The Experts below are selected from a list of 119646 Experts worldwide ranked by ideXlab platform
Shunsaku Hirai - One of the best experts on this subject based on the ideXlab platform.
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localization of alzheimer amyloid beta Protein Precursor and its relation to senile plaque amyloid
Gerontology, 1994Co-Authors: Haruyasu Yamaguchi, Takeshi Kawarabayashi, Tsuneo Yamazaki, Xaoyan Sun, Yasujirou Sakai, Shunsaku HiraiAbstract:The authors examined the ultrastructural localization of amyloid β Protein Precursor (APP) in normal human brains immu-nohistochemically using 3 kinds of APP antisera. The patterns of immunoreaction d
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Amyloid β Protein Precursor accumulates in swollen neurites throughout rat brain with aging
Neuroscience letters, 1993Co-Authors: Takeshi Kawarabayashi, Haruyasu Yamaguchi, Mikio Shoji, Yasuo Harigaya, Makoto Tanaka, Koji Ishiguro, Shunsaku HiraiAbstract:Abstract We immunocytochemically studied the expression of amyloid β Protein Precursor (APP) in the brains of normal aged rats, and found APP accumulation in swollen neurites, most of which were axons. These swollen neurites appeared throughout the central nervous system of aged rats; most of them were negative for neurofilament, ubiquitin, and tau. Such widely distributed APP accumulation in swollen neurites may reflect impaired fast axonal transport due to aging. APP immunostaining may be a good method to detect widely distributed age-related changes.
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Ultrastructural localization of amyloid β/A4 Protein Precursor in the normal rat brain
Virchows Archiv. B Cell pathology including molecular pathology, 1993Co-Authors: Tsuneo Yamazaki, Takeshi Kawarabayashi, Haruyasu Yamaguchi, Shunsaku HiraiAbstract:The ultrastructural localization of amyloidβ/ 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.
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ultrastructural localization of alzheimer amyloid β a4 Protein Precursor in the cytoplasm of neurons and senile plaque associated astrocytes
Acta Neuropathologica, 1992Co-Authors: Haruyasu Yamaguchi, Mikio Shoji, Tsuneo Yamazaki, Koji Ishiguro, Y Nakazato, Shunsaku HiraiAbstract:The ultrastructural localization of amyloid β/A4 Protein Precursor (APP) in the brains of control and Alzheimer's disease patients was examined immunohistochemically using antisera against the N and C termini of APP. In both control and Alzheimer brains, immunoreaction for APP was seen in the cytoplasm of most neurons, on plasma membranes, outer membrane of mitochondria, granular substance and neurofilaments. Cell bodies and foot processes of astrocytes, containing glial filaments, were also labeled. In primitive and classic type senile plaques, APP immunoreaction products were localized in the astroglial processes that surrounded the amyloid mass of the senile plaques. Swollen degenerating neurites in the senile plaques were also labeled. Amyloid fibrils were negative with APP antisera.
Haruyasu Yamaguchi - One of the best experts on this subject based on the ideXlab platform.
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localization of alzheimer amyloid beta Protein Precursor and its relation to senile plaque amyloid
Gerontology, 1994Co-Authors: Haruyasu Yamaguchi, Takeshi Kawarabayashi, Tsuneo Yamazaki, Xaoyan Sun, Yasujirou Sakai, Shunsaku HiraiAbstract:The authors examined the ultrastructural localization of amyloid β Protein Precursor (APP) in normal human brains immu-nohistochemically using 3 kinds of APP antisera. The patterns of immunoreaction d
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Amyloid β Protein Precursor accumulates in swollen neurites throughout rat brain with aging
Neuroscience letters, 1993Co-Authors: Takeshi Kawarabayashi, Haruyasu Yamaguchi, Mikio Shoji, Yasuo Harigaya, Makoto Tanaka, Koji Ishiguro, Shunsaku HiraiAbstract:Abstract We immunocytochemically studied the expression of amyloid β Protein Precursor (APP) in the brains of normal aged rats, and found APP accumulation in swollen neurites, most of which were axons. These swollen neurites appeared throughout the central nervous system of aged rats; most of them were negative for neurofilament, ubiquitin, and tau. Such widely distributed APP accumulation in swollen neurites may reflect impaired fast axonal transport due to aging. APP immunostaining may be a good method to detect widely distributed age-related changes.
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Ultrastructural localization of amyloid β/A4 Protein Precursor in the normal rat brain
Virchows Archiv. B Cell pathology including molecular pathology, 1993Co-Authors: Tsuneo Yamazaki, Takeshi Kawarabayashi, Haruyasu Yamaguchi, Shunsaku HiraiAbstract:The ultrastructural localization of amyloidβ/ 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.
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ultrastructural localization of alzheimer amyloid β a4 Protein Precursor in the cytoplasm of neurons and senile plaque associated astrocytes
Acta Neuropathologica, 1992Co-Authors: Haruyasu Yamaguchi, Mikio Shoji, Tsuneo Yamazaki, Koji Ishiguro, Y Nakazato, Shunsaku HiraiAbstract:The ultrastructural localization of amyloid β/A4 Protein Precursor (APP) in the brains of control and Alzheimer's disease patients was examined immunohistochemically using antisera against the N and C termini of APP. In both control and Alzheimer brains, immunoreaction for APP was seen in the cytoplasm of most neurons, on plasma membranes, outer membrane of mitochondria, granular substance and neurofilaments. Cell bodies and foot processes of astrocytes, containing glial filaments, were also labeled. In primitive and classic type senile plaques, APP immunoreaction products were localized in the astroglial processes that surrounded the amyloid mass of the senile plaques. Swollen degenerating neurites in the senile plaques were also labeled. Amyloid fibrils were negative with APP antisera.
