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Neuropathological Lesions (neuropathological + lesion)
Selected AbstractsMotor neuron disease group accompanied by inclusions of unidentified protein signaled by ubiquitinNEUROPATHOLOGY, Issue 2 2004Kenji Ikeda Peculiar tau-negative, ubiquitin-positive inclusions appear in dementia with ALS (ALS-D), the majority of lobar atrophy (Pick's disease) without Pick body and a small portion of ALS. Another common neuropathological lesion in these diseases is the motor neuron involvement with the degenerative processes. The lower motor neuron is predominantly involved in ALS and ALS-D while the upper motor neuron is predominantly involved, but in varying degrees in a considerable number of patients with lobar atrophy that lack Pick bodies. There are, however, some points that have yet to be elucidated. The boundary between these diseases is not always clear and a significant number of cases are considered to be the transitional form. Lobar atrophy without Pick body seems to be a heterogeneous disease group. The nature of ubiquitin inclusions also needs to be clarified. Nevertheless, we postulate that these diseases are grouped with the concept of motor neuron disease-inclusion dementia. [source] Oxidative stress increases levels of endogenous amyloid-, peptides secreted from primary chick brain neuronsAGING CELL, Issue 5 2008Claire Goldsbury Summary Oxidative damage is associated with Alzheimer's disease and mild cognitive impairment, but its relationship to the development of neuropathological lesions involving accumulation of amyloid-, (A,) peptides and hyperphosphorylated tau protein remains poorly understood. We show that inducing oxidative stress in primary chick brain neurons by exposure to sublethal doses of H2O2 increases levels of total secreted endogenous A, by 2.4-fold after 20 h. This occurs in the absence of changes to intracellular amyloid precursor protein or tau protein levels, while heat-shock protein 90 is elevated 2.5-fold. These results are consistent with the hypothesis that aging-associated oxidative stress contributes to increasing A, generation and up-regulation of molecular chaperones in Alzheimer's disease. [source] Neuropathology of Alzheimer's DiseaseMOUNT SINAI JOURNAL OF MEDICINE: A JOURNAL OF PERSONALIZED AND TRANSLATIONAL MEDICINE, Issue 1 2010Daniel P. Perl MD Abstract Alois Alzheimer first pointed out that the disease which would later bear his name has a distinct and recognizable neuropathological substrate. Since then, much has been added to our understanding of the pathological lesions associated with the condition. The 2 primary cardinal lesions associated with Alzheimer's disease are the neurofibrillary tangle and the senile plaque. The neurofibrillary tangle consists of abnormal accumulations of abnormally phosphorylated tau within the perikaryal cytoplasm of certain neurons. The senile plaque consists of a central core of beta-amyloid, a 4-kD peptide, surrounded by abnormally configured neuronal processes or neurites. Other neuropathological lesions are encountered in cases of Alzheimer's disease, but the disease is defined and recognized by these 2 cardinal lesions. Other lesions include poorly understood changes such as granulovacuolar degeneration and eosinophilic rodlike bodies (Hirano bodies). The loss of synaptic components is a change that clearly has a significant impact on cognitive function and represents another important morphological alteration. It is important to recognize that distinguishing between Alzheimer's disease, especially in its early stages, and normal aging may be very difficult, particularly if one is examining the brains of patients who died at an advanced old age. It is also noted that instances of pure forms of Alzheimer's disease, in the absence of other coexistent brain disease processes, such as infarctions or Parkinson's disease,related lesions, are relatively uncommon, and this must be taken into account by researchers who employ postmortem brain tissues for research. Mt Sinai J Med 77:32&–42, 2010. © 2010 Mount Sinai School of Medicine [source] Heparan Sulfate Accumulation with A, Deposits in Alzheimer's Disease and Tg2576 Mice is Contributed by Glial CellsBRAIN PATHOLOGY, Issue 4 2008Paul O'Callaghan Abstract Amyloid ,-peptide (A,) plaques, one of the major neuropathological lesions in Alzheimer's disease (AD), can be broadly subdivided into two morphological categories: neuritic and diffuse. Heparan sulfate (HS) and HS proteoglycans (HSPGs) are codeposits of multiple amyloidoses, including AD. Although HS has been considered a limiting factor in the initiation of amyloid deposition, the pathological implications of HS in A, deposits of AD remain unclear. In this study, immunohistochemistry combined with fluorescence and confocal microscopy was employed to gain deeper insight into the accumulation of HS with A, plaques in sporadic and familial AD. Here we demonstrate that HS preferentially accumulated around the A,40 dense cores of neuritic plaques, but was largely absent from diffuse A,42 plaques, suggesting that A,42 deposition may occur independently of HS. A codeposition pattern of HS with A, deposits in Tg2576 mice was also examined. We identified the membrane-bound HSPGs, glypican-1 (GPC1) and syndecan-3 (SDC3), in glial cells associated with A, deposits, proximal to sites of HS accumulation. In mouse primary glial cultures, we observed increased levels of GPC1 and SDC3 following A, stimulation. These results suggest that HS codeposits with A,40 in neuritic plaques and is mainly derived from glial cells. [source] | ||||||||||