have been associated with progressive polyneuropathy with or without intellectual disability and ptosis in some cases, and with a complex phenotype with immunodeficiency, skin changes and myelodysplasia. MCM3AP encoded protein functions as an acetyltransferase that acetylates the replication protein, MCM3, and plays a key role in the regulation of DNA replication. In this study, we report a novel variant in MCM3AP (p.Ile954Thr), in a family including three affected individuals with characteristic features of Charcot-Marie-Tooth neuropathy and multiple sclerosis, an inflammatory condition of the central nervous system without known genetic cause. The affected individuals were homozygous for a missense MCM3AP variant, located at the Sac3 domain, which was predicted to affect conserved amino acid likely important for the function of the germinal-centre associated nuclear protein. Our data support further expansion of the clinical spectrum linked to MCM3AP variant and highlight that MCM3AP should be considered in patients with accompaniment of recessive motor axonal Charcot-Marie-Tooth neuropathy and multiple sclerosis.

Place, publisher, year, edition, pages
Oxford University Press, 2019
Keywords
multiple sclerosis, Charcot-Marie-Tooth
National Category
Basic Medicine
Research subject
Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-17978 (URN)10.1093/braincomms/fcz011 (DOI)
Available from: 2019-12-05 Created: 2019-12-05 Last updated: 2019-12-27Bibliographically approved
Sedghi, M., Salari, M., Moslemi, A.-R., Kariminejad, A., Davis, M., Goullée, H., . . . Tajsharghi, H. (2018). Ataxia-telangiectasia-like disorder in a family deficient for MRE11A, caused by a MRE11 variant. Neurology: Genetics, 4(6), Article ID e295.
Open this publication in new window or tab >>Ataxia-telangiectasia-like disorder in a family deficient for MRE11A, caused by a MRE11 variant
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2018 (English)In: Neurology: Genetics, ISSN 2376-7839, Vol. 4, no 6, article id e295Article in journal (Refereed) Published
Abstract [en]

Objective We report 3 siblings with the characteristic features of ataxia-telangiectasia-like disorder associated with a homozygous MRE11 synonymous variant causing nonsense-mediated mRNA decay (NMD) and MRE11A deficiency. Methods Clinical assessments, next-generation sequencing, transcript and immunohistochemistry analyses were performed. Results The patients presented with poor balance, developmental delay during the first year of age, and suffered from intellectual disability from early childhood. They showed oculomotor apraxia, slurred and explosive speech, limb and gait ataxia, exaggerated deep tendon reflex, dystonic posture, and mirror movement in their hands. They developed mild cognitive abilities. Brain MRI in the index case revealed cerebellar atrophy. Next-generation sequencing revealed a homozygous synonymous variant in MRE11 (c.657C>T, p.Asn219=) that we show affects splicing. A complete absence of MRE11 transcripts in the index case suggested NMD and immunohistochemistry confirmed the absence of a stable protein. Conclusions Despite the critical role of MRE11A in double-strand break repair and its contribution to the Mre11/Rad50/Nbs1 complex, the absence of MRE11A is compatible with life. 

Place, publisher, year, edition, pages
Lippincott Williams & Wilkins, 2018
National Category
Clinical Laboratory Medicine
Research subject
Bioinformatics; Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-16631 (URN)10.1212/NXG.0000000000000295 (DOI)000455099800019 ()30584599 (PubMedID)2-s2.0-85060870481 (Scopus ID)
Note

From the Medical Genetics Laboratory (M. Sedghi), Alzahra University Hospital, Isfahan University of Medical Sciences, Isfahan, Iran; Department of Neurology (M. Salari), Shahid Beheshti University of Medical Science, Tehran, Iran; Department of Pathology (A.-R.M.), University of Gothenburg, Sahlgrenska University Hospital, Sweden; Kariminejad-Najmabadi Pathology & Genetics Center (A.K.), Tehran, Iran; Department of Diagnostic Genomics (M.D.), Pathwest, QEII Medical Centre; Centre for Medical Research (H.G., N.L., H.T.), The University of Western Australia and the Harry Perkins Institute for Medical Research, Nedlands, Australia; School of Bioscience (B.O.), University of Skovde; and Division Biomedicine (H.T.), School of Health and Education, University of Skovde, Sweden.

