Early clinical signs and treatment of Menkes disease

Fujisawa, Chie; Kodama, Hiroko; Sato, Yasuhiro; Mimaki, Masakazu; Yagi, Minoru; Awano, Hiroyuki; Matsuo, Muneaki; Shintaku, Haruo; Yoshida, Sayaka; Takayanagi, Masaki; Kubota, Minoru; Takahashi, Akihito; Akasaka, Yoshikiyo

doi:10.1016/j.ymgmr.2022.100849

Cited by 15 publications

(9 citation statements)

References 36 publications

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“…The same variant in an infant with delayed Menkes diagnosis (Woodfin et al, 2019), and then copper histidinate treatment, led to premature death, underlying the need of early diagnosis. Therefore, copper histidinate therapy might only modify the progression of disease if initiated within 30 days after birth, as has been reported elsewhere (Vairo et al, 2019;Fujisawa et al, 2022). In our case Menkes disease was diagnosed at 4 months of age, thus the patient was treated with symptomatic management because copper histidine treatment would not have been effective.…”

Section: Discussionsupporting

confidence: 57%

Menkes disease complicated by concurrent ACY1 deficiency: A case report

Mauri

Saielli²,

Alfei³

et al. 2023

Front. Genet.

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Introduction: Menkes disease is an X‐linked recessive condition caused by mutations in the ATP7A gene, which leads to severe copper deficiency. Aminoacylase-1 deficiency is a rare inborn error of metabolism caused by homozygous or compound heterozygous variant in the ACY1 gene, characterized by increased urinary excretion of specific N-acetyl amino acids.Case presentation: We report an infant with neurological findings such as seizures, neurodevelopmental delay and hypotonia. Metabolic screening showed low serum copper and ceruloplasmin, and increased urinary excretion of several N-acetylated amino acids. Whole-exome sequencing analysis (WES) revealed the novel de novo variant c.3642_3649dup (p.Ala1217Aspfs*2) in the ATP7A gene, leading to a diagnosis of Menkes disease, and the simultaneous presence of the homozygous ACY1 variant c.1057C>T (p.Arg353Cys) causative of Aminoacylase-1 deficiency.Conclusion: Our patient had two rare conditions with different treatment courses but overlapping clinical features. The identified novel ATP7A mutation associated with Menkes disease expands the ATP7A gene spectrum.

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Section: Discussionsupporting

confidence: 57%

Menkes disease complicated by concurrent ACY1 deficiency: A case report

Mauri

Saielli²,

Alfei³

et al. 2023

Front. Genet.

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“…3 While the CTR1 defect described here apparently impeded fetal and neonatal copper uptake, infants with Menkes disease are presumably born with normal copper stores but gradually develop increasing copper deficiency due to failure of intestinal copper uptake. [12][13][14][15][16][17] The corkscrew appearance of cerebral arterial vessels, as revealed by MR angiography, in the CTR1 patient resembles the tortuosity of cranial arteries observed as a consistent feature of children with Menkes disease. 12 Cerebral infarctions and hemorrhages have also been reported in some Menkes disease patients, 18 presumably secondary to arterial fragility and occlusion.…”

Section: Biochemical Investigationsmentioning

confidence: 62%

Fatal congenital copper transport defect caused by a homozygous likely pathogenic variant of SLC31A1

et al. 2022

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Known hereditary human diseases featuring impaired copper trafficking across cellular membranes involve ATP7A (Menkes disease, occipital horn disease, X-linked spinal muscular atrophy type 3) and ATP7B (Wilson disease). Herein, we report a newborn infant of consanguineous parents with a homozygous pathogenic variant in a highly conserved sequence of SLC31A1, coding for the copper influx transporter 1, CTR1. This missense variant, c.236T > C, was detected by whole exome sequenc-

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“…Both excess and deficient concentrations of metal ions in the body can cause mild to fatal diseases. For example, Wilsons disease, that results in a buildup of copper in the body [17] can be treated by copper-chelation therapy [18]; whereas copper deficiency due to Menkes disease [19], which causes copper deficiency in cells, is usually fatal, although copper therapy has been shown to ameliorate the condition [20]. Likewise an excess of iron, as in that caused by the genetic hemochromatosis [21], is treated using iron-binding sorbents [22]; and iron deficiency, anemia, is treated by iron supplements or transfusion [23].…”

Section: Metal Binding In Biological Systemsmentioning

confidence: 99%

“…Destabilization and misfolding caused by manganese-binding in prion disease [149] was studied with a 30-amino acid peptide comprising three repeats of a decapeptide repeat in the C-terminal region of the calcium protein, Cap43, that was probed using 1D 1 H-NMR to follow line-broadening upon binding and elucidate the role of divalent ions in the pathogenesis of prion disease [150]. Mn(II) ion binding to a peptide derived from amyloid beta, Aβ (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23), was also studied by measuring line-broadening upon binding by 1D 1 H-NMR [151].…”

Section: Manganesementioning

confidence: 99%

“…A model of the structure of a complex of Co(II) and a fragment of amyloid beta protein, Aβ (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23), was determined by canonical methodology on a sample with a 1:0.01 molar ratio of peptide-to-cobalt. The intensity of the signals were measured as a function of titration and signals with reduced intensity were considered to be proximate to the cobalt ion and served as the cobalt binding center [151].…”

Section: Cobaltmentioning

confidence: 99%

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Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

Shalev

2022

IJMS

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Metal chelation can provide structural stability and form reactive centers in metalloproteins. Approximately one third of known protein structures are metalloproteins, and metal binding, or the lack thereof, is often implicated in disease, making it necessary to be able to study these systems in detail. Peptide-metal complexes are both present in nature and can provide a means to focus on the binding region of a protein and control experimental variables to a high degree. Structural studies of peptide complexes with metal ions by nuclear magnetic resonance (NMR) were surveyed for all the essential metal complexes and many non-essential metal complexes. The various methods used to study each metal ion are presented together with examples of recent research. Many of these metal systems have been individually reviewed and this current overview of NMR studies of metallopeptide complexes aims to provide a basis for inspiration from structural studies and methodology applied in the field.

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Early clinical signs and treatment of Menkes disease

Cited by 15 publications

References 36 publications

Menkes disease complicated by concurrent ACY1 deficiency: A case report

Menkes disease complicated by concurrent ACY1 deficiency: A case report

Fatal congenital copper transport defect caused by a homozygous likely pathogenic variant of SLC31A1

Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

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