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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Restrictive cardiomyopathy (RCM) is a rare heart muscle disease characterized by impaired ventricular filling due to stiffened ventricular walls, leading to significant diastolic dysfunction.EtiologyRestrictive cardiomyopathy can arise from both inherited and acquired diseases, many of which are systemic. It is categorized into four main types: infiltrative, storage, non-infiltrative, and endomyocardial diseases.Infiltrative diseases, such as amyloidosis, lead to RCM by depositing amyloid...
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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
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Rapid Generation of Amyloid from Native Proteins In vitro
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[Amyloidosis: Up-to-date].

N Magy-Bertrand1

  • 1Service de médecine interne, CHRU de Besançon, 3, boulevard Fleming, 25030 Besançon cedex, France; UFR sciences médicales et pharmaceutiques, université de Franche-Comté, rue Claude-Goudimel, 25000 Besançon, France.

La Revue De Medecine Interne
|February 15, 2016
PubMed
Summary
This summary is machine-generated.

Recent advancements in amyloidosis research have improved disease typing and patient management. New therapies offer hope for increased survival in systemic amyloidosis patients.

Keywords:
Amyloses systémiquesDiagnosisDiagnosticPrognosisPronosticSystemic amyloidosisTraitementTreatment

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Area of Science:

  • Medicine
  • Biochemistry
  • Genetics

Background:

  • Amyloidosis is a systemic protein-folding disease.
  • Significant progress in typing, clinical management, and prognostic markers has been made over the last decade.
  • Novel therapeutic agents are emerging for systemic amyloidosis.

Purpose of the Study:

  • To summarize recent advancements in amyloidosis diagnosis and treatment.
  • To highlight the impact of new molecular techniques and risk-stratification tools.
  • To discuss emerging therapies and their potential to improve patient survival.

Main Methods:

  • Utilizing advanced biological molecular techniques for amyloidosis typing.
  • Employing Cardiac MRI and biomarkers for precise risk-stratification, particularly in AL amyloidosis.
  • Reviewing emerging therapeutic strategies including biotherapies, gene therapy, and immunotherapy.

Main Results:

  • Molecular techniques enable typing of previously unidentified amyloidosis.
  • Cardiac MRI and biomarkers facilitate accurate risk-stratification, guiding chemotherapy adjustments.
  • Emerging treatments show promise for enhancing survival rates.

Conclusions:

  • Systemic amyloidosis management has significantly improved due to advancements in typing and risk-stratification.
  • New therapeutic approaches offer hope for increased patient survival.
  • Continued research into novel treatments is crucial for combating systemic amyloidosis.