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Journal articles on the topic 'Menkes disease; Copper transport'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Herd, S. M., J. Camakaris, R. Christofferson, P. Wookey, and D. M. Danks. "Uptake and efflux of copper-64 in Menkes'-disease and normal continuous lymphoid cell lines." Biochemical Journal 247, no. 2 (October 15, 1987): 341–47. http://dx.doi.org/10.1042/bj2470341.

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The accumulation of copper over 2 h by normal lymphoid cells and those from Menkes'-disease patients (Menkes' cells) was found to be biphasic, with an initial phase of rapid uptake, an approach to steady state at around 40-60 min, followed by a further accumulation phase. The accumulation of copper was not diminished by the addition of a variety of metabolic inhibitors, suggesting that copper uptake is not an active process. The presence of carbonyl cyanide m-chlorophenylhydrazone in the culture medium stimulated the uptake and accumulation of copper in both normal and Menkes' cells to the same absolute level. This effect appeared to be specific for copper, since the accumulation of Zn and Cd was unaffected. Menkes' cells did not differ from normal in their initial rate of copper uptake. Analysis of the uptake curve suggested that the membrane transport of copper involves both passive and facilitated diffusion. Initial rate of efflux from the cells was approximated by two methods. Menkes' cells did not appear to be affected in this function. It seems likely that the basic defect in Menkes' disease involves a step in intracellular copper transport rather than the membrane transport of copper.

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2

Agertt, Fabio, Ana C. S. Crippa, Paulo J. Lorenzoni, Rosana H. Scola, Isac Bruck, Luciano de Paola, Carlos E. Silvado, and Lineu C. Werneck. "Menkes' disease: case report." Arquivos de Neuro-Psiquiatria 65, no. 1 (March 2007): 157–60. http://dx.doi.org/10.1590/s0004-282x2007000100032.

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Menkes’ disease is a rare neurodegenerative disorder due to an intracellular defect of a copper transport protein. We describe a 7 months male patient who presented with seizures, hypoactivity and absence of visual contact. The investigation disclosed pilli torti and thrycorrexis nodosa in the hair, low serum levels of both copper and ceruloplasmin, brain magnetic resonance study showed atrophy and white matter hypointensities on T1-weighted images, electroencephalogram reveals moderate background activity disorganization and epileptiform activity, and muscle biopsy with type 2 fiber atrophy. The clinical, laboratorial, genetic, muscle biopsy and neurophysiological findings in Menkes’ disease are discussed.

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3

Choudhary, Richa, Anita Choudhary, and S. Sitaraman. "Menkes Disease- A Rare Neurodegenerative Disorder." Journal of Nepal Paediatric Society 35, no. 2 (January 20, 2016): 177–80. http://dx.doi.org/10.3126/jnps.v35i2.11966.

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Menkes Disease is a rare neurological disorder of impaired copper transport, characterized by progressive neurodegeneration, refractory epilepsy and characteristic hair abnormalities. Here, we report a 5 month old child with developmental delay, refractory seizures, and hypopigmented short, sparse hair with microscopic pili torti; low serum copper and ceruloplasmin and neuroimaging revealing white matter hyperintensities and tortuous vessels.J Nepal Paediatr Soc 2015;35(2):177-180

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4

Qian, Y., E. Tiffany-Castiglioni, and E. D. Harris. "Functional analysis of a genetic defect of copper transport (Menkes disease) in different cell lines." American Journal of Physiology-Cell Physiology 271, no. 1 (July 1, 1996): C378—C384. http://dx.doi.org/10.1152/ajpcell.1996.271.1.c378.

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To define the function of the Cu-transporting ATPase in Menkes disease, Menkes and normal fibroblasts were incubated with 67Cu before and after brief exposure to -SH reagents, p-chloromercuribenzoate (PCMB) and dithiothreitol (DTT). Accumulation and retention were compared among these cells, BeWo cells, and rat C6 glioma cells similarly treated. The Michaelis constant for influx of 67Cu into normal and Menkes fibroblasts was practically the same (0.21 +/- 0.07 vs. 0.24 +/- 0.06 microM). The PCMB treatment stimulated 67Cu accumulation in C6 cells, inhibited accumulation in normal and Menkes fibroblasts, and did not affect BeWo cells. DTT stimulated 67Cu uptake in all cells but BeWo cells. DTT treatment after PCMB further enhanced 67Cu accumulation in normal fibroblasts and C6 cells but had no enhancing effect on Menkes fibroblasts or BeWo cells. Menkes fibroblasts and BeWo cells released 67Cu at rates considerably slower than normal fibroblasts (0.06 and 0.09 vs. 0.22%/min, respectively). The PCMB blocked 67Cu release from normal fibroblasts but did not affect Menkes fibroblasts or BeWo cells. Reverse transcription-polymerase chain reaction analysis of total RNA from BeWo cells failed to show a predicted 943-base pair fragment representing a partial transcript of the Menkes factor. The fragment was present in extracts from normal fibroblasts. We conclude that the mechanism underlying Cu homeostasis varies among different cell types. As exemplified by BeWo and Menkes cells, failure to efflux Cu ions may be linked with the failure to express a functional Cu-transporting ATPase, namely, the Menkes protein.

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5

ACKLAND, M. Leigh, E. Jean CORNISH, A. Jenny PAYNTER, Andrew GRIMES, Agnes MICHALCZYK, and F. B. Julian MERCER. "Expression of Menkes disease gene in mammary carcinoma cells." Biochemical Journal 328, no. 1 (November 15, 1997): 237–43. http://dx.doi.org/10.1042/bj3280237.

