The ubiquitously expressed MURR1 protein is absent in canine copper toxicosis

Klomp, Adriana E.; Sluis, Bart van de; Klomp, Leo W. J.; Wijmenga, Cisca

doi:10.1016/s0168-8278(03)00380-5

Cited by 133 publications

(149 citation statements)

References 23 publications

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“…COMMD1 was localized in cytoplasmic vesicular compartments that were particularly profound in the perinuclear region ( Figure 1D). The observed localization of both ATP7B and COMMD1 was consistent with previous reports 9,11 . Overlay of the images ( Figure 1E) revealed that ATP7B and COMMD1 localization partially overlaps, supporting an endogenous interaction between these proteins.…”

Section: Commd1 and Atp7b Are Localized In Overlapping Regions In Heksupporting

confidence: 92%

“…Recently, COMMD1 was implicated as a novel regulator of hepatic copper excretion as a deficiency of this protein causes copper toxicosis in Bedlington terriers 10,11 , a canine disorder that shares many pathophysiological features with WD 12 . Subsequent identification of COMMD1 as an interacting partner of ATP7B further supports the role of COMMD1 in copper homeostasis 13 , and suggests that these two proteins cooperate to facilitate excretion of copper from the hepatocyte into the bile canaliculus.…”

Section: Introductionmentioning

confidence: 99%

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Distinct Wilson’s Disease Mutations in ATP7B Are Associated With Enhanced Binding to COMMD1 and Reduced Stability of ATP7B

et al. 2007

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Background/Aims-Wilson disease is characterized by hepatic copper overload and caused by mutations in the gene encoding the copper transporting P-type ATPase ATP7B. ATP7B interacts with COMMD1, a protein that is deleted in Bedlington terriers with hereditary copper toxicosis. Here we characterized the implications of the interaction between COMMD1 and ATP7B in relation to the pathogenesis of Wilson disease.

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Section: Commd1 and Atp7b Are Localized In Overlapping Regions In Heksupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Distinct Wilson’s Disease Mutations in ATP7B Are Associated With Enhanced Binding to COMMD1 and Reduced Stability of ATP7B

et al. 2007

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“…In the absence of effective ATP7B, Cu accumulates, particularly in the liver, causing cirrhosis and reduced organ function, leading to an early death in those with this genetic trait (Wilson disease). The identity and role of all the participants needed to transport excess copper to the bile are not yet understood; and other gene products must also be involved, including MURR1/COMMD1 (Burstein et al 2005;Klomp et al 2003), a multifunctional protein defective in the Bedlington terrier, a lack of which also results in liver copper accumulation and toxicity. In rats and humans, however, the ability to excrete excess copper via the bile is well developed and largely responsible for maintenance of whole body copper homeostasis (Linder 2001).…”

Section: Introductionmentioning

confidence: 99%

Copper binding components of blood plasma and organs, and their responses to influx of large doses of 65Cu, in the mouse

et al. 2008

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To establish for the first time how mice might differ from rats and humans in terms of copper transport, excretion, and copper binding proteins, plasma and organ cytosols from adult female C57CL6 mice were fractionated and analyzed by directly coupled size exclusion HPLC-ICP-MS, before and after i.p. injection of large doses of 65 Cu. Plasma from untreated mice had different proportions of Cu associated with transcuprein/macroglobulin, ceruloplasmin and albumin than in humans and rats, and two previously undetected copper peaks (Mr 700k and 15k) were observed. Cytosols had Cu peaks seen previously in rat liver (Mr >1000k, 45k and 11k) plus one of 110kDa. 65 Cu (141 μg) administered over 14h, initially loaded plasma albumin and mainly entered liver and kidney (especially 28kDa and 11kDa components). Components of other organs were less, but still significantly enriched. 63 Cu/ 65 Cu ratios returned almost to normal by 14d, indicating a robust system for excreting excess copper. We conclude that there are significant differences but also strong similarities in copper metabolism between mice, rats and humans; that the liver is able to buffer enormous changes in copper status; and that a large number of mammalian copper proteins remain to be identified.

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“…COMMD1 is a 188-amino acid soluble protein that is expressed in most tissues, with the highest expression in the liver (33). COMMD1 is localized throughout the cytoplasm, in the nucleus, endosomes, and lysosomal compartments (34). The COMMD1 gene was found to be deleted in Bedlington terrier dogs that exhibit canine copper toxicosis, a chronic liver copper overload disease that resembles WD (33).…”

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confidence: 99%

Clusterin and COMMD1 Independently Regulate Degradation of the Mammalian Copper ATPases ATP7A and ATP7B

Materia

Cater

Klomp³

et al. 2012

Journal of Biological Chemistry

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Background: Clusterin and COMMD1 interact to down-regulate copper transporters ATP7A and ATP7B. Results: Clusterin and COMMD1 act independently and under different conditions to target ATP7B degradation via different pathways. Conclusion: Clusterin and COMMD1 regulate the quality control of ATP7A/ATP7B and directly impact copper homeostasis. Significance: Clusterin and COMMD1 allelic variations may influence the clinical expression of Menkes and Wilson diseases.

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The ubiquitously expressed MURR1 protein is absent in canine copper toxicosis

Cited by 133 publications

References 23 publications

Distinct Wilson’s Disease Mutations in ATP7B Are Associated With Enhanced Binding to COMMD1 and Reduced Stability of ATP7B

Distinct Wilson’s Disease Mutations in ATP7B Are Associated With Enhanced Binding to COMMD1 and Reduced Stability of ATP7B

Copper binding components of blood plasma and organs, and their responses to influx of large doses of 65Cu, in the mouse

Clusterin and COMMD1 Independently Regulate Degradation of the Mammalian Copper ATPases ATP7A and ATP7B

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