Available from: 2019-02-15 Created: 2019-02-15 Last updated: 2019-05-09
Dahl-Halvarsson, M., Olive, M., Pokrzywa, M., Ejeskär, K., Palmer, R. H., Uv, A. E. & Tajsharghi, H. (2018). Drosophila model of myosin myopathy rescued by overexpression of a TRIM-protein family member. Proceedings of the National Academy of Sciences of the United States of America, 115(28), E6566-E6575
Open this publication in new window or tab >>Drosophila model of myosin myopathy rescued by overexpression of a TRIM-protein family member
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2018 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 115, no 28, p. E6566-E6575Article in journal (Refereed) Published
Abstract [en]

Myosin is a molecular motor indispensable for body movement and heart contractility. Apart from pure cardiomyopathy, mutations in MYH7 encoding slow/β-cardiac myosin heavy chain also cause skeletal muscle disease with or without cardiac involvement. Mutations within the α-helical rod domain of MYH7are mainly associated with Laing distal myopathy. To investigate the mechanisms underlying the pathology of the recurrent causative MYH7 mutation (K1729del), we have developed a Drosophila melanogaster model of Laing distal myopathy by genomic engineering of the Drosophila Mhc locus. Homozygous MhcK1728del animals die during larval/pupal stages, and both homozygous and heterozygous larvae display reduced muscle function. Flies expressing only MhcK1728del in indirect flight and jump muscles, and heterozygous MhcK1728del animals, were flightless, with reduced movement and decreased lifespan. Sarcomeres of MhcK1728del mutant indirect flight muscles and larval body wall muscles were disrupted with clearly disorganized muscle filaments. Homozygous MhcK1728del larvae also demonstrated structural and functional impairments in heart muscle, which were not observed in heterozygous animals, indicating a dose-dependent effect of the mutated allele. The impaired jump and flight ability and the myopathy of indirect flight and leg muscles associated with MhcK1728del were fully suppressed by expression of Abba/Thin, an E3-ligase that is essential for maintaining sarcomere integrity. This model of Laing distal myopathy in Drosophila recapitulates certain morphological phenotypic features seen in Laing distal myopathy patients with the recurrent K1729del mutation. Our observations that Abba/Thin modulates these phenotypes suggest that manipulation of Abba/Thin activity levels may be beneficial in Laing distal myopathy.

Place, publisher, year, edition, pages
National Academy of Sciences, 2018
National Category
Genetics Neurology
Research subject
Biomedical Genetics
Identifiers
urn:nbn:se:his:diva-15878 (URN)10.1073/pnas.1800727115 (DOI)000438050900023 ()29946036 (PubMedID)2-s2.0-85049855441 (Scopus ID)
Available from: 2018-06-29 Created: 2018-06-29 Last updated: 2019-11-20Bibliographically approved
Lee, R. G., Sedghi, M., Salari, M., Shearwood, A.-M. J., Stentenbach, M., Kariminejad, A., . . . Filipovska, A. (2018). Early-onset Parkinson disease caused by a mutation in CHCHD2 and mitochondrial dysfunction. Neurology Genetics, 4(5), Article ID e276.
Open this publication in new window or tab >>Early-onset Parkinson disease caused by a mutation in CHCHD2 and mitochondrial dysfunction
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2018 (English)In: Neurology Genetics, ISSN 2376-7839, Vol. 4, no 5, article id e276Article in journal (Refereed) Published
Abstract [en]

