The purpose of this study was to evaluate the character and evolution of bone lesions attributable to amyloid deposition in patients on long-term dialysis. Thirty-five patients who were treated with hemodialysis for 5 to 22 years were studied by a review of medical records and hand radiographs. The frequency, distribution, character, and evolution of skeletal cyst-like lesions believed to be secondary to amyloid deposition were evaluated in relation to dialysis duration. The number and size of these lesions increased with dialysis duration, present in 28% of the patients after 5 through 9 years of hemodialysis and in 91% after 15 through 22 years. In contrast, the changes of hyperparathyroidism decreased. Of patients with skeletal wrist lesions, radiographs of symptomatic large joints were available in 15; five had bone abnormalities. Skeletal amyloid deposition was verified pathologically in nine sites (five patients). It is concluded that skeletal lesions believed to be due to amyloid deposition increase with dialysis duration and most commonly affect the wrists. They have a distinctive character, distribution, and evolution and are often associated with carpal tunnel syndrome.
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http://dx.doi.org/10.1097/00124743-199504000-00004 | DOI Listing |
Brain Commun
January 2025
Institute for Stroke and Dementia Research, University Hospital, Ludwig Maximilian University of Munich, Munich 81377, Germany.
Traumatic brain injury is widely viewed as a risk factor for dementia, but the biological mechanisms underlying this association are still unclear. In previous studies, traumatic brain injury has been associated with the hallmark pathologies of Alzheimer's disease, i.e.
View Article and Find Full Text PDFCNS Neurosci Ther
January 2025
State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China.
Background: Alzheimer's disease (AD) is a debilitating neurodegenerative disorder that is difficult to predict and is typically diagnosed only after symptoms manifest. Recently, CD4 T cell-derived double-negative T (DNT) cells have shown strong immuno-regulatory properties in both in vitro and in vivo neuronal inflammation studies. However, the effectiveness of DNT cells in treating on AD are not yet fully understood.
View Article and Find Full Text PDFJ Neurosci
January 2025
Department of Neurobiology and Behavior and Center for the Neurobiology of Learning and Memory, University of California, Irvine, Irvine, California 92697 USA
Cerebral amyloid-beta (Aβ) accumulation, a hallmark pathology of Alzheimer's disease (AD), precedes clinical impairment by two to three decades. However, it is unclear whether Aβ contributes to subtle memory deficits observed during the preclinical stage. The heterogenous emergence of Aβ deposition may selectively impact certain memory domains, which rely on distinct underlying neural circuits.
View Article and Find Full Text PDFJ Neurosci
January 2025
Fujian Provincial Key Laboratory of Neurodegenerative Disease and Aging Research, Institute of Neuroscience, School of Medicine, Xiamen University, Xiamen, Fujian 361102, China
Accumulation of astrocytes around β-amyloid (Aβ) plaques is one of the earliest neuropathological changes in Alzheimer's disease (AD), but the underlying mechanisms and significance remain unclear. Cell adhesion molecule protocadherin-γC5 (Pcdh-γC5) has been reported to implicate in AD. Here we find elevated expression level of Pcdh-γC5 in the brain of 5×FAD mice and Aβ-treated astrocytes, and further reveal that Pcdh-γC5 deficiency leads to exacerbated Aβ deposition in 5×FAD mice.
View Article and Find Full Text PDFJ Mol Biol
January 2025
Department of Biosciences, University of Milan, Italy; Institute of Molecular and Translational Cardiology, IRCCS, Policlinico San Donato, Milan, Italy. Electronic address:
Light chain (AL) amyloidosis is the most common systemic amyloid disease characterized by abnormal accumulation of amyloid fibrils derived from immunoglobulin light chains (LCs). Both full-length (FL) LCs and their isolated variable (VL) and constant (CL) domains contribute to amyloid deposits in multiple organs, with the VL domain predominantly forming the fibril core. However, the role and interplay of these domains in amyloid aggregation and toxicity are poorly understood.
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