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Two P-type ATPases, MNK and WND were recently shown to be defective in the human disorders of copper transport, Menkes disease and Wilson disease respectively. These proteins are important in copper homeostasis but their full physiological function has not been established. This study uses the human breast carcinoma line, PMC42, to investigate copper transport in the mammary gland. Northern blot analysis indicated that both MNK and WND mRNA are expressed in these cells. Western blot analysis with an MNK-specific antibody demonstrated a band of approx. 178 kDa, close to the expected size of 163 kDa. Treatment of PMC42 cells with lactational hormones (oestrogen and progesterone for 3 days followed by dexamethasone, insulin and prolactin for a further 3 days) did not produce an obvious increase in MNK expression as measured by Northern and Western blots. By using indirect immunofluorescence with the MNK antibody, the intracellular distribution of MNK was found to be predominantly perinuclear, consistent with Golgi localization. Punctate staining was also seen in a smaller proportion of cells, suggesting that some MNK is associated with endosomes. Treatment of PMC42 cells with lactational hormones increased the intensity of the perinuclear and punctate fluorescence. Exposure of cells to 100 mM copper resulted in the dispersion of the fluorescence towards the periphery of the cell. The results suggest a role for MNK in the secretion of copper into milk and that PMC42 cells are a valuable model for investigating the detailed cellular function of MNK and WND.

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6

Kaler, Stephen G. "Metabolic and Molecular Bases of Menkes Disease and Occipital Horn Syndrome." Pediatric and Developmental Pathology 1, no. 1 (January 1998): 85–98. http://dx.doi.org/10.1007/s100249900011.

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Menkes disease and occipital horn syndrome (OHS) are related disorders of copper transport that involve abnormal neurodevelopment, connective tissue problems, and often premature death. Location of the gene responsible for these conditions on the X chromosome was indicated by pedigree analysis from the time of these syndromes' earliest descriptions. Characterization of an affected female with an X-autosomal translocation was used to identify the Menkes/OHS gene, which encodes a highly evolutionarily conserved, copper-transporting P-type ATPase. The gene normally is expressed in nearly all human tissues, and it localizes to the trans-Golgi network of cells. However, in over 70% of Menkes and OHS patients studied, expression of this gene has been demonstrated to be abnormal. Major gene deletions detectable by Southern blotting account for 15–20% of patients, and an interesting spectrum of other mutations is evident among 58 families whose precise molecular defects have been reported as of this writing. The center region of the gene seems particularly prone to mutation, and those that influence mRNA processing and splicing appear to be relatively common. Further advances in understanding the molecular and cell biological mechanisms involved in normal copper transport may ultimately yield new and better approaches to the management of these disorders.

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7

Waldrop, G. L., and M. J. Ettinger. "The relationship of excess copper accumulation by fibroblasts from the brindled mouse model of Menkes disease to the primary defect." Biochemical Journal 267, no. 2 (April 15, 1990): 417–22. http://dx.doi.org/10.1042/bj2670417.

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Fibroblasts from the brindled mouse model of Menkes disease are known to accumulate excess copper. Most of the copper in the cytosol of these fibroblasts is bound to metallothionein (MT), which is elevated in Menkes or brindled mouse fibroblasts. Copper accumulation by normal fibroblasts containing excess MT was examined to determine if the excess copper accumulation phenotype was secondary to excess MT or associated with the primary defect in fibroblasts from the brindled mice. MT was induced in normal fibroblasts by copper, zinc or dexamethasone to levels comparable with those in brindled mice fibroblasts, as determined by radioimmunoassays. Normal fibroblasts containing excess MT accumulate copper normally, i.e. they do not exhibit the excess copper accumulation phenotype. Consistent with this result, copper efflux from normal fibroblasts containing excess MT was also normal. The data suggest that one function of the protein associated with the primary defect is to help determine how much copper is taken up and retained by fibroblasts and other cell types exhibiting the excess copper phenotype in Menkes disease. The capacity of this protein is apparently exceeded in normal fibroblasts if serum or albumin is not present extracellularly to limit total copper uptake. Consistent with a defect in an intracellular protein, the kinetics of copper transport by brindled mice fibroblasts were found to be normal.

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8

DiDonato, Michael, and Bibudhendra Sarkar. "Copper transport and its alterations in Menkes and Wilson diseases." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1360, no. 1 (February 1997): 3–16. http://dx.doi.org/10.1016/s0925-4439(96)00064-6.

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9

Fatemi, Negah, and Bibudhendra Sarkar. "Insights into the mechanism of copper transport by the Wilson and Menkes disease copper-transporting ATPases." Inorganica Chimica Acta 339 (November 2002): 179–87. http://dx.doi.org/10.1016/s0020-1693(02)00949-0.

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10

Gautam-Basak, M., J. F. Gallelli, and B. Sarkar. "Formulation of copper-histidine for the treatment of Menkes disease, a genetic disorder of copper transport." Journal of Inorganic Biochemistry 51, no. 1-2 (July 1993): 415. http://dx.doi.org/10.1016/0162-0134(93)85444-d.

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11

Hung, Ya Hui, Meredith J. Layton, Ilia Voskoboinik, Julian F. B. Mercer, and James Camakaris. "Purification and membrane reconstitution of catalytically active Menkes copper-transporting P-type ATPase (MNK; ATP7A)." Biochemical Journal 401, no. 2 (December 21, 2006): 569–79. http://dx.doi.org/10.1042/bj20060924.

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The MNK (Menkes disease protein; ATP7A) is a major copper- transporting P-type ATPase involved in the delivery of copper to cuproenzymes in the secretory pathway and the efflux of excess copper from extrahepatic tissues. Mutations in the MNK (ATP7A) gene result in Menkes disease, a fatal neurodegenerative copper deficiency disorder. Currently, detailed biochemical and biophysical analyses of MNK to better understand its mechanisms of copper transport are not possible due to the lack of purified MNK in an active form. To address this issue, we expressed human MNK with an N-terminal Glu-Glu tag in Sf9 [Spodoptera frugiperda (fall armyworm) 9] insect cells and purified it by antibody affinity chromatography followed by size-exclusion chromatography in the presence of the non-ionic detergent DDM (n-dodecyl β-D-maltopyranoside). Formation of the classical vanadate-sensitive phosphoenzyme by purified MNK was activated by Cu(I) [EC50=0.7 μM; h (Hill coefficient) was 4.6]. Furthermore, we report the first measurement of Cu(I)-dependent ATPase activity of MNK (K0.5=0.6 μM; h=5.0). The purified MNK demonstrated active ATP-dependent vectorial 64Cu transport when reconstituted into soya-bean asolectin liposomes. Together, these data demonstrated that Cu(I) interacts with MNK in a co-operative manner and with high affinity in the sub-micromolar range. The present study provides the first biochemical characterization of a purified full-length mammalian copper-transporting P-type ATPase associated with a human disease.

