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The entire coding region and adjacent splice sites of ATP7B gene were amplified.
Homozygous mutation in ATP7B promoter, which disrupts a MTF1 binding site, was identified in a patient with Wilson disease.
Study reported a patient with Wilson's disease (WD) presenting with a novel deletion mutation (c.532_574del43) and a known missense mutation (c.3517G > A) located in the two different ATP7B alleles.
In our review, we highlight the roles of ATP7A/7B in platinum drug resistance and cancer progression. We also discuss the possible mechanisms of platinum drug resistance mediated by ATP7A/7B and provide novel strategies for overcoming resistance. This review may be helpful for understanding the roles of ATP7A and ATP7B in platinum drug resistance
Study reports the NMR structure of the metal-binding domain 1 (MBD1) of ATP7B. The structure reveals the disruptive mechanism of G85V mutation, one of the very few Singular Wilson disease causing missense mutations in the MBD1-4 region of ATP7B. The protein misfolding will disrupt MBD1-3 interactions, and interfere with proper ATP7B trafficking and activity which, in turn may be followed by protein degradation.
Single-particle analysis yielded a low-resolution 3D model that provides the first insight into an overall architecture of human ATP7B, positions of the main domains, and a dimer interface.
The genotypes of ATP7B gene may be novel and significant biomarkers for predicting the gastrointestinal toxicity of platinum-based chemotherapy in NSCLC patients.
The ATP7B gene codes the ATP7B protein, which is an acronym for: ATPase activity, 7 distinct domain, and B class for second P-type ATPase copper binding pump.
Mutations in the alpha-1-antitrypsin and Wilson's genes may act as cofactors in the pathogenesis of fatty liver diseases.
Compound heterozygous mutations Arg778Leu and a variant in intron4:c.1707 + 5G>A were identified in a case of Wilson's disease with adrenocortical insufficiency. c.1707 + 5G>A variant resulted in exon 4 skipping.
These findings were different from previous studies in Asia. Our research established a suitable strategy for ATP7B gene testing in northern Vietnamese WD patients.
Wilson disease (WD) is an autosomal-recessive disease caused by mutations in the ATP7B gene which encodes a copper-transporting ATPase.
The role of metal-binding domains in ATP7B function and Wilson disease causing point mutations.[review]
for ATP7B mutations, the more severe impact on ATP7B protein was, the younger onset age and lower Cp level presented. The feasibility of presymptomatic DNA diagnosis and predicting clinical manifestation or severity of Wilson disease (WD) would be facilitated with identified mutations and genotype-phenotype correlation precisely revealed in the study.
Among those >800 reported mutations of the ATP7B gene missense/nonsense mutations are very rare. A874V-ATP7B protein mutant showed apparent destabilization and endoplasmic reticulum retention, and lost copper transport activity, thus likely causing Wilson disease phenotype.
Our findings imply that reduced stability and enhanced dynamics of MBD1 or MBD6 is the origin of ATP7B dysfunction in Wilson disease patients with the G85V or G591D mutation.
single nucleotide polymorphisms in ATP7B gene is associated with copper dysmetabolism in Alzheimer's disease.
Mutation in ATP7B gene is associated with copper dysmetabolism in Wilson disease.
We here demonstrate that ATP7B confers multidrug resistance by facilitating nuclear drug efflux and late endosomal drug sequestration.
Data suggest that N-terminal segment of metal-binding domains (MBDs) 1-3 of ATOX1 interact with nucleotide-binding domain of ATP7B, thus physically coupling the domains involved in copper binding and those involved in ATP hydrolysis; interactions with MBDs 1-3 of ATOX1 activate ATP7B ATP hydrolysis. (ATOX1 = copper transport protein ATOX1; ATP7B = Cu-binding P type ATPase ATP7B)
DBH-containing neurons express both ATP7A and ATP7B. The two transporters are located in distinct cellular compartments and oppositely regulate the export of soluble DBH from cultured neuronal cells under resting conditions.
Copper homeostasis in the testes is closely controlled by copper-transporting ATPases ATP7A and ATP7B proteins.
This study showed that knockout of Atp7b led to altered lipid metabolism and liver steatosis in the absence of inflammation.
