The Experts below are selected from a list of 6 Experts worldwide ranked by ideXlab platform
Barbro B. Johansson - One of the best experts on this subject based on the ideXlab platform.
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Secondary thalamic Lesions after ligation of the middle cerebral artery: an ultrastructural study
Acta Neuropathologica, 1995Co-Authors: Claes Nordborg, Barbro B. JohanssonAbstract:Earlier light microscopic, immunocytochemical and morphometric investigations indicate that noxious substances transported with the vasogenic edema from hemispheric infarcts influence the character, timing and extent of the secondary thalamic Lesions. The object of the present study was to analyze the ultrastructure of the secondary damage and the cytolytic Nerve Cell change which ensues in the thalamus within a week after the infarction. Adult spontaneously hypertensive rats (SHR) were studied either 7 days after permanent ligation of the right middle cerebral artery (MCA) (n = 4) or 7 days after a 2-h temporary occlusion of the MCA (n = 4). Light microscopy revealed damage in the ipsilateral thalamic nuclei and the electron microscopic analysis showed that the cytolytic Nerve Cell degeneration was somatodendritic. Central chromatolysis was not observed. Somatodendritic Nerve Cell degeneration, as found in the secondary thalamic Lesions in the present study, has been described in excitotoxic brain damage as well as in chronic, edematous Lesions in stroke-prone spontaneously hypertensive rats. The possibility that the cytolytic thalamic Nerve Cell Lesion is influenced by excitatory, noxious substances spreading with the edema fluid from the infarct has, thus, to be considered.
Claes Nordborg - One of the best experts on this subject based on the ideXlab platform.
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Secondary thalamic Lesions after ligation of the middle cerebral artery: an ultrastructural study
Acta Neuropathologica, 1995Co-Authors: Claes Nordborg, Barbro B. JohanssonAbstract:Earlier light microscopic, immunocytochemical and morphometric investigations indicate that noxious substances transported with the vasogenic edema from hemispheric infarcts influence the character, timing and extent of the secondary thalamic Lesions. The object of the present study was to analyze the ultrastructure of the secondary damage and the cytolytic Nerve Cell change which ensues in the thalamus within a week after the infarction. Adult spontaneously hypertensive rats (SHR) were studied either 7 days after permanent ligation of the right middle cerebral artery (MCA) (n = 4) or 7 days after a 2-h temporary occlusion of the MCA (n = 4). Light microscopy revealed damage in the ipsilateral thalamic nuclei and the electron microscopic analysis showed that the cytolytic Nerve Cell degeneration was somatodendritic. Central chromatolysis was not observed. Somatodendritic Nerve Cell degeneration, as found in the secondary thalamic Lesions in the present study, has been described in excitotoxic brain damage as well as in chronic, edematous Lesions in stroke-prone spontaneously hypertensive rats. The possibility that the cytolytic thalamic Nerve Cell Lesion is influenced by excitatory, noxious substances spreading with the edema fluid from the infarct has, thus, to be considered.
Annica Dahlström - One of the best experts on this subject based on the ideXlab platform.
