Coincident Distribution of ZnT3 and Aβ in the Cerebral Vessels and Choroid Plexus of APP/PS1 Transgenic Mouse
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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.Keywords:
Plexus
Pathogenesis
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Glucuronidase
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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.
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Amyloid (mycology)
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Human brain
Insulin-degrading enzyme
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Amyloid deposition in the cerebral vessels is the hallmark of cerebral amyloid angiopathy (CAA). In order to establish which type of cell produces amyloid, we performed Northern blot analysis and in situ hybridization studies on human meningeal arteries. Northern blotting showed that amyloid precursor protein (APP) mRNA was expressed not only in the cerebral cortex, but also in the meninges. An antisense RNA probe that hybridizes with APP transcripts was used for in situ hybridization. This analytic modality revealed APP messages in the tunica media of the meningeal arteries and arterioles. The presence of smooth muscle cells in these vessels was verified immunohistochemically on consecutive serial sections. These observations indicate that APP is produced by vascular smooth muscle cells.
Northern blot
Amyloid (mycology)
Meninges
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We studied the immunocytochemical distribution of amyloid β protein precursor (APP) in the nervous systems of the mouse and the rat, and changes with aging and brain damage induced by intraventricular injection of kainic acid in the rat brains. We used three different antisera against synthetic peptides of APP and one monoclonal antibody against APP. On Western blot analysis, both antisera against carboxyl-and amino-terminal regions of APP recognized the same 106-122 KDa proteins from mouse brain. Immunocytochemically, APP immunoreactivity was located in all types of neurons and some glial cells in both the central and peripheral nervous systems. In the brains of normal aged rats, APP accumulated in swollen neurites, most of which were axons. These swollen neurites appeared throughout the central nervous system. In the rat brains injected with kainic acid, APP positive dystrophic neurites appeared around the track of the cannula after 3 h, neurons near the lesion showed increased APP immunoreactivity after 6 h, and reactive astrocytes expressed APP with Kunitz-type protease inhibitor domain in the lesion and ipsilateral hippocampus after 3 days. APP was expressed by neurons and glial cells throughout nervous systems, and these distributions changed with aging and brain damage.
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Immunostaining
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Ependymal Cell
Subependymal zone
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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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The ultrastructural localization of amyloid beta/A4 protein precursor (APP) was studied immunohistochemically in normal rat brains using antibodies against different portions of APP. In cerebral cortical neurons and Purkinje cells. APP reaction products were located in the cytoplasm and on cell surface membranes. Some Golgi apparatuses and rough endoplasmic reticulum also showed APP immunoreactivity on their membranes and some vesicles near the trans face of the Golgi apparatuses were stained. In the neuropil of the cerebral cortex and the cerebellar molecular layer, many cell processes, which surrounded synapses and were considered to be astrocytic, were APP-positive. Foot processes around capillaries and subpial astrocytic processes were also immuno-positive. At the ultrastructural level, APP-positive astrocytic processes were identified.
Neuropil
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