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12

Hardman, Belinda, Agnes Michalczyk, Mark Greenough, James Camakaris, Julian F. B. Mercer, and M. Leigh Ackland. "Hormonal regulation of the Menkes and Wilson copper-transporting ATPases in human placental Jeg-3 cells." Biochemical Journal 402, no. 2 (February 12, 2007): 241–50. http://dx.doi.org/10.1042/bj20061099.

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Copper deficiency during pregnancy results in early embryonic death and foetal structural abnormalities including skeletal, pulmonary and cardiovascular defects. During pregnancy, copper is transported from the maternal circulation to the foetus by mechanisms which have not been clearly elucidated. Two copper-transporting ATPases, Menkes (ATP7A; MNK) and Wilson (ATP7B; WND), are expressed in the placenta and both are involved in placental copper transport, as copper accumulates in the placenta in both Menkes and Wilson disease. The regulatory mechanisms of MNK and WND and their exact role in the placenta are unknown. Using a differentiated polarized Jeg-3 cell culture model of placental trophoblasts, MNK and WND were shown to be expressed within these cells. Distinct roles for MNK and WND are suggested on the basis of their opposing responses to insulin. Insulin and oestrogen increased both MNK mRNA and protein levels, altered the localization of MNK towards the basolateral membrane in a copper-independent manner, and increased the transport of copper across this membrane. In contrast, levels of WND were decreased in response to insulin, and the protein was located in a tight perinuclear region, with a corresponding decrease in copper efflux across the apical membrane. These results are consistent with a model of copper transport in the placenta in which MNK delivers copper to the foetus and WND returns excess copper to the maternal circulation. Insulin and oestrogen stimulate copper transport to the foetus by increasing the expression of MNK and reducing the expression of WND. These data show for the first time that MNK and WND are differentially regulated by the hormones insulin and oestrogen in human placental cells.

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13

YANG, Xiao-Li, Naoyuki MIURA, Yoshihiko KAWARADA, Kunihiko TERADA, Konstantin PETRUKHIN, T. Conrad GILLIAM, and Toshihiro SUGIYAMA. "Two forms of Wilson disease protein produced by alternative splicing are localized in distinct cellular compartments." Biochemical Journal 326, no. 3 (September 15, 1997): 897–902. http://dx.doi.org/10.1042/bj3260897.

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Copper is an essential trace element in prokaryotes and eukaryotes and is strictly regulated by biological mechanisms. Menkes and Wilson diseases are human disorders that arise from disruption of the normal process of copper export from the cytosol to the extracellular environment. Recently a gene for Wilson disease (WD) (also named the ATP7B gene) was cloned. This gene encodes a copper transporter of the P-type ATPase. We prepared monoclonal and polyclonal anti-(WD protein) antibodies and characterized the full-length WD protein as well as a shorter form that is produced by alternative splicing in the human brain. We found that the WD protein is localized mainly in the Golgi apparatus, whereas the shorter form is present in the cytosol. These results suggest that the alternative WD proteins act as key regulators of copper metabolism, perhaps by performing distinct roles in the intracellular transport and export of copper.

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14

Dierick, Herman A., Ayla N. Adam, June F. Escara-Wilke, and Thomas W. Glover. "Immunocytochemical Localization of the Menkes Copper Transport Protein (ATP7A) to the Trans-Golgi Network." Human Molecular Genetics 6, no. 3 (March 1, 1997): 409–16. http://dx.doi.org/10.1093/hmg/6.3.409.

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Abstract We have generated polyclonal antibodies against the amino-terminal third of the Menkes protein (ATP7A; MNK) by immunizing rabbits with a histidine-tagged MNK fusion construct containing metal-binding domains 1–4. The purified antibodies were used in Western analysis of cell lysates and in indirect immunofluorescence experiments on cultured cells. On Western blots, the antibodies recognized the ∼165 kDa MNK protein in CHO cells and human fibroblasts. No MNK signal could be detected in fibroblasts from a patient with Menkes disease or in Hep3B hepatocellular carcinoma cells, confirming the specificity of the antibodies. Immunocytochemical analysis of CHO cells and human fibroblasts showed a distinct perinuclear signal corresponding to the pattern of the Golgi complex. This staining pattern was similar to that of α-mannosidase II which is a known resident enzyme of the Golgi complex. Using brefeldin A, a fungal inhibitor of protein secretion, we further demonstrated that the MNK protein is localized to the trans-Golgi network. This data provides direct evidence for a subcellular localization of the MNK protein which is similar to the proposed vacuolar localization of Ccc2p, the yeast homolog of MNK and WND (ATP7B), the Wilson disease gene product. In light of the proposed role of MNK both in subcellular copper trafficking and in copper efflux, these data suggest a model for how these two processes are linked and represent an important step in the functional analysis of the MNK protein.

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15

Donsante, Anthony, Paul Johnson, Laura A. Jansen, and Stephen G. Kaler. "Somatic mosaicism in Menkes disease suggests choroid plexus-mediated copper transport to the developing brain." American Journal of Medical Genetics Part A 152A, no. 10 (August 26, 2010): 2529–34. http://dx.doi.org/10.1002/ajmg.a.33632.

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16

Marklová, Eliška. "Microelements and Inherited Metabolic Diseases." Acta Medica (Hradec Kralove, Czech Republic) 45, no. 4 (2002): 129–33. http://dx.doi.org/10.14712/18059694.2019.69.