ATP7B is transported from the trans-Golgi network (TGN) to the bile canaliculus by basolateral sorting and endocytosis, and microtubule-mediated transcytosis through the subapical compartment.
Data indicate that the copper-transporting ATPase gene (Atp7b) knockout mice showed a drastic, time-dependent accumulation of hepatic copper.
The aim of this study was to identify copper disturbances according to various brain compartments and further dissect the causal relationship between copper storage and neuronal damage using Atp7b(-/-) mice.
DKWSLLL sequence is essential for ATP7b sorting at the TGN, transport from the TGN to the PM, endocytosis, and recycling to the TGN and PM.
Ligand-activated nuclear receptors FXR/NR1H4 and GR/NR3C1 and nuclear receptor interacting partners are less abundant in Atp7b(-/-) hepatocyte nuclei.
By performing dynamic PET, authors obtained the first real-time measurements of 64Cu distribution in the organs or tissues of Atp7b -/- mice.
Clusterin and COMMD1 independently regulate degradation of the mammalian copper ATPases ATP7A and ATP7B.
Neuroinflammatory and behavioural changes in the Atp7B mutant mouse model of Wilson's disease.
The Jackson toxic milk mouse as a model for copper loading
Both Atp7a and Atp7b are expressed in glomeruli; however, Atp7b is also seen in the kidney medulla suggesting that glomeruli are responsible for regulating copper levels in the filtrate
In mice in which this enzyme has been knocked out, the is a reduced level of beta-hydroxylase and norepinephrine in the adrenal gland.
Mice homozygous for the recessive txJ mutation examined at 6 months of age exhibited a reduced number of amyloid plaques and diminished plasma Abeta levels. Homozygosity for txJ increased survival and lowered endogenous CNS Abeta.
Distinct functions of ATP7A and ATP7B in the cerebellum and illustrate a tight link between copper homeostasis in Purkinje neuerons and Bergmann glia.
in Atp7b-/- mice elevated copper affects specific cellular targets at the transcription and/or translation levels and has distinct effects on liver metabolic function, prior to appearance of histopathological changes
Both Cu-ATPases (ATP7A and ATP7b) regulate renal copper, with ATP7A playing a major role in exporting copper via basolateral membranes and protecting renal tissue against copper overload.
review of quantitative detection of copper-transporting ATPases in tissues and distinct biochemical characteristics and dissimilar trafficking properties of ATP7A and ATP7B in cells, in which they are co-expressed, indicating distinct specific functions
Studies using polarized PMC42-LA cells that overexpressed mAtp7B protein showed that this transporter facilitates copper efflux from the apical surface of the cells.
A copper-dependent ATPase hydrolysis in a native Golgi-enriched preparation from liver, was characterized.
Using the CRISPR/Cas9 system, the study creates a single amino acid substitute rabbit model for Wilson disease (WD). The defined point mutations in the rabbit ATP7B gene were derived by microinjecting synthesized RNAs with single-strand DNA oligonucleotides donor sequences into zygotes, and the efficiency of homology-directed knock-in of point mutations was enhanced when RNAs were injected into younger zygotes.
This gene is a member of the P-type cation transport ATPase family and encodes a protein with several membrane-spanning domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least 2 putative copper-binding sites. This protein functions as a monomer, exporting copper out of the cells, such as the efflux of hepatic copper into the bile. Alternate transcriptional splice variants, encoding different isoforms with distinct cellular localizations, have been characterized. Mutations in this gene have been associated with Wilson disease (WD).
ATPase, Cu(2+)- transporting, beta polypeptide
, Wilson disease-associated protein
, copper pump 2
, copper-transporting ATPase 2
, Wilson protein
, toxic milk
, wilson disease-associated protein homolog
, ATPase, Cu++ transporting, beta polypeptide (same as Wilson disease)
, PINA gene, promoter
, pineal night-specific ATPase
, ATPase 7B protein
, ATPase, Cu++ transporting, beta polypeptide (Wilson disease)
, Wilson's disease protein
, copper-transporting ATPase
, ATPase, Cu++ transporting, beta polypeptide
, ATPase, Cu(2+)-transporting, beta polypeptide
, copper-transporting ATPase 2-like