Objective Our goal was to identify the gene(s) associated with an early-onset form of Parkinson disease (PD) and the molecular defects associated with this mutation. Methods We combined whole-exome sequencing and functional genomics to identify the genes associated with early-onset PD. We used fluorescence microscopy, cell, and mitochondrial biology measurements to identify the molecular defects resulting from the identified mutation. Results Here, we report an association of a homozygous variant in CHCHD2, encoding coiled-coil-helix-coiled-coil-helix domain containing protein 2, a mitochondrial protein of unknown function, with an early-onset form of PD in a 26-year-old Caucasian woman. The CHCHD2 mutation in PD patient fibroblasts causes fragmentation of the mitochondrial reticular morphology and results in reduced oxidative phosphorylation at complex I and complex IV. Although patient cells could maintain a proton motive force, reactive oxygen species production was increased, which correlated with an increased metabolic rate. Conclusions Our findings implicate CHCHD2 in the pathogenesis of recessive early-onset PD, expanding the repertoire of mitochondrial proteins that play a direct role in this disease.

Place, publisher, year, edition, pages
Wolters Kluwer, 2018
National Category
Clinical Medicine
Research subject
Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-16378 (URN)10.1212/NXG.0000000000000276 (DOI)000447372900012 ()30338296 (PubMedID)
Available from: 2018-11-09 Created: 2018-11-09 Last updated: 2019-09-30Bibliographically approved
Nilipour, Y., Nafissi, S., Tjust, A. E., Ravenscroft, G., Hossein-Nejad Nedai, H., Taylor, R. L., . . . Tajsharghi, H. (2018). Ryanodine receptor type 3 (RYR3) as a novel gene associated with a myopathy with nemaline bodies. European Journal of Neurology, 25(6), 841-847
Open this publication in new window or tab >>Ryanodine receptor type 3 (RYR3) as a novel gene associated with a myopathy with nemaline bodies
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2018 (English)In: European Journal of Neurology, ISSN 1351-5101, E-ISSN 1468-1331, Vol. 25, no 6, p. 841-847Article in journal (Refereed) Published
Abstract [en]

Background: Nemaline myopathy has been associated with mutations in twelve genes to date. However, for some patients diagnosed with nemaline myopathy, definitive mutations are not identified in the known genes, suggesting there are other genes involved. This study describes compound heterozygosity for rare variants in RYR3 in one such patient.

Results: Clinical examination of the patient at 22 years of age revealed a long-narrow face, high arched palate and bilateral facial weakness. She had proximal weakness in all four limbs, mild scapular winging but no scoliosis. Muscle biopsy revealed wide variation in fibre size with type 1 fibre predominance and atrophy. Abundant nemaline bodies were located in perinuclear areas, subsarcolemmal and within the cytoplasm. No likely pathogenic mutations in known nemaline myopathy genes were identified. Copy number variation in known nemaline myopathy genes was excluded by nemaline myopathy targeted array-CGH. Next generation sequencing revealed compound heterozygous missense variants in the ryanodine receptor type 3 gene (RYR3).  RYR3 transcripts are expressed in human fetal and adult skeletal muscle as well as in human brain or cauda equina samples. Immunofluorescence of human skeletal muscle revealed a "single-row" appearance of RYR3, interspaced between the "double-rows" of RYR1 at each A-I junction.

Conclusion: The results suggest that variants in RYR3 may cause a recessive muscle disease with pathological features including nemaline bodies. We characterize the expression pattern of RYR3 in human skeletal muscle and brain and the subcellular localization of RYR1 and RYR3 in human skeletal muscle.

