Plectin expression patterns determine two distinct subtypes of epidermolysis bullosa simplex

Natsuga, Ken; Nishie, Wataru; Akiyama, Masashi; Nakamura, Hideki; Shinkuma, Satoru; McMillan, James R.; Nagasaki, Akari; Has, Cristina; O‐Uchi, Toshiaki; Ishiko, Akira; Hirako, Yoshiaki; Owaribe, Katsushi; Sawamura, Daisuke; Bruckner‐Tuderman, Leena; Shimizu, Hiroshi

doi:10.1002/humu.21189

Cited by 44 publications

(66 citation statements)

References 50 publications

(53 reference statements)

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“…32 We therefore confirmed presence of the rodless domain by sequencing cDNA and used realtime PCR to compare the relative abundance of the rodless transcript in P1, P2, and 3 normal controls. The rodless transcript/full transcript ratio was 0.15 in P1, 0.32 in P2, and 0.22 Ϯ 0.03 (mean Ϯ SD) in 3 controls.…”

Section: Resultsmentioning

confidence: 89%

“…It has been suggested that expression of the rodless transcript can mitigate the phenotype in patients who carry mutations in the plectin rod domain. 32 However, real-time PCR indicates that expression of the rodless transcript was higher in the more severely affected P2. Thus in the patients studied by us the abundance of the rodless transcript was not a reliable indicator of the clinical phenotype.…”

Section: Resultsmentioning

confidence: 99%

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Myasthenic syndrome caused by plectinopathy

Selcen¹,

Juel²,

Hobson‐Webb³

et al. 2011

Neurology

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Section: Resultsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Myasthenic syndrome caused by plectinopathy

Selcen¹,

Juel²,

Hobson‐Webb³

et al. 2011

Neurology

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“…Almost half of the patients (20) were homozygotes. In summary, 54 different mutations in eight exons (9,14,19,21,22,24,31,32) and in three introns (i11, i25, i30) were found by DNA molecular analysis. Mutations were mostly located in exons 31 (69% of all mutations) and 32 (14% of all mutations), see Table 1.…”

Section: Discussionmentioning

confidence: 99%

“…In these patients the full-length plectin is absent, but they typically express a rodless plectin isoform, which delays the onset of MD because of the remaining IFbinding site. 13,14 In EBS-PA patients the more severe disease phenotype is caused by the fact that both full-length and rodless plectin isoforms are deficient. 15 So far, 49 patients with EBS-MD have been described in the literature (our patient included).…”

Section: Discussionmentioning

confidence: 99%

Epidermolysis bullosa simplex with muscular dystrophy. Review of the literature and a case report

Kýrová

Kopečková

Bučková

et al. 2017

J Dermatol Case Rep

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Background: Epidermolysis bullosa simplex associated with muscular dystrophy is a genetic skin disease caused by plectin deficiency. A case of a 19-year-old Czech patient affected with this disease and a review all previously published clinical cases are presented. Main observations: In our patient, skin signs of the disease developed after birth. Bilateral ptosis at the age of 8 years was considered as the first specific symptom of muscular dystrophy. Since then, severe scoliosis, urological and psychiatric complication have quickly developed. The signs of plectin deficiency were found by histopathological studies, electron microscopy and antigen mapping of the skin and muscular samples. Two autosomal recessive mutations in the plectin gene leading to premature termination codon were disclosed by mutation analysis. By review of all published clinical cases, 49 patients with this disease were found. 54 different mutations in the plectin gene were published, p.(Arg2319*) in exon 31 being the most frequently found. Median age of muscular dystrophy development was 9.5 years. Hoarseness and respiratory complications were the most often complications beside skin involvement. Conclusion: Epidermolysis bullosa simplex with muscular dystrophy was diagnosed based on clinical, histopathological (skin and muscle biopsy) and mutation analysis of the plectin gene. Overview of the genetic and clinical characteristic of this disease could be presented by review of all previously published clinical cases. (J Der-

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“…Patients exhibit severe skin blistering with gastric abnormalities, particularly pyloric or duodenal atresia (Nakamura et al, 2005). Most EBS-MD patients have mutations in exon 31 encoding the plectin rod domain and it may be that expression of the rodless isoform, which is maintained in these patients, alleviates skin blistering symptoms (which are much less severe than those in patients with EBS-PA) and delays the onset of muscle weakness (Natsuga et al, 2010). It is worth noting that mutations in ITGA6 and ITGB4, encoding the hemidesmosomal integrin subunits a 6 and b 4 respectively, can result in another form of EB, junctional EB-PA. EBS-Olga is an autosomal dominant disease that is characterised by skin blistering, predominantly on the hands and feet, and generalised bruising.…”

Section: Diseases Of Plectin and Bpag1mentioning

confidence: 99%

Plakin Proteins, Hemidesmosomes and Human Disease

Chidgey

2012

Encyclopedia of Life Sciences

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The plakin proteins are a family of cytolinker proteins that connect elements of the cell cytoskeleton to each other and to junctional complexes at the cell membrane. There are seven mammalian plakin proteins and they are characterised by the presence of a plakin domain and/or a plakin repeat domain. The plakins play a vital role in maintaining the integrity of tissues, such as the skin and heart, which are subjected to mechanical stress. Two plakin proteins, plectin and bullous pemphigoid antigen 1 (BPAG1), are essential components of hemidesmosomes, cell–extracellular matrix junctions of epithelial cells, and inherited mutations in either can result in the skin blistering disease epidermolysis bullosa simplex. Mutations in the desmosomal plakin protein desmoplakin can cause the heart muscle disorder arrhythmogenic right ventricular dysplasia, a common cause of sudden cardiac arrest and death in young adults. Plakin proteins are targeted by pathogenic autoantibodies in the skin blistering diseases bullous pemphigoid and paraneoplastic pemphigus. Key Concepts: The plakin proteins are a family of cytolinker proteins that connect elements of the cell cytoskeleton to each other and to junctional complexes at the cell membrane. Seven plakin proteins are found in mammals; plectin, BPAG1, desmoplakin, envoplakin, periplakin, microtubule–actin crosslinking factor 1 and epiplakin. Plectin and BPAG1 are important constituents of hemidesmosomes, cell–extracellular matrix junctions. Mutations in plakin proteins can result in skin blistering disease, muscular dystrophy, autonomic neuropathy and cardiomyopathy. Plakin proteins have been implicated in the autoimmune skin blistering diseases bullous pemphigoid and paraneoplastic pemphigus.

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Plectin expression patterns determine two distinct subtypes of epidermolysis bullosa simplex

Cited by 44 publications

References 50 publications

Myasthenic syndrome caused by plectinopathy

Myasthenic syndrome caused by plectinopathy

Epidermolysis bullosa simplex with muscular dystrophy. Review of the literature and a case report

Plakin Proteins, Hemidesmosomes and Human Disease

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