An 82-year-old man with suspected systemic amyloidosis and complete atrioventricular block underwent vascular biopsy during his pacemaker implantation with pathology showing amyloid deposits. 99mTc-aprotinin SPECT revealed increased radiotracer uptake along the left ventricular wall, consistent with cardiac amyloidosis. 11C-PiB PET/CT performed for the evaluation of amyloid deposits in the brain showed findings suggestive of Alzheimer disease without abnormal radiotracer concentration in the myocardium to match the 99mTc-aprotinin SPECT findings. Dynamic PET images showed increased 11C-PiB concentration in the left ventricular myocardium at 2 minutes after injection, with subsequent tracer clearance by approximately 5 minutes, consistent with normal 11C-PiB biodistribution.
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http://dx.doi.org/10.1097/RLU.0b013e318251e1d3 | DOI Listing |
J Biochem Mol Toxicol
February 2025
Department of Histology and Embryology, Faculty of Basic Medical Sciences, Hubei University of Medicine, Shiyan, People's Republic of China.
The coexistence of Alzheimer's disease (AD) and chronic pain (CP) in the elderly population has been extensively documented, and a growing body of evidence supports the potential interconnections between these two conditions. This comprehensive review explores the mechanisms by which CP may contribute to the development and progression of AD, with a particular focus on neuroinflammatory pathways and the role of microglia, as well as the activation of the NLR family pyrin domain containing 3 (NLRP3) inflammasome. The review proposes that prolonged pain processing in critical brain regions can dysregulate the activity of the NLRP3 inflammasome within microglia, leading to the overproduction of pro-inflammatory cytokines and excessive oxidative stress in these regions.
View Article and Find Full Text PDFStem Cell Res Ther
January 2025
NHC Key Laboratory of Human Disease Comparative Medicine, Beijing Engineering Research Center for Experimental Animal Models of Human Critical Diseases, International Center for Technology and Innovation of Animal Model, Institute of Laboratory Animal Sciences, Chinese Academy of Medical Sciences (CAMS) & Comparative Medicine Center, Peking Union Medical College (PUMC), Beijing, 100021, China.
Background: Alzheimer's disease (AD) is a progressive neurodegenerative condition affecting around 50 million people worldwide. Bone marrow-derived mesenchymal stem cells (BMMSCs) have emerged as a promising source for cellular therapy due to their ability to differentiate into multiple cell types and their paracrine effects. However, the direct injection of BMMSCs can lead to potential unpredictable impairments, prompting a renewed interest in their paracrine effects for AD treatment.
View Article and Find Full Text PDFMol Neurodegener
January 2025
Department of Neurobiology and Behavior, Charlie Dunlop School of Biological Sciences, University of California, Irvine, CA, 92697-4545, USA.
Background: Apolipoprotein E ε4 (APOE4) is the strongest genetic risk factor for late-onset Alzheimer's disease (LOAD). A recent case report identified a rare variant in APOE, APOE3-R136S (Christchurch), proposed to confer resistance to autosomal dominant Alzheimer's Disease (AD). However, it remains unclear whether and how this variant exerts its protective effects.
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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