Ultrastructural Localization of Zinc Transporter 3 and Zinc Ions In Mouse Choroid Plexus
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The cellular localization of zinc transporter 7 protein in the mouse choroid plexus was examined in this study. Zinc transporter 7 immunoreactive cells were detected in the third, lateral, and fourth ventricles of CD-1 mouse brain. Distinct zinc transporter 7 immunoreactivity was concentrated in the perinuclear regions of the positive cells. The results from zinc autometallography showed that zinc-positive grains were also predominantly located in the perinuclear areas. Ultrastructural localization showed that zinc transporter 7 immunostaining was predominantly present in the membrane and cisternae of the cis-Golgi networks and some vesicle compartments. The results support the notion that zinc transporter 7 may participate in the transport of the cytoplasmic zinc into the Golgi apparatus, and may be involved in local packaging of zinc-binding proteins in the mouse choroid plexus.
Immunostaining
Transport protein
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Superior cervical ganglion
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The present work addresses the cellular and subcellular localization of the zinc transporter 7 (ZNT7, SLC30a7) protein and the distribution of zinc ions (Zn2+) in the mouse spinal cord. Our results indicated that the ZNT7 immunoreactive neurons were widely distributed in the Rexed's laminae of the gray matter in all spinal segments examined. The ependyma cells of the central canal and glia cells in the white matter were also shown ZNT7-positive. The ZNT7 immunoreactivity was mainly detected in the perinuclear regions of ZNT7-positive cells in the spinal gray matter. For ependyma cells, the immunoreactivity of ZNT7 was detected in the cytoplasm near the lumina of the central canal. Ultrastructural localization showed that ZNT7 was predominately present in the membrane of the Golgi stacks. The double immunofluorescence studies confirmed this result. Other intracellular organelles including the endoplasmic reticulum, mitochondria and lysosomes were devoid of ZNT7-immunostaining. The chelatable Zn2+ ions in the spinal cord were found predominantly in the terminals of the neuron rather than the cell body in the gray matter. However, overlapping distribution of chelatable Zn2+ ions and ZNT7 was found in the ependyma cells. The present study supports the notion that ZNT7 may function to supply zinc ions to the newly synthesized metalloproteins in the secretory pathway of the spinal neuron and the ependyma cell.
Ependyma
Immunostaining
Ependymal Cell
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Inner plexiform layer
Inner nuclear layer
Outer plexiform layer
Outer nuclear layer
Ganglion cell layer
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The cellular distribution of membrane proteins in the choroid plexus (CP) is known to differ from other transporting epithelia. The Na,K‐ATPase is atypically located in the luminal membrane and AQP1 is located in both membranes. Genetic deletion of slc4a10 , which encodes the key basolateral Na + loader Ncbe, is known to decrease the abundance of AQP1 and Na, K ATPase and cause a redistribution of ezrin that anchors certain membrane proteins to the cytoskeleton. The aim of the present study was to determine the distribution of known anchoring proteins and cytoskeletal components in CP of normal and NCBE knockout mice by immunohistochemical analysis. A known binding partner of AQP1, β‐catenin, was located only near the basolateral membrane and was less abundant in the NCBE knockout mouse. Ankyrin 3, a known Na,K ATPase anchor in CP was localized near the luminal membrane, but was less abundant in the NCBE knockout mouse. Spectrin cytoskeleton was localized close to the luminal membrane and is known to bind to Ankyrin 3. In the NCBE knockout mouse, spectrin labelling was observed in both membrane domains, however, but predominantly basolaterally. In conclusion, AQP1 in the luminal membrane of CP is not anchored to β‐catenin. Furthermore, the removal of the key Na + loader, NCBE, causes not only a decrease in abundance of the Na, K ATPase binding partner Ankyrin 3, but also a redistribution of the spectrin‐cytoskeleton.
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Epithelial polarity
Knockout mouse
Apical membrane
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Objective To investigate the localization of zinc transporter 7(ZnT7) protein and free zinc ions in ependyma cells in mouse spinal cord and choroid plexus cells in mouse brain.Methods Zinc selenide autometallography(AMG) was used to detect free zinc ions in mouse ependyma and choroid plexus 1.5 hours after sodium selenite treatment;SABC immunohistochemistry was used to detect the location of ZnT7 protein in ependyma and choroid epithelium.Results One and half hours after selenite intraperitoneal injection,almost all ependyma and choroid plexus cells showed AMG positive reactivity.ZnT7-immunoreactive cells were observed in almost all ependyma cells and choroid plexus cells,and the distribution of the immunoreactivity was similar to the AMG staining.Conclusion The abundant distribution of both ZnT7 protein and free zinc ions in mouse ependyma and choroid plexus cells suggests that zinc may play a important role in ependyma and choroid plexus.
Ependyma
Ependymal Cell
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Ependymal Cell
GLUT2
Ependyma
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Object To investigate the localizations of zinc transporter 3(ZnT3) andβ-amyloid protein(Aβ)in the cerebral vessels and choroid plexus of APP/PS1 transgenic mouse and to explore the possible role of ZnT3 in AD pathogenesis. Methods Immunofluorescence and confocal laser scanning microscopy were used to analyze the coincident distribution of ZnT3 and Aβ in the cerebral vessels and choroid plexus of APP/PS1 transgenic mouse. Results In the APP/PS1 transgenic mouse, the epithelial cells of choroid plexus of the lateral, third, and fourth ventricles presented both Aβ and ZnT3 positive immunoreactivity in the cytoplasm, but absent in the nucleus. ZnT3 immunoreactivity was also observed in almost all the Aβ-positive wall of blood vessels. Conclusion The coincident distributions of ZnT3 and Aβ immunoreactivity in the cerebral vessels and choroid plexus suggest that ZnT3 may be involved in the deposition of Aβ in the cerebral vessels and choroid plexus.
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Pathogenesis
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