Place, publisher, year, edition, pages
Blackwell Publishing, 2018
Keywords
RYR3, intracellular Ca2+ channels, nemaline myopathy, ryanodine receptors
National Category
Medical and Health Sciences Genetics Medical Genetics Neurology
Research subject
Biomedical Genetics; Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-14955 (URN)10.1111/ene.13607 (DOI)000431989200012 ()29498452 (PubMedID)2-s2.0-85044433098 (Scopus ID)
Funder
Swedish Research CouncilEU, FP7, Seventh Framework Programme
Available from: 2018-03-12 Created: 2018-03-12 Last updated: 2018-09-25Bibliographically approved
Dahl-Halvarsson, M., Pokrzywa, M., Rauthan, M., Pilon, M. & Tajsharghi, H. (2017). Myosin Storage Myopathy in C. elegans and Human Cultured Muscle Cells. PLoS ONE, 12(1), Article ID e0170613.
Open this publication in new window or tab >>Myosin Storage Myopathy in C. elegans and Human Cultured Muscle Cells
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2017 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 12, no 1, article id e0170613Article in journal (Refereed) Published
Abstract [en]

Myosin storage myopathy is a protein aggregate myopathy associated with the characteristic subsarcolemmal accumulation of myosin heavy chain in muscle fibers. Despite similar histological findings, the clinical severity and age of onset are highly variable, ranging from no weakness to severe impairment of ambulation, and usually childhood-onset to onset later in life. Mutations located in the distal end of the tail of slow/beta-cardiac myosin heavy chain are associated with myosin storage myopathy. Four missense mutations (L1793P, R1845W, E1883K and H1901L), two of which have been reported in several unrelated families, are located within or closed to the assembly competence domain. This location is critical for the proper assembly of sarcomeric myosin rod filaments. To assess the mechanisms leading to protein aggregation in myosin storage myopathy and to evaluate the impact of these mutations on myosin assembly and muscle function, we expressed mutated myosin proteins in cultured human muscle cells and in the nematode Caenorhabditis elegans. While L1793P mutant myosin protein efficiently incorporated into the sarcomeric thick filaments, R1845W and H1901L mutants were prone to formation of myosin aggregates without assembly into striated sarcomeric thick filaments in cultured muscle cells. In C. elegans, mutant alleles of the myosin heavy chain gene unc-54 corresponding to R1845W, E1883K and H1901L, were as effective as the wild-type myosin gene in rescuing the null mutant worms, indicating that they retain functionality. Taken together, our results suggest that the basis for the pathogenic effect of the R1845W and H1901L mutations are primarily structural rather than functional. Further analyses are needed to identify the primary trigger for the histological changes seen in muscle biopsies of patients with L1793P and E1883K mutations.

Place, publisher, year, edition, pages
Public Library of Science, 2017
National Category
Medical Biotechnology Basic Medicine
Research subject
Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-13464 (URN)10.1371/journal.pone.0170613 (DOI)000396176100086 ()28125727 (PubMedID)2-s2.0-85010877212 (Scopus ID)
Available from: 2017-03-31 Created: 2017-03-31 Last updated: 2019-11-18Bibliographically approved
Kariminejad, A., Dahl-Halvarsson, M., Ravenscroft, G., Afroozan, F., Keshavarz, E., Goullée, H., . . . Tajsharghi, H. (2017). TOR1A variants cause a severe arthrogryposis with developmental delay, strabismus and tremor. Brain, 140(11), 2851-2859
Open this publication in new window or tab >>TOR1A variants cause a severe arthrogryposis with developmental delay, strabismus and tremor
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2017 (English)In: Brain, ISSN 0006-8950, E-ISSN 1460-2156, Vol. 140, no 11, p. 2851-2859Article in journal (Refereed) Published
Abstract [en]

Autosomal dominant torsion dystonia-1 is a disease with incomplete penetrance most often caused by an in-frame GAG deletion (p.Glu303del) in the endoplasmic reticulum luminal protein torsinA encoded by TOR1A.