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In addition to the main groups of inherited metabolic diseases, including mitochondrial, peroxisomal and lysosomal defects, organic acidurias, porphyrias, defects of amino acids, saccharides and fatty acids metabolism, disorders of transport and utilisation of microelements have also been recognized. Recent findings concerning hereditary hemochromatosis (iron), Wilson and Menkes diseases (copper), molybdenum cofactor deficiency (molybdenum), defects of cobalamine synthesis (cobalt) and acrodermatitis enteropathica (zinc) are reviewed.

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17

Anbukumar, Dhanalakshmi S., Stephen G. Kaler, and J. Evan Sadler. "The Involvement of Copper Transport in Von Willebrand Factor Multimer Assembly." Blood 128, no. 22 (December 2, 2016): 2530. http://dx.doi.org/10.1182/blood.v128.22.2530.2530.

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Abstract In the event of vascular injury, the underlying prothrombotic extracellular matrix becomes exposed to circulating blood. Endothelial cells at the site of injury secrete multimeric von Willebrand factor (VWF) that will bind to the exposed extracellular matrix and create a scaffold to which platelets can adhere, forming a platelet plug. These critical steps after vascular injury are essential for creating a stable clot. Intracellular VWF multimer assembly is required for its extracellular function, and defects in VWF assembly cause the bleeding diathesis, von Willebrand disease. In a cell-free in vitro system, we and others find that EDTA or EGTA inhibits multimer formation, and calcium ions have been proposed to be required for this process. However, we find that the binding affinity of calcium ions for VWF D domains is very weak (Kdof 300-400 μM) and that buffers containing less than 2 μM calcium ions support multimer assembly even though few calcium binding sites could be occupied. These results suggest a role for cations other than calcium in VWF multimer assembly. Here we show that copper ions support VWF multimer assembly in a cell-free system and that the intracellular copper transporter, ATP7A, is required for VWF multimer assembly in cultured cells. Some calcium binding proteins undergo a conformational change upon binding calcium ions and exhibit a decrease in the apparent molecular weight (an electrophoretic mobility shift) as assessed by SDS-PAGE and Western blot. Although the D domains of VWF bind calcium ions, they do not exhibit this behavior. We tested a panel of other divalent cations including: iron, magnesium, manganese, zinc, and copper. We found that the VWF N-terminal D'D3 dimer bound copper ions as demonstrated by a shift in electrophoretic mobility. We therefore assessed the effect of copper ions on VWF multimer assembly in vitro. Briefly, addition of monensin (1.5 μM) to human umbilical vein endothelial cells (HUVEC) caused secretion of C-terminal dimers of proVWF into the media. Pretreatment of the conditioned media with the divalent cation chelator, EGTA, or the copper chelator, tetraethylenepentamine (TEPA), preceded immunopurification of C-terminal dimers of proVWF using a rabbit polyclonal anti-hVWF antibody (DAKO A0082) bound to protein A magnetic beads. Beads were incubated at pH 7.4 or pH 5.8, and in the presence or absence of divalent cations for 3 hours at 37°C before analyzing the VWF by gel electrophoresis. Addition of calcium ions (100 μM) to proVWF dimers pretreated with only EGTA allowed some VWF multimer assembly; however, copper ions (100 μM) induced the assembly of higher molecular weight multimers from proVWF dimers pretreated with either EGTA or TEPA. With either divalent cation, multimers assembled at low pH, but not at neutral pH. These findings support a role for copper ions in VWF synthesis. In vivo, free copper ions are toxic; therefore, they are sequestered by a system of chaperones and transporters. We examined the role of the intracellular copper transporter, ATP7A, in VWF multimerization because it is expressed in the trans Golgi network of endothelial cells, the site of VWF multimer assembly. Mick Petris (University of Missouri-Columbia) provided both wildtype and ATP7A knockout mouse embryonic fibroblasts (MEFs). We stably expressed full length human VWF and analyzed the secreted multimers by agarose gel electrophoresis. Wildtype MEFs produced multimeric VWF; however, culturing the MEFs in the presence of the copper chelator, TEPA, markedly impaired VWF multimer assembly. Moreover, ATP7A-null MEFs secreted only VWF dimers. These results indicate that copper ions and ATP7A contribute to VWF multimer assembly in cells. The dependence of VWF assembly on ATP7A in cultured cells suggests that humans with congenital ATP7A deficiency (Menkes disease) could have detectable abnormalities in VWF multimer structure, although dietary copper and parenteral copper replacement therapy could affect this phenotype. Our preliminary analyses have identified a Menkes disease patient with low plasma levels of VWF antigen, multimers and activity. Further study will be required to determine the prevalence and significance of altered VWF multimer assembly in Menkes disease. Disclosures Sadler: BioMarin: Consultancy; 23andMe: Consultancy; Ablynx: Consultancy.

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18

Martinez-Fierro, Margarita L., Griselda A. Cabral-Pacheco, Idalia Garza-Veloz, Jesus Acuña-Quiñones, Laura E. Martinez-de-Villarreal, Marisol Ibarra-Ramirez, Joke Beuten, et al. "Whole-Exome Sequencing, Proteome Landscape, and Immune Cell Migration Patterns in a Clinical Context of Menkes Disease." Genes 12, no. 5 (May 14, 2021): 744. http://dx.doi.org/10.3390/genes12050744.

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Menkes disease (MD) is a rare and often lethal X-linked recessive syndrome, characterized by generalized alterations in copper transport and metabolism, linked to mutations in the ATPase copper transporting α (ATP7A) gene. Our objective was to identify genomic alterations and circulating proteomic profiles related to MD assessing their potential roles in the clinical features of the disease. We describe the case of a male patient of 8 months of age with silvery hair, tan skin color, hypotonia, alterations in neurodevelopment, presence of seizures, and low values of plasma ceruloplasmin. Trio-whole-exome sequencing (Trio-WES) analysis, plasma proteome screening, and blood cell migration assays were carried out. Trio-WES revealed a hemizygous change c.4190C > T (p.S1397F) in exon 22 of the ATP7A gene. Compared with his parents and with child controls, 11 plasma proteins were upregulated and 59 downregulated in the patient. According to their biological processes, 42 (71.2%) of downregulated proteins had a participation in cellular transport. The immune system process was represented by 35 (59.3%) downregulated proteins (p = 9.44 × 10−11). Additional studies are necessary to validate these findings as hallmarks of MD.