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Differential localization of α-, β- and γ-synucleins in the rat CNS
Neuroscience, 2002Co-Authors: P Henning Jensen, Annica DahlströmAbstract:Abstract α-Synuclein is a presynaptic protein that normally participates in the homeostasis of synaptic vesicles. Missense mutations in its gene cause the protein to participate actively in the development of heritable forms of Parkinson’s disease. Moreover, its metabolism is perturbed in all cases of Parkinson’s disease where α-synuclein accumulates in a filamentous form in the Lewy body Nerve Cell Lesion. Lewy bodies also develop in other common neurodegenerative disorders, like dementia with Lewy bodies and Lewy body variant of Alzheimer’s disease. In the present study, we have studied the detailed distribution of α-, β- and γ-synuclein in the rat CNS. α-Synuclein was not observed in perikarya, but was distributed with high intensity in Nerve terminals in the caudate and putamen and ventral pallidum, where β-synuclein was much weaker and less densely distributed in the caudate and putamen. γ-Synuclein was not found in the caudate and putamen. α-Synuclein was robustly distributed in the substantia nigra pars reticulata, but was very weak or virtually absent from the perikarya of the neurons in the pars compacta. In contrast, β-synuclein was very weak or absent from the substantia nigra. γ-Synuclein was absent from the terminals of substantia nigra pars reticulata, but sparsely distributed γ-synuclein-containing neurons were detected in the substantia nigra pars compacta. In the brainstem, α-synuclein as well as γ-synuclein were present in the locus coeruleus with high intensity, while β-synuclein was very weak. In addition, α-synuclein was intense in the vagus nucleus, but weak in the oculomotor, facial, hypoglossal, accessory and ambiguous nuclei, where β-synuclein was very intensely present. Furthermore, γ-synuclein was localized in the terminals and in Cell bodies of the Edinger–Westphal nucleus, the red nucleus, locus coeruleus, and most cranial Nerve-related nuclei. In the spinal cord, α- and γ-synucleins were intensely present in laminae I and II and in the preganglionic sympathetic nuclei, whereas β-synuclein was very weak. These results indicate that α-synuclein is abundant in central catecholaminergic regions. β-Synuclein is more localized in the somatic cholinergic components, while it is particularly weak or absent from catecholaminergic neurons. γ-Synuclein appears to be present in both cholinergic and catecholaminergic regions, but very weak in the forebrain.
P Henning Jensen - One of the best experts on this subject based on the ideXlab platform.
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Differential localization of α-, β- and γ-synucleins in the rat CNS
Neuroscience, 2002Co-Authors: P Henning Jensen, Annica DahlströmAbstract:Abstract α-Synuclein is a presynaptic protein that normally participates in the homeostasis of synaptic vesicles. Missense mutations in its gene cause the protein to participate actively in the development of heritable forms of Parkinson’s disease. Moreover, its metabolism is perturbed in all cases of Parkinson’s disease where α-synuclein accumulates in a filamentous form in the Lewy body Nerve Cell Lesion. Lewy bodies also develop in other common neurodegenerative disorders, like dementia with Lewy bodies and Lewy body variant of Alzheimer’s disease. In the present study, we have studied the detailed distribution of α-, β- and γ-synuclein in the rat CNS. α-Synuclein was not observed in perikarya, but was distributed with high intensity in Nerve terminals in the caudate and putamen and ventral pallidum, where β-synuclein was much weaker and less densely distributed in the caudate and putamen. γ-Synuclein was not found in the caudate and putamen. α-Synuclein was robustly distributed in the substantia nigra pars reticulata, but was very weak or virtually absent from the perikarya of the neurons in the pars compacta. In contrast, β-synuclein was very weak or absent from the substantia nigra. γ-Synuclein was absent from the terminals of substantia nigra pars reticulata, but sparsely distributed γ-synuclein-containing neurons were detected in the substantia nigra pars compacta. In the brainstem, α-synuclein as well as γ-synuclein were present in the locus coeruleus with high intensity, while β-synuclein was very weak. In addition, α-synuclein was intense in the vagus nucleus, but weak in the oculomotor, facial, hypoglossal, accessory and ambiguous nuclei, where β-synuclein was very intensely present. Furthermore, γ-synuclein was localized in the terminals and in Cell bodies of the Edinger–Westphal nucleus, the red nucleus, locus coeruleus, and most cranial Nerve-related nuclei. In the spinal cord, α- and γ-synucleins were intensely present in laminae I and II and in the preganglionic sympathetic nuclei, whereas β-synuclein was very weak. These results indicate that α-synuclein is abundant in central catecholaminergic regions. β-Synuclein is more localized in the somatic cholinergic components, while it is particularly weak or absent from catecholaminergic neurons. γ-Synuclein appears to be present in both cholinergic and catecholaminergic regions, but very weak in the forebrain.