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Optimizing drug therapies in cardiac amyloidosis.

Pharmacol Ther

January 2025

Division of Cardiology, University of Louisville Hospital, Louisville, KY, United States of America. Electronic address:

Article Synopsis
  • Cardiac amyloidosis (CA) is a challenging heart condition characterized by the buildup of amyloid proteins, leading to poor outcomes but improvements in diagnosis and treatment options are underway.
  • The article discusses treatment advancements for two main types: transthyretin cardiac amyloidosis (ATTR-CA) and light chain mediated cardiac amyloidosis (AL-CA), highlighting promising therapies for ATTR-CA that target amyloid fibril formation.
  • Current treatment for AL-CA typically involves chemotherapy, and successful management of CA relies on a team of specialists from various medical fields to address patient needs effectively.
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Aims: Cardiac amyloidosis (CA) is associated with various complications, and one of them are thromboembolic events (TEEs), which can significantly impact patients' quality of life. Predicting and managing the risk of these TEEs in patients without atrial fibrillation (AF) pose significant challenges, as many occur independently of AF presence. Several predictors, particularly echocardiographic ones, have been linked to an increased risk, but there is no consensus on stratification or preventive treatment.

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BACKGROUND Amyloidosis refers to an assortment of diseases characterized by the accumulation and deposition of misfolded proteins in the extracellular matrix of tissues and organs. It may present systemically, affecting multiple organs, or locally by affecting a single organ. When the lungs or mediastinal structures are involved, the term pulmonary amyloid is used.

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The presence of circulating human apolipoprotein J reduces the occurrence of cerebral microbleeds in a transgenic mouse model with cerebral amyloid angiopathy.

Alzheimers Res Ther

July 2024

Neurovascular Research Laboratory, Vall d'Hebron Research Institute, Universitat Autònoma de Barcelona, Passeig Vall d'Hebron, 119-129, Mediterranean Building, 1st floor, lab 106, Barcelona, 08035, Spain.

Background: Cerebral amyloid angiopathy (CAA) is characterized by amyloid-β (Aβ) deposition in cerebral vessels, leading to lobar cerebral microbleeds (CMB) and intracerebral hemorrhages (ICH). Apolipoprotein J (ApoJ) is a multifunctional chaperone related to Aβ aggregation and clearance. Our study investigated the vascular impact of chronic recombinant human Apolipoprotein J (rhApoJ) treatment in a transgenic mouse model of β-amyloidosis with prominent CAA.

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Article Synopsis
  • * The cryogenic electron microscopy (cryo-EM) analysis of heart-derived AL amyloid (AL59) revealed a unique double-layered structure with a u-shaped core that challenges previous assumptions about the building blocks of amyloid fibrils.
  • * Additionally, the study found that collagen VI (COLVI) wraps around the amyloid fibrils, forming a protective helical superstructure, indicating a possible new mechanism for the stability and persistence of amyloid deposits in the body.
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