7.2.2.9 aorta - 668543 7.2.2.9 ARPE-19 cell - 669011 7.2.2.9 astrocyte - 670415 7.2.2.9 BHY cell - 697073 7.2.2.9 bile canaliculus cellular distribution of ATP7B, stable ATP7B pool localized to the tight junctions that seal the bile canaliculi shown 686925 7.2.2.9 bile duct ATP7B is expressed in bile duct epithelial cells, where it may mediate copper secretion into bile fluid 667210 7.2.2.9 brain - 246908, 246909 7.2.2.9 brain ATP7A expression is most abundant in the early postnatal period, reaching peak levels at P4 in neocortex and cerebellum. In the developing and adult brain, ATP7A levels are greatest in the choroid plexus/ependymal cells of the lateral and third ventricles. ATP7A expression decreases in most neuronal subpopulations from birth to adulthood. ATP7A expression increases in CA2 hippocampal pyramidal and cerebellar Purkinje neurons 670415 7.2.2.9 brain ATP7A is widely expressed throughout the CNS 712175 7.2.2.9 brain expression of ATP7A, not of ATP7B 713537 7.2.2.9 brain intensely detected in neuronal cells of the hippocampal formation, olfactory bulbs, cerebellum, cerebral cortex and nuclei in the brainstem 246911 7.2.2.9 breast expression is greater in lactating tissue than in nonlactating tissue, detected in luminal epithelial cells of the alveoli and ducts but not in myoepithelial cells 246918 7.2.2.9 Caco-2 cell - 710815 7.2.2.9 Caco-2 cell model for the ATP7A trafficking in enterocytes 684720 7.2.2.9 carcinoma cell - 699977 7.2.2.9 cerebellar Purkinje cell - 687481 7.2.2.9 cerebellum ATP7A and ATP7B 712175 7.2.2.9 cerebellum ATP7A expression is most abundant in the early postnatal period, reaching peak levels at P4 in neocortex and cerebellum 670415 7.2.2.9 cerebrovascular endothelial cell - 246919 7.2.2.9 CHO cell copper-resistant CHO cells which overexpress the enzyme 246912 7.2.2.9 CHO-CUR3 cell - 712170 7.2.2.9 CHO-K1 cell - 712170 7.2.2.9 colonic cancer cell ATP7A shown to be expressed in 23.5% of clinical colon cancer specimens but not in the adjacent normal epithelium 685944 7.2.2.9 conidium - -, 712728 7.2.2.9 cytotrophoblast Menkes disease protein, i.e. ATP7A 670523 7.2.2.9 duodenum ATP7A is present on apical domains of duodenal enterocytes in control rats and on brush-border and basolateral membrane domains in iron-deprived rats 669393 7.2.2.9 endothelial cell - 670415 7.2.2.9 enterocyte - 696595 7.2.2.9 enterocyte ATP7A 699977 7.2.2.9 epithelial cell airway, cell type-specific expression of ATP7A and ATP7B in airway epithelial cells 713537 7.2.2.9 fibroblast - 668543, 696595, 710802 7.2.2.9 fibroblast fibroblasts from the female Menkes translocation patient show no detectable expression of the transcript, five additional fibroblast lines from unrelated Menkes patients show alterations in the expression of this gene 246908 7.2.2.9 fibroblast isolated from Menkes disease patients, transfection with ATP7A 685944 7.2.2.9 heart - 246908, 699709 7.2.2.9 HEK-293 cell ATP7A and ATP7B 701335 7.2.2.9 Hep-G2 cell - 668712, 685500, 701335 7.2.2.9 Hep-G2 cell localization of ATP7B in polarized hepatocytes 684720 7.2.2.9 Hep-G2 cell trafficking of ATP7B in Hep-G2 cells is not regulated by cis-diamminedichloroplatinum, DDP, while Huh7 cells show a biphasic response with a sharp 50% decrease in cell survival 698990 7.2.2.9 HEPA 1-6 cell - 718774 7.2.2.9 hepatocellular carcinoma cell the overexpression of ATP7B in hepatocellular carcinoma might be associated with unfavorable clinical outcome in patients treated with cisplantin-based chemotherapy 667210 7.2.2.9 hepatocyte - 699977, 712175 7.2.2.9 hepatocyte ATP7B interaction with p62 is a key component of the copper-induced trafficking pathway that delivers ATP7B to subapical vesicles of hepatocytes for the removal of excess copper into bile 669449 7.2.2.9 hepatocyte ATP7B is observed close to the plasma membrane, both at the sinusoidal and at the biliary pole 668477 7.2.2.9 hepatocyte copper-induced relocalization summarized in 688298 7.2.2.9 hepatocyte primary and cultured 701335 7.2.2.9 hepatocyte primary, ATP7B is highly expressed in hepatocytes 698990 7.2.2.9 hepatoma cell Hep3B 656023 7.2.2.9 hippocampus - 689738, 696595 7.2.2.9 hippocampus primary hippocampal neurons 689738 7.2.2.9 HSC-3 cell - 697073 7.2.2.9 Huh-7 cell - 698990 7.2.2.9 IEC-6 cell - 710815 7.2.2.9 intestinal epithelium - 710815 7.2.2.9 intestine - 710815 7.2.2.9 intestine ATP7A and ATP7B 712175 7.2.2.9 intestine high levels of ATP7A 699977 7.2.2.9 JEG-3 cell - 684963 