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19

Gitlin, Mariko Suzuki1 and Jonathan D. "Intracellular localization of the Menkes and Wilson's disease proteins and their role in intracellular copper transport." Pediatrics International 41, no. 4 (August 1999): 436–42. http://dx.doi.org/10.1046/j.1442-200x.1999.01090.x.

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20

Dolgova, Nataliya V., Sergiy Nokhrin, Corey H. Yu, Graham N. George, and Oleg Y. Dmitriev. "Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification." Biochemical Journal 454, no. 1 (July 26, 2013): 147–56. http://dx.doi.org/10.1042/bj20121656.

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Human copper transporters ATP7B (Wilson's disease protein) and ATP7A (Menkes' disease protein) have been implicated in tumour resistance to cisplatin, a widely used anticancer drug. Cisplatin binds to the copper-binding sites in the N-terminal domain of ATP7B, and this binding may be an essential step of cisplatin detoxification involving copper ATPases. In the present study, we demonstrate that cisplatin and a related platinum drug carboplatin produce the same adduct following reaction with MBD2 [metal-binding domain (repeat) 2], where platinum is bound to the side chains of the cysteine residues in the CxxC copper-binding motif. This suggests the same mechanism for detoxification of both drugs by ATP7B. Platinum can also be transferred to MBD2 from copper chaperone Atox1, which was shown previously to bind cisplatin. Binding of the free cisplatin and reaction with the cisplatin-loaded Atox1 produce the same protein-bound platinum intermediate. Transfer of platinum along the copper-transport pathways in the cell may serve as a mechanism of drug delivery to its target in the cell nucleus, and explain tumour-cell resistance to cisplatin associated with the overexpression of copper transporters ATP7B and ATP7A.

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Donsante, Anthony, Paul Johnson, Laura A. Jansen, and Stephen G. Kaler. "Erratum to: Somatic Mosaicism in Menkes Disease Suggests Choroid Plexus-Mediated Copper Transport to the Developing Brain." American Journal of Medical Genetics Part A 155, no. 8 (July 19, 2011): 2044. http://dx.doi.org/10.1002/ajmg.a.34065.

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22

Lutsenko, Svetlana, Natalie L. Barnes, Mee Y. Bartee, and Oleg Y. Dmitriev. "Function and Regulation of Human Copper-Transporting ATPases." Physiological Reviews 87, no. 3 (July 2007): 1011–46. http://dx.doi.org/10.1152/physrev.00004.2006.

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Copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B are evolutionarily conserved polytopic membrane proteins with essential roles in human physiology. The Cu-ATPases are expressed in most tissues, and their transport activity is crucial for central nervous system development, liver function, connective tissue formation, and many other physiological processes. The loss of ATP7A or ATP7B function is associated with severe metabolic disorders, Menkes disease, and Wilson disease. In cells, the Cu-ATPases maintain intracellular copper concentration by transporting copper from the cytosol across cellular membranes. They also contribute to protein biosynthesis by delivering copper into the lumen of the secretory pathway where metal ion is incorporated into copper-dependent enzymes. The biosynthetic and homeostatic functions of Cu-ATPases are performed in different cell compartments; targeting to these compartments and the functional activity of Cu-ATPase are both regulated by copper. In recent years, significant progress has been made in understanding the structure, function, and regulation of these essential transporters. These studies raised many new questions related to specific physiological roles of Cu-ATPases in various tissues and complex mechanisms that control the Cu-ATPase function. This review summarizes current data on the structural organization and functional properties of ATP7A and ATP7B as well as their localization and functions in various tissues, and discusses the current models of regulated trafficking of human Cu-ATPases.

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23

OHTA, Yuriko, Noriyuki SHIRAISHI, Yoshihiro SAMBONGI, Masamitsu FUTAI, and Morimitsu NISHIKIMI. "Evidence That Single Missense Mutations in the Atp7a Gene of Two Mouse Models for Menkes' Disease Are Responsible for Impaired Copper Transport." Journal of Clinical Biochemistry and Nutrition 29 (2000): 37–44. http://dx.doi.org/10.3164/jcbn.29.37.

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24

Riggle, Perry J., and Carol A. Kumamoto. "Role of a Candida albicans P1-Type ATPase in Resistance to Copper and Silver Ion Toxicity." Journal of Bacteriology 182, no. 17 (September 1, 2000): 4899–905. http://dx.doi.org/10.1128/jb.182.17.4899-4905.2000.

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ABSTRACT Copper ion homeostasis is complicated in that copper is an essential element needed for a variety of cellular processes but is toxic at excess levels. To identify Candida albicans genes that are involved in resistance to copper ion toxicity, a library containing inserts of C. albicans genomic DNA was used to complement the copper sensitivity phenotype of a Saccharomyces cerevisiae cup1Δ strain that is unable to produce Cup1p, a metallothionein (MT) responsible for high-level copper ion resistance. A P1-type ATPase (CPx type) that is closely related to the human Menkes and Wilson disease proteins was cloned. The gene encoding this pump was termed CRD1 (for copper resistance determinant). A gene encoding a 76-amino-acid MT similar to higher eukaryotic MTs in structure was also cloned, and the gene was termed CRD2. Transcription of the CRD1 gene was found to increase upon growth with increasing copper levels, while the CRD2 mRNA was expressed at a constant level. Strains with the CRD1gene disrupted were extremely sensitive to exogenous copper and failed to grow in medium containing 100 μM CuSO4. Thesecrd1 strains also exhibited increased sensitivity to silver and cadmium, indicating that Crd1p is somewhat promiscuous with respect to metal ion transport. Although strains with the CRD2 gene disrupted showed reduced growth rate with increasing copper concentration, the crd2 mutants eventually attained wild-type levels of growth, demonstrating that CRD2 is less important for resistance to copper ion toxicity. Crd1p is the first example of a eukaryotic copper pump that provides the primary source of cellular copper resistance, and its ability to confer silver resistance may enhance the prevalence of C. albicans as a nosocomial pathogen.