Jean-noël Octave - One of the best experts on this subject based on the ideXlab platform.
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Alternative polyadenylation of the amyloid Protein Precursor mRNA regulates translation.
The EMBO journal, 1992Co-Authors: F. De Sauvage, Véronique Kruys, Olivier Marinx, Georges Huez, Jean-noël OctaveAbstract:The sequence of several cDNAs encoding the amyloid Protein Precursor showed that two polyadenylation sites of the mRNA are utilized; RNA blot analysis with different riboprobes indicated that this explains the difference between the two major 3.2 and 3.4 kb mRNAs found in the human brain. These two mRNAs, which contain the whole sequence of the natural molecules, were synthesized by in vitro transcription and translated in Xenopus oocytes. The long mRNA using the second polyadenylation site produced more Protein than the short mRNA. The sequence contained within the two polyadenylation sites used in the 3' untranslated region of the amyloid Protein Precursor mRNA was also able to increase the production of the chicken lysozyme or the chloramphenicol acetyl transferase, as demonstrated by in vivo translation of different chimeric mRNAs obtained by in vitro transcription. This difference in Protein production was also observed when chimeric cDNA constructs were transfected into Chinese hamster ovary cells. Since long mRNAs are not more stable than short mRNAs, the sequence contained within the two polyadenylation sites of the amyloid Protein Precursor mRNA increases the translation.
F. De Sauvage - One of the best experts on this subject based on the ideXlab platform.
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Alternative polyadenylation of the amyloid Protein Precursor mRNA regulates translation.
The EMBO journal, 1992Co-Authors: F. De Sauvage, Véronique Kruys, Olivier Marinx, Georges Huez, Jean-noël OctaveAbstract:The sequence of several cDNAs encoding the amyloid Protein Precursor showed that two polyadenylation sites of the mRNA are utilized; RNA blot analysis with different riboprobes indicated that this explains the difference between the two major 3.2 and 3.4 kb mRNAs found in the human brain. These two mRNAs, which contain the whole sequence of the natural molecules, were synthesized by in vitro transcription and translated in Xenopus oocytes. The long mRNA using the second polyadenylation site produced more Protein than the short mRNA. The sequence contained within the two polyadenylation sites used in the 3' untranslated region of the amyloid Protein Precursor mRNA was also able to increase the production of the chicken lysozyme or the chloramphenicol acetyl transferase, as demonstrated by in vivo translation of different chimeric mRNAs obtained by in vitro transcription. This difference in Protein production was also observed when chimeric cDNA constructs were transfected into Chinese hamster ovary cells. Since long mRNAs are not more stable than short mRNAs, the sequence contained within the two polyadenylation sites of the amyloid Protein Precursor mRNA increases the translation.
J Kimura - One of the best experts on this subject based on the ideXlab platform.
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Ultrastructural localization of amyloid Protein Precursor in the normal and postischemic gerbil brain.
Brain Research, 1995Co-Authors: H Tomimoto, I Akiguchi, H Wakita, S Nakamura, J KimuraAbstract:Intracellular localization of amyloid Protein Precursor (APP) in the normal and postischemic gerbil brain was examined by immunoelectron microscopy. In the normal brain, APP immunoreactivity was localized to the multivesicular body, the nuclear membrane, Golgi apparatus and rough endoplasmic reticulum. After ischemia for 5 min and reperfusion for 24 h, some neurons became intensely immunoreactive for APP in the subiculum and CA3 region of the hippocampus and layers III and V/VI of the cerebral cortex. No intense labeling occurred in glial cells. Intensely labeled neurons were characterized by eccentric nuclei and accumulation of cellular organelles in the center of the neuronal perikarya, as well as a strongly immunoreactive nuclear membrane and cisternal structures, which were presumed to be dispersed Golgi apparatus and/or fragmented rough ER. APP immunoreactivity in the multivesicular body suggests re-internalization of APP and its degradation in the endosomal-lysosomal pathway. The ultrastructural features of neurons with intense APP immunoreactivity suggested mild neuronal damage, similar to those found in central chromatolysis. This indicates that accumulation of APP in these neurons is caused by disturbance of axonal transport, although the information does not allow us to exclude the possibility of an increase in APP production.
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Regional accumulation of amyloid Protein Precursor in the gerbil brain following transient cerebral ischemia
Neuroscience letters, 1992Co-Authors: H Wakita, H Tomimoto, I Akiguchi, S Nakamura, Katsunori Ohnishi, J KimuraAbstract:Alterations of beta/A4 amyloid Protein Precursor (APP) were investigated immunohistochemically in the gerbil brain after transient global ischemia and subsequent reperfusion. Marked accumulation of this Protein peaking at 24 h occurred in the neurons of the CA3 and paramedian region of the hippocampus as well as layers III, V and VI of the cerebral cortex. On the contrary, the accumulation was not observed in the neurons of the CA1 region. These results indicate that distribution of APP is altered depending on tissue viabilities after cerebral ischemia.
