Wilson Disease
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What is Wilson disease?
Wilson disease is an inherited disorder in which excessive amounts of copper accumulate in the body, particularly in the liver, brain, and eyes. Symptoms of Wilson disease usually appear between the ages of 6 and 40, but most often begin during the teenage years. In children, liver disease is the most common feature. Signs and symptoms of liver disease include yellowing of the skin or the whites of the eye (jaundice), fatigue, loss of appetite, and abdominal swelling. Psychiatric and nervous system problems are common in young adults with Wilson disease. Signs and symptoms can include clumsiness, trembling, difficulty walking, speech problems, deteriorating school work, depression, anxiety, and mood swings. In many individuals with Wilson disease, copper deposits form a green-to-brownish ring, called the Kayser-Fleischer ring, around the cornea (the front surface of the eye).
How common is Wilson disease?
Wilson disease is a rare disorder that affects approximately 1 in 30,000 individuals.
What genes are related to Wilson disease?
Mutations in the ATP7B gene cause Wilson disease.
The ATP7B gene makes a protein important for copper transport and the elimination of excess copper from the body. The mutated gene prevents the transport protein from functioning properly, allowing copper to accumulate in the liver, brain, and other tissues.
How do people inherit Wilson disease?
This condition is inherited in an autosomal recessive pattern, which means two copies of the gene in each cell are altered. Most often, the parents of an individual with an autosomal recessive disorder each carry one copy of the altered gene but do not show signs and symptoms of the disorder.
Source: National Institutes of Health
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Investigators at University of Florence target hepatolenticular degeneration
2009 JUN 1 - (NewsRx.com) -- "ATP7B is a human P-1B-type ATPase that has a crucial role in maintaining copper(I) homeostasis. Mutations in the corresponding gene are the cause of Wilson disease," scientists writing in the Journal of Biological Chemistry report. "Among its various distinguishing features is a long (similar to 630 amino acids) N-terminal cytosolic tail containing six domains that are individually folded and capable of binding one copper(I) ion each. We expressed the entire tail as a single construct in Escherichia coli and investigated its interaction with its copper chaperone (i.e. HAH1) by solution NMR spectroscopy. We observed that all six of the metal-binding domains were metallated by Cu(I)-HAH1, with the first, the second, and the fourth domains forming an adduct with it. This behavior is different from that of the highly similar human ATPase ATP7A, in which only two domains form such an adduct," wrote L. Banci and colleagues, University of Florence. The researchers concluded: "The distinct behaviors of the different domains were analyzed in terms of the energetics of Cu(I) transfer, hinting at a specific role of the interaction with copper(I)-HAH1 in the overall functional process." Banci and colleagues published their study in the Journal of Biological Chemistry (An NMR Study of the Interaction of the N-terminal Cytoplasmic Tail of the Wilson Disease Protein with Copper(I)-HAH1. Journal of Biological Chemistry, 2009;284(14):9354-9360). Additional information can be obtained by contacting I. Bertini, University of Florence, Magnet Resonance Center, Via L Sacconi 6, I-50019 Sesto Fiorentino, Italy. The publisher of the Journal of Biological Chemistry can be contacted at: American Society Biochemistry Molecular Biology Inc., 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. Keywords: Italy, Sesto Fiorentino, ATPase, Amino Acids, Biological Chemistry, Copper, Drugs, Enzyme Research, Escherichia coli, Hepatolenticular Degeneration, Pharmaceuticals, Therapy, Treatment, University of Florence. This article was prepared by Biotech Business Week editors from staff and other reports. Copyright 2009, Biotech Business Week via NewsRx.com.
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