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Niccoli Asabella, Artor, Giuseppe Lucio Cascini, Corinna Altini, Domenico Paparella, Antonio Notaristefano, and Giuseppe Rubini. "The Copper Radioisotopes: A Systematic Review with Special Interest to 64Cu." BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/786463.

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Copper (Cu) is an important trace element in humans; it plays a role as a cofactor for numerous enzymes and other proteins crucial for respiration, iron transport, metabolism, cell growth, and hemostasis. Natural copper comprises two stable isotopes, 63Cu and 65Cu, and 5 principal radioisotopes for molecular imaging applications (60Cu, 61Cu, 62Cu, and 64Cu) and in vivo targeted radiation therapy (64Cu and 67Cu). The two potential ways to produce Cu radioisotopes concern the use of the cyclotron or the reactor. A noncopper target is used to produce noncarrier-added Cu thanks to a chemical separation from the target material using ion exchange chromatography achieving a high amount of radioactivity with the lowest possible amount of nonradioactive isotopes. In recent years, Cu isotopes have been linked to antibodies, proteins, peptides, and nanoparticles for preclinical and clinical research; pathological conditions that influence Cu metabolism such as Menkes syndrome, Wilson disease, inflammation, tumor growth, metastasis, angiogenesis, and drug resistance have been studied. We aim to discuss all Cu radioisotopes application focusing on 64Cu and in particular its form 64CuCl2 that seems to be the most promising for its half-life, radiation emissions, and stability with chelators, allowing several applications in oncological and nononcological fields.

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Donsante, Anthony, Ling Yi, Patricia M. Zerfas, Lauren R. Brinster, Patricia Sullivan, David S. Goldstein, Joseph Prohaska, Jose A. Centeno, Elisabeth Rushing, and Stephen G. Kaler. "ATP7A Gene Addition to the Choroid Plexus Results in Long-term Rescue of the Lethal Copper Transport Defect in a Menkes Disease Mouse Model." Molecular Therapy 19, no. 12 (December 2011): 2114–23. http://dx.doi.org/10.1038/mt.2011.143.

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Gaier, E. D., R. M. Rodriguiz, J. Zhou, M. Ralle, W. C. Wetsel, B. A. Eipper, and R. E. Mains. "In vivo and in vitro analyses of amygdalar function reveal a role for copper." Journal of Neurophysiology 111, no. 10 (May 15, 2014): 1927–39. http://dx.doi.org/10.1152/jn.00631.2013.

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Mice with a single copy of the peptide amidating monooxygenase ( Pam) gene (PAM+/−) are impaired in contextual and cued fear conditioning. These abnormalities coincide with deficient long-term potentiation (LTP) at excitatory thalamic afferent synapses onto pyramidal neurons in the lateral amygdala. Slice recordings from PAM+/− mice identified an increase in GABAergic tone (Gaier ED, Rodriguiz RM, Ma XM, Sivaramakrishnan S, Bousquet-Moore D, Wetsel WC, Eipper BA, Mains RE. J Neurosci 30: 13656–13669, 2010). Biochemical data indicate a tissue-specific deficit in Cu content in the amygdala; amygdalar expression of Atox-1 and Atp7a, essential for transport of Cu into the secretory pathway, is reduced in PAM+/− mice. When PAM+/− mice were fed a diet supplemented with Cu, the impairments in fear conditioning were reversed, and LTP was normalized in amygdala slice recordings. A role for endogenous Cu in amygdalar LTP was established by the inhibitory effect of a brief incubation of wild-type slices with bathocuproine disulfonate, a highly selective, cell-impermeant Cu chelator. Interestingly, bath-applied CuSO4 had no effect on excitatory currents but reversibly potentiated the disynaptic inhibitory current. Bath-applied CuSO4 was sufficient to potentiate wild-type amygdala afferent synapses. The ability of dietary Cu to affect signaling in pathways that govern fear-based behaviors supports an essential physiological role for Cu in amygdalar function at both the synaptic and behavioral levels. This work is relevant to neurological and psychiatric disorders in which disturbed Cu homeostasis could contribute to altered synaptic transmission, including Wilson's, Menkes, Alzheimer's, and prion-related diseases.

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Millichap, J. Gordon. "Menkes Disease: Copper-Histidine Therapy." Pediatric Neurology Briefs 7, no. 11 (November 1, 1993): 84. http://dx.doi.org/10.15844/pedneurbriefs-7-11-5.

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Schaefer, Mark, and Jonathan D. Gitlin. "IV. Wilson’s disease and Menkes disease." American Journal of Physiology-Gastrointestinal and Liver Physiology 276, no. 2 (February 1, 1999): G311—G314. http://dx.doi.org/10.1152/ajpgi.1999.276.2.g311.

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Copper is an essential transition metal that permits the facile transfer of electrons in a series of critical biochemical pathways. Menkes disease and Wilson’s disease are inherited disorders of copper metabolism resulting from the absence or dysfunction of homologous copper-transporting ATPases that reside in the trans-Golgi network of all cells. Despite striking differences in the clinical presentation of these two diseases, the respective ATPases function in precisely the same manner within the cell and the unique clinical features of each disease are entirely the result of the tissue-specific expression of each protein. Elucidation of the basic defect in these rare genetic disorders has provided a valuable heuristic paradigm for understanding the mechanisms of cellular copper homeostasis.

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Sarkar, Bibudhendra, Karen Lingertat-Walsh, and Joe T. R. Clarke. "Copper-histidine therapy for Menkes disease." Journal of Pediatrics 123, no. 5 (November 1993): 828–30. http://dx.doi.org/10.1016/s0022-3476(05)80870-4.

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31

Garnica, Adolfo, Wai Yee Chan, and Owen Rennert. "Copper-histidine treatment of Menkes disease." Journal of Pediatrics 125, no. 2 (August 1994): 336–37. http://dx.doi.org/10.1016/s0022-3476(94)70236-5.