We report an association of the homozygous dominant disease-causing TOR1A p.Glu303del mutation, and a novel homozygous missense variant (p.Gly318Ser) with a severe arthrogryposis phenotype with developmental delay, strabismus and tremor in three unrelated Iranian families. All parents who were carriers of the TOR1A variant showed no evidence of neurological symptoms or signs, indicating decreased penetrance similar to families with autosomal dominant torsion dystonia-1. The results from cell assays demonstrate that the p.Gly318Ser substitution causes a redistribution of torsinA from the endoplasmic reticulum to the nuclear envelope, similar to the hallmark of the p.Glu303del mutation.

Our study highlights that TOR1A mutations should be considered in patients with severe arthrogryposis and further expands the phenotypic spectrum associated with TOR1A mutations. 

Place, publisher, year, edition, pages
Oxford University Press, 2017
Keywords
TOR1A, endoplasmic reticulum luminal protein torsinA, DYT1 dystonia, TOR1A p.Glu303del, severe arthrogryposis
National Category
Clinical Medicine
Research subject
Translational Medicine TRIM
Identifiers
urn:nbn:se:his:diva-14154 (URN)10.1093/brain/awx230 (DOI)000414357800017 ()29053766 (PubMedID)2-s2.0-85034765470 (Scopus ID)
Funder
EU, FP7, Seventh Framework Programme, 608473MoRe Research, 608473Swedish Research Council
Available from: 2017-09-25 Created: 2017-09-25 Last updated: 2018-02-27Bibliographically approved
Kariminejad, A., Ghaderi-Sohi, S., Hossein-Nejad Nedai, H., Varasteh, V., Moslemi, A.-R. & Tajsharghi, H. (2016). Lethal multiple pterygium syndrome, the extreme end of the RYR1 spectrum. BMC Musculoskeletal Disorders, 17(1), 1-5, Article ID 109.
Open this publication in new window or tab >>Lethal multiple pterygium syndrome, the extreme end of the RYR1 spectrum
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2016 (English)In: BMC Musculoskeletal Disorders, ISSN 1471-2474, E-ISSN 1471-2474, Vol. 17, no 1, p. 1-5, article id 109Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: Lethal multiple pterygium syndrome (LMPS, OMIM 253290), is a fatal disorder associated with anomalies of the skin, muscles and skeleton. It is characterised by prenatal growth failure with pterygium present in multiple areas and akinesia, leading to muscle weakness and severe arthrogryposis. Foetal hydrops with cystic hygroma develops in affected foetuses with LMPS. This study aimed to uncover the aetiology of LMPS in a family with two affected foetuses.

METHODS AND RESULTS: Whole exome sequencing studies have identified novel compound heterozygous mutations in RYR1 in two affected foetuses with pterygium, severe arthrogryposis and foetal hydrops with cystic hygroma, characteristic features compatible with LMPS. The result was confirmed by Sanger sequencing and restriction fragment length polymorphism analysis.

CONCLUSIONS: RYR1 encodes the skeletal muscle isoform ryanodine receptor 1, an intracellular calcium channel with a central role in muscle contraction. Mutations in RYR1 have been associated with congenital myopathies, which form a continuous spectrum of pathological features including a severe variant with onset in utero with fetal akinesia and arthrogryposis. Here, the results indicate that LMPS can be considered as the extreme end of the RYR1-related neonatal myopathy spectrum. This further supports the concept that LMPS is a severe disorder associated with defects in the process known as excitation-contraction coupling.

Place, publisher, year, edition, pages
BioMed Central, 2016
Keywords
Lethal multiple pterygium syndrome, Akinesia, Arthrogryposis, Foetal hydrops, Cystic hygroma, Ryanodine receptor 1, RYR1
National Category
Medical Genetics
Identifiers
urn:nbn:se:his:diva-12050 (URN)10.1186/s12891-016-0947-5 (DOI)000371387600001 ()26932181 (PubMedID)2-s2.0-84959363680 (Scopus ID)
Available from: 2016-03-18 Created: 2016-03-18 Last updated: 2018-01-10Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-8854-5213

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