7.2.2.9 kidney - 246908, 246909, 701335 7.2.2.9 kidney ATP7A and ATP7B 701335 7.2.2.9 kidney ATP7A and ATP7B are co-expressed in proximal and distal epithelial cells 712175 7.2.2.9 kidney basolateral membrane, intracellular vesicles 684373 7.2.2.9 kidney high levels of ATP7B 699977 7.2.2.9 leaf - 688693 7.2.2.9 liver - 246916, 668477, 699709, 712486, 718542 7.2.2.9 liver ATP7A 712175 7.2.2.9 liver ATP7A and ATP7B 701335 7.2.2.9 liver ATPB7 predominantly 695478 7.2.2.9 liver copper excretion into the bile 686925 7.2.2.9 liver high levels of ATP7B 699977 7.2.2.9 liver little or no activity 246908 7.2.2.9 lung - 246908 7.2.2.9 macrophage - 712400 7.2.2.9 mammary epithelium ATP7A expressed in 684927 7.2.2.9 mammary gland - 696595 7.2.2.9 mammary gland ATP7A protein 10fold to 20fold higher in transgenic than in control mice 684927 7.2.2.9 mammary gland transgenic mice 684927 7.2.2.9 microglia - 670415 7.2.2.9 midgut larval stage, copper-inducible 687122 7.2.2.9 ML-DmBG3-c2 cell - 719036 7.2.2.9 additional information all tissues except liver 655952 7.2.2.9 additional information expression levels of ATP7A and other Cu homeostasis proteins are not significantly affected by Cu exposure 699709 7.2.2.9 additional information no ATP7B expression in normal hepatic cells 667210 7.2.2.9 additional information when the copper concentration in the hepatocyte increases, ATP7B relocates to the canalicular compartment and excretes excess copper to the bile, intestinal ATPA7 exports the absorbed copper from the enterocytes into the blood stream to supply the copper for the systemic need in a process that involves trafficking of he transporter towards the basolateral membrane 699977 7.2.2.9 mycelium - -, 713041 7.2.2.9 neocortex ATP7A expression is most abundant in the early postnatal period, reaching peak levels at P4 in neocortex and cerebellum 670415 7.2.2.9 neuron hippocampal, neuronal MNK trafficking may occur independently of its catalytic cycle 696595 7.2.2.9 neuron main neurons of leg, wing margin, labellum, maxillary palps and third antennal segment 687122 7.2.2.9 neuron polarized sorting of the Cu2+ transporter ATP7B to the somatodendritic domain of rat hippocampal neurons is mediated by recognition of dileucine-based signals in the cytosolic domains of the proteins by the sigma1 subunit of the clathrin adaptor AP-1. Under basal Cu2+ conditions, ATP7B is localized to the trans-Golgi network and the plasma membrane of the soma and dendrites but not the axon. Mutation of a dileucine-based signal in ATP7B or overexpression of a dominant-negative sigma1 mutant results in nonpolarized distribution of ATP7B between the somatodendritic and axonal domains. Addition of high Cu2+ concentrations causes loss of trans-Golgi network localization and somatodendritic polarity of ATP7B 734662 7.2.2.9 oligodendrocyte - 670415 7.2.2.9 oocyte heterologous expression into Xenopus laevis 685370 7.2.2.9 optic nerve presence of ATP7A in the axons of postnatal, but not adult, optic nerve 670415 7.2.2.9 oral squamous cell carcinoma cell - 697073 7.2.2.9 pancreas - 246908 7.2.2.9 parotid acinar cell Menkes protein could be involved in copper secretion from acinar cells into saliva 667104 7.2.2.9 pharyngeal muscle - 246915 7.2.2.9 placenta - 246908, 246909, 684963, 696595 7.2.2.9 placenta Menkes disease protein, i.e. ATP7A is present in the syncytiotrophoblast, cytotrophoblast and the fetal vascular endothelial cells. Placental level does not change across pregancy 670523 7.2.2.9 placenta Wilson disease protein is present only in the syncytiotrophoblast 670523 7.2.2.9 RAW-264.7 cell - 712400 7.2.2.9 retina - 669011 7.2.2.9 retinal pigment epithelium - 669011 7.2.2.9 retinal pigment epithelium both Cu-ATPases ATP7A and ATP7B are expressed within retinal pigment epithelium 712175 7.2.2.9 SCHNEIDER-2 cell - 719036 7.2.2.9 seedling - 719895 7.2.2.9 skin fibroblast - 669449 7.2.2.9 skin fibroblast overexpressing ATP7A or ATP7B 667448 7.2.2.9 syncytiotrophoblast - 684963 7.2.2.9 syncytiotrophoblast Menkes disease protein, i.e. ATP7A is present in the syncytiotrophoblast, cytotrophoblast and the fetal vascular endothelial cells 670523 7.2.2.9 syncytiotrophoblast Wilson disease protein is present only in the syncytiotrophoblast 670523 7.2.2.9 tanycyte - 670415 7.2.2.9 trophozoite - 654545 7.2.2.9 vascular endothelial cell - 668543 7.2.2.9 vascular endothelial cell fetal. Menkes disease protein, i.e. ATP7A 670523 7.2.2.9 vascular smooth muscle cell - 668543