A family of maladies known as amyloid disorders, proteinopathy, or amyloidosis, are characterized by the accumulation of abnormal protein aggregates containing cross-β-sheet amyloid fibrils in many organs and tissues. Often, proteins that have been improperly formed or folded make up these fibrils. Nowadays, most treatments for amyloid illness focus on managing symptoms rather than curing or preventing the underlying disease process. However, recent advances in our understanding of the biology of amyloid diseases have led to the development of innovative therapies that target the emergence and accumulation of amyloid fibrils. Examples of these treatments include the use of small compounds, monoclonal antibodies, gene therapy, and others. In the end, even if the majority of therapies for amyloid diseases are symptomatic, greater research into the biology behind these disorders is identifying new targets for potential therapy and paving the way for the development of more effective treatments in the future.
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http://dx.doi.org/10.1016/bs.pmbts.2024.03.008 | DOI Listing |
J Cardiovasc Med (Hagerstown)
February 2025
Center for Diagnosis and Treatment of Cardiomyopathies, Cardiovascular Department, Azienda Sanitaria Universitaria Giuliano-Isontina (ASUGI), University of Trieste.
Diagnosing cardiac amyloidosis (CA) is challenging because of its phenotypic heterogeneity, multiorgan involvement requiring interaction among experts in different specialties and subspecialties, lack of a single noninvasive diagnostic tool, and still limited awareness in the medical community. Missing or delaying the diagnosis of CA may profoundly impact on patients' outcomes, as potentially life-saving treatments may be omitted or delayed. The suspicion of CA should arise when "red flags" for this condition are present, together with increased left ventricular wall thickness.
View Article and Find Full Text PDFJ Cardiovasc Med (Hagerstown)
February 2025
Cardiology Unit, Azienda Ospedaliera Universitaria di Ferrara, Cona, Ferrara, Italy.
Introduction: Cardiac amyloidosis typically causes restrictive cardiomyopathy, in which the impairment of diastolic function is dominant. Echocardiography provides prognostic information through some important parameters: left ventricular ejection fraction (LVEF) and global longitudinal strain (GLS). However, LVEF often remains preserved despite disease progression, and GLS is not routinely performed as it is limited by suboptimal image quality.
View Article and Find Full Text PDFSci Adv
January 2025
Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Distinct tau amyloid assemblies underlie diverse tauopathies but defy rapid classification. Cell and animal experiments indicate tau functions as a prion, as different strains propagated in cells cause unique, transmissible neuropathology after inoculation. Strain amplification requires compatibility of the monomer and amyloid template.
View Article and Find Full Text PDFSci Transl Med
January 2025
Institute for Stroke and Dementia Research (ISD), University Hospital, LMU Munich, 81377 Munich, Germany.
In Alzheimer's disease (AD), amyloid-β (Aβ) triggers the aggregation and spreading of tau pathology, which drives neurodegeneration and cognitive decline. However, the pathophysiological link between Aβ and tau remains unclear, which hinders therapeutic efforts to attenuate Aβ-related tau accumulation. Aβ has been found to trigger neuronal hyperactivity and hyperconnectivity, and preclinical research has shown that tau spreads across connected neurons in an activity-dependent manner.
View Article and Find Full Text PDFDown syndrome, resulting from trisomy of human chromosome 21, is a common form of chromosomal disorder that results in intellectual disability and altered risk of several medical conditions. Individuals with Down syndrome have a greatly increased risk of Alzheimer's disease (DSAD), due to the presence of the APP gene on chromosome 21 that encodes the amyloid-β precursor protein (APP). APP can be processed to generate amyloid-β, which accumulates in plaques in the brains of people who have Alzheimer's disease and is the upstream trigger of disease.
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