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Horn, Nina, and Pernilla Wittung-Stafshede. "ATP7A-Regulated Enzyme Metalation and Trafficking in the Menkes Disease Puzzle." Biomedicines 9, no. 4 (April 6, 2021): 391. http://dx.doi.org/10.3390/biomedicines9040391.

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Copper is vital for numerous cellular functions affecting all tissues and organ systems in the body. The copper pump, ATP7A is critical for whole-body, cellular, and subcellular copper homeostasis, and dysfunction due to genetic defects results in Menkes disease. ATP7A dysfunction leads to copper deficiency in nervous tissue, liver, and blood but accumulation in other tissues. Site-specific cellular deficiencies of copper lead to loss of function of copper-dependent enzymes in all tissues, and the range of Menkes disease pathologies observed can now be explained in full by lack of specific copper enzymes. New pathways involving copper activated lysosomal and steroid sulfatases link patient symptoms usually related to other inborn errors of metabolism to Menkes disease. Additionally, new roles for lysyl oxidase in activation of molecules necessary for the innate immune system, and novel adapter molecules that play roles in ERGIC trafficking of brain receptors and other proteins, are emerging. We here summarize the current knowledge of the roles of copper enzyme function in Menkes disease, with a focus on ATP7A-mediated enzyme metalation in the secretory pathway. By establishing mechanistic relationships between copper-dependent cellular processes and Menkes disease symptoms in patients will not only increase understanding of copper biology but will also allow for the identification of an expanding range of copper-dependent enzymes and pathways. This will raise awareness of rare patient symptoms, and thus aid in early diagnosis of Menkes disease patients.

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Tümer, Zeynep, Nina Horn, Tønne Tønnesen, John Christodoulou, Joe T. R. Clarke, and Bibudhendra Sarkar. "Early copper-histidine treatment for Menkes disease." Nature Genetics 12, no. 1 (January 1996): 11–13. http://dx.doi.org/10.1038/ng0196-11.

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Menkes, John H. "Menkes disease and Wilson disease: two sides of the same copper coin Part 1: Menkes disease." European Journal of Paediatric Neurology 3, no. 4 (January 1999): 147–58. http://dx.doi.org/10.1016/s1090-3798(99)90048-x.

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35

Kim, B.-E. "A copper treatable Menkes disease mutation associated with defective trafficking of a functional Menkes copper ATPase." Journal of Medical Genetics 40, no. 4 (April 1, 2003): 290–95. http://dx.doi.org/10.1136/jmg.40.4.290.

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36

Sarkar, Bibudhendra. "Early copper histidine therapy in classic menkes disease." Annals of Neurology 41, no. 1 (January 1997): 134. http://dx.doi.org/10.1002/ana.410410125.

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37

Guthrie, Liam M., Shivatheja Soma, Sai Yuan, Andres Silva, Mohammad Zulkifli, Thomas C. Snavely, Hannah Faith Greene, et al. "Elesclomol alleviates Menkes pathology and mortality by escorting Cu to cuproenzymes in mice." Science 368, no. 6491 (May 7, 2020): 620–25. http://dx.doi.org/10.1126/science.aaz8899.

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Loss-of-function mutations in the copper (Cu) transporter ATP7A cause Menkes disease. Menkes is an infantile, fatal, hereditary copper-deficiency disorder that is characterized by progressive neurological injury culminating in death, typically by 3 years of age. Severe copper deficiency leads to multiple pathologies, including impaired energy generation caused by cytochrome c oxidase dysfunction in the mitochondria. Here we report that the small molecule elesclomol escorted copper to the mitochondria and increased cytochrome c oxidase levels in the brain. Through this mechanism, elesclomol prevented detrimental neurodegenerative changes and improved the survival of the mottled-brindled mouse—a murine model of severe Menkes disease. Thus, elesclomol holds promise for the treatment of Menkes and associated disorders of hereditary copper deficiency.

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Rizk, Tamer, Adel Mahmoud, Tahani Jamali, and Salah Al-Mubarak. "Menkes Disease Presenting with Epilepsia Partialis Continua." Case Reports in Neurological Medicine 2014 (2014): 1–5. http://dx.doi.org/10.1155/2014/525784.

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Aim. We aim to describe a female patient with Menkes disease who presented with epilepsia partialis continua.Case Presentation. Seventeen-months-old Saudi infant was presented with repetitive seizures and was diagnosed to have epilepsia partialis continua.Discussion. Menkes disease (OMIM: 309400) is considered a rare, X-linked recessive neurodegenerative disorder resulting from a mutation in the gene coding for the copper transporting ATPase (ATP7A). Affected individuals usually present with kinky hair, skeletal changes, prolonged jaundice, hypothermia, developmental regression, decreased tone, spasticity, weakness, and therapy resistant seizures.Conclusion. Raising awareness of abnormal presentation of this rare disease may help in the control of seizures through subcutaneous copper supplementation.

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Van Den Berg, G. J., and C. J. A. Van Den Hamer. "87 64-COPPER UPTAKE IN FIBROBLASTS IN MENKES' DISEASE." Pediatric Research 20, no. 10 (October 1986): 1048. http://dx.doi.org/10.1203/00006450-198610000-00141.

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40

Sheela, SR, M. Latha, P. Liu, K. Lem, and SG Kaler. "Copper-replacement treatment for symptomatic Menkes disease: ethical considerations." Clinical Genetics 68, no. 3 (August 11, 2005): 278–83. http://dx.doi.org/10.1111/j.1399-0004.2005.00496.x.

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41

George, David H., and Robin E. Casey. "Menkes Disease after Copper Histidine Replacement Therapy: Case Report." Pediatric and Developmental Pathology 4, no. 3 (May 2001): 281–88. http://dx.doi.org/10.1007/s100240010142.

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Menkes disease (MD) is an X-linked recessive disorder of copper metabolism, characterized in its untreated state by progressive disorders of multiple systems, especially the central nervous system (CNS) and connective tissue, and death by 3 years of age. Recently, therapy with copper-histidine has modified the severity of MD and permitted survival into adolescence. Clinical response has been greater for the neurological abnormalities than for the connective tissue abnormalities. In this report, we describe the postmortem pathology of one individual who had received copper-histidine therapy and died at age 10; we believe this to be the first such pathological report. The postmortem examination demonstrated significant pathology of mesenchymal tissues, including skeletal abnormalities, vascular degeneration, and bladder diverticula. The CNS, by contrast, showed minimal pathology. The phenotype was more consistent with occipital horn syndrome, a milder allelic disorder of copper metabolism, than with classic MD. The differential sensitivity of CNS and mesenchymal tissues to copper-histidine therapy may result from heterogeneity in the response of different copper-dependent enzymes.

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42

Bull, Peter C., and Diane W. Cox. "Wilson disease and Menkes disease: new handles on heavy-metal transport." Trends in Genetics 10, no. 7 (July 1994): 246–52. http://dx.doi.org/10.1016/0168-9525(94)90172-4.

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43

Norgate, Melanie, Esther Lee, Adam Southon, Ashley Farlow, Philip Batterham, James Camakaris, and Richard Burke. "Essential Roles in Development and Pigmentation for the Drosophila Copper Transporter DmATP7." Molecular Biology of the Cell 17, no. 1 (January 2006): 475–84. http://dx.doi.org/10.1091/mbc.e05-06-0492.

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Defects in the mammalian Menkes and Wilson copper transporting P-type ATPases cause severe copper homeostasis disease phenotypes in humans. Here, we find that DmATP7, the sole Drosophila orthologue of the Menkes and Wilson genes, is vital for uptake of copper in vivo. Analysis of a DmATP7 loss-of-function allele shows that DmATP7 is essential in embryogenesis, early larval development, and adult pigmentation and is probably required for copper uptake from the diet. These phenotypes are analogous to those caused by mutation in the mouse and human Menkes genes, suggesting that like Menkes, DmATP7 plays at least two roles at the cellular level: delivering copper to cuproenzymes required for pigmentation and neuronal function and removing excess cellular copper via facilitated efflux. DmATP7 displays a dynamic and unexpected expression pattern in the developing embryo, implying novel functions for this copper pump and the lethality observed in DmATP7 mutant flies is the earliest seen for any copper homeostasis gene.

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Ambrosini, L., and J. F. B. Mercer. "Defective Copper-Induced Trafficking and Localization of the Menkes Protein in Patients With Mild and Copper-Treated Classical Menkes Disease." Human Molecular Genetics 8, no. 8 (August 1, 1999): 1547–55. http://dx.doi.org/10.1093/hmg/8.8.1547.

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Dumitriu, Mihaela Cezara, and Robert Mihai Enache. "Menkes disease – a multidisciplinary approach for a proper evolution." Medical Image Database 2, no. 1 (May 23, 2019): 13–14. http://dx.doi.org/10.33695/mid.v2i1.24.

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Menkes disease is a genetic disorder of copper metabolism that is detectable before birth. It is characterized by seizures, mental retardation, stunted growth, failure to thrive, unstable body temperature, and very unusual color and texture of hair.The incidence of Menkes disease is about 1: 300.000 newborns in Europe, mainly involving boys. In this case, we present a 3 year old boy, known with Menkes disease from 4 months old, who was admitted to hospital for recurrent acute upper respiratory tract infections (URI). In 2016 he was hospitalized for craniofacial dysmorphism and marked generalized hypotonia, after a paroxysmal cerebral event with loss of consciousness, capping eyes and generalized hypotonia, lasting about 1 hour, at home. Except for these, clinical examination showed deformed thorax, prominent sternum with wide bases, deformed lower legs. Dermatologic and neurologic examination showed the typical aspect of kinky hair and specific epileptic-wave elements on EEG. Based on all these, but also low levels of copper and ceruloplamin, the patient was diagnosed with Menkes disease. He is treated with Phenobarbital (40 mg/day), Valproic acid (1.5 mg x3/day), Diazepam for convulsions and Metamizole (300 mg). The evolution was favorable, without seizures, but with numerous respiratory infections, treated with antibiotics. In conclusion, this case is distinguished by the fact that Menkes disease, an extremely rare condition, can manifest initially by repeated respiratory infections that require a multidisciplinary approach for an early diagnosis, so the patients could surpass the age of three years, noted in literature as the maximum age of survival.

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Fontaine, Sharon La, Stephen D. Firth, James Camakaris, Anna Englezou, Michael B. Theophilos, Michael J. Petris, Michelle Howie, et al. "Correction of the Copper Transport Defect of Menkes Patient Fibroblasts by Expression of the Menkes and Wilson ATPases." Journal of Biological Chemistry 273, no. 47 (November 20, 1998): 31375–80. http://dx.doi.org/10.1074/jbc.273.47.31375.

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O'Halloran, T., R. Pufahl, C. Singer, D. Huffman, G. Munson, and W. Outten. "Menkes and Wilson disease: Coordination chemistry of copper chaperone domains." Journal of Inorganic Biochemistry 67, no. 1-4 (July 1997): 142. http://dx.doi.org/10.1016/s0162-0134(97)80020-7.

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48

Harris, Edward D. "Menkes' Disease: Perspective and Update on a Fatal Copper Disorder." Nutrition Reviews 51, no. 8 (April 27, 2009): 235–38. http://dx.doi.org/10.1111/j.1753-4887.1993.tb03111.x.

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Türner, Zeynep, and Nina Horn. "Menkes Disease: Recent Advances and New Insights into Copper Metabolism." Annals of Medicine 28, no. 2 (January 1996): 121–29. http://dx.doi.org/10.3109/07853899609092936.

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Kaler, Stephen G. "Menkes disease mutations and response to early copper histidine treatment." Nature Genetics 13, no. 1 (May 1996): 21–22. http://dx.doi.org/10.1038/